MHC peptide complexes and uses thereof in infectious diseases

ABSTRACT

Novel compounds carrying ligands capable of binding to counter receptors on relevant target cells are disclosed. The compounds possess a number of advantageous features, rendering them very suitable for a wide range of applications, including use as detection systems, detection of relevant target cells as well as a number of other methods. In particular, novel MHC complexes comprising one or more MHC molecules are disclosed. The affinity and specificity of the MHC-peptide complexes are surprisingly high. The possibility of presenting to the target cells a plurality of MHC-peptide complexes makes the MHC complexes according to the present invention an extremely powerful tool e.g. in the field of therapy and diagnosis. The invention generally relates to the field of therapy, including therapeutic methods and therapeutic compositions. Also comprised by the present invention is the sample-mounted use of MHC complexes and MHC multimers.

This application claims priority under 35 U.S.C. § 120 as a continuation of U.S. application Ser. No. 12/619,039 filed Nov. 16, 2009, which is a continuation of PCT Application No. PCT/DK2008/000118 filed Mar. 26, 2008, which claims priority to the following Danish Patent applications Nos.—PA 2007 00461, filed Mar. 26, 2007, PA 2007 00973, filed Jul. 3, 2007, PA 2007 00975, filed Jul. 3, 2007, PA 2007 00972, filed Jul. 3, 2007, and PA 2007 00974, filed Jul. 3, 2007 and also claims priority to the following U.S. Provisional Patent Application Nos.—U.S. 60/907,217 filed Mar. 26, 2007, U.S. 60/929,583, filed Jul. 3, 2007, U.S. 60/929,581, filed Jul. 3, 2007, U.S. 60/929,582, filed Jul. 3, 2007, and U.S. 60/929,586, Jul. 3, 2007, the contents of each of which are hereby incorporated by reference.

All patent and non-patent references cited in U.S. 60/907,217 as well as in this application are hereby incorporated by reference in their entirety. U.S. 60/907,217 is hereby also incorporated herein by reference in its entirety.

FIELD OF INVENTION

The present invention relates to MHC-peptide complexes and uses thereof in the treatment of a disease in an individual.

BACKGROUND OF THE INVENTION

Biochemical interactions between peptide epitope specific membrane molecules encoded by the Major Histocompatibility Complex (MHC, in humans HLA) and T-cell receptors (TCR) are required to elicit specific immune responses. This requires activation of T-cells by presentation to the T-cells of peptides against which a T-cell response should be raised. The peptides are presented to the T-cells by the MHC complexes.

The Immune Response

The immune response is divided into two parts termed the innate immune response and the adaptive immune response. Both responses work together to eliminate pathogens (antigens). Innate immunity is present at all times and is the first line of defense against invading pathogens. The immediate response by means of pre-existing elements, i.e. various proteins and phagocytic cells that recognize conserved features on the pathogens, is important in clearing and control of spreading of pathogens. If a pathogen is persistent in the body and thus only partially cleared by the actions of the innate immune system, the adaptive immune system initiate a response against the pathogen. The adaptive immune system is capable of eliciting a response against virtually any type of pathogen and is unlike the innate immune system capable of establishing immunological memory.

The adaptive response is highly specific to the particular pathogen that activated it but it is not so quickly launched as the innate when first encountering a pathogen. However, due to the generation of memory cells, a fast and more efficient response is generated upon repeated exposure to the same pathogen. The adaptive response is carried out by two distinct sets of lymphocytes, the B cells producing antibodies leading to the humoral or antibody mediated immune response, and the T cells leading to the cell mediated immune response.

T cells express a clonotypic T cell receptor (TCR) on the surface. This receptor enable the T cell to recognize peptide antigens bound to major histocompatibility complex (MHC) molecules, called human leukocyte antigens (HLA) in man. Depending on the type of pathogen, being intracellular or extracellular, the antigenic peptides are bound to MHC class I or MHC class II, respectively. The two classes of MHC complexes are recognized by different subsets of T cells; Cytotoxic CD8+ T cells recognizing MHC class I and CD4+ helper cells recognizing MHC class II. In general, TCR recognition of MHC-peptide complexes result in T cell activation, clonal expansion and differentiation of the T cells into effector, memory and regulatory T cells.

B cells express a membrane bound form of immunoglobulin (Ig) called the B cell receptor (BCR). The BCR recognizes an epitope that is part of an intact three dimensional antigenic molecule. Upon BCR recognition of an antigen the BCR:antigen complex is internalized and fragments from the internalized antigen is presented in the context of MHC class II on the surface of the B cell to CD4+ helper T-cells (Th). The specific Th cell will then activate the B cell leading to differentiation into an antibody producing plasma cell.

A very important feature of the adaptive immune system is its ability to distinguish between self and non-self antigens, and preferably respond against non-self. If the immune system fails to discriminate between the two, specific immune responses against self-antigens are generated. These autoimmune reactions can lead to damage of self-tissue.

The adaptive immune response is initiated when antigens are taken up by professional antigen presenting cells such as dendritic cells, Macrophages, Langerhans cells and B-cells. These cells present peptide fragments, resulting from the degradation of proteins, in the context of MHC class II proteins (Major Histocompatibility Complex) to helper T cells. The T helper cells then mediate help to B-cells and antigen specific cytotoxic T cells, both of which have received primary activation signals via their BCR respective TCR. The help from the Th-cell is mediated by means of soluble mediators e.g. cytokines.

In general the interactions between the various cells of the cellular immune response is governed by receptor-ligand interactions directly between the cells and by production of various soluble reporter substances e.g. cytokines by activated cells.

MHC-Peptide Complexes.

MHC complexes function as antigenic peptide receptors, collecting peptides inside the cell and transporting them to the cell surface, where the MHC-peptide complex can be recognized by T-lymphocytes. Two classes of classical MHC complexes exist, MHC class I and II. The most important difference between these two molecules lies in the protein source from which they obtain their associated peptides. MHC class I molecules present peptides derived from endogenous antigens degraded in the cytosol and are thus able to display fragments of viral proteins and unique proteins derived from cancerous cells. Almost all nucleated cells express MHC class I on their surface even though the expression level varies among different cell types. MHC class II molecules bind peptides derived from exogenous antigens. Exogenous proteins enter the cells by endocytosis or phagocytosis, and these proteins are degraded by proteases in acidified intracellular vesicles before presentation by MHC class II molecules. MHC class II molecules are only expressed on professional antigen presenting cells like B cells and macrophages.

The three-dimensional structure of MHC class I and II molecules are very similar but important differences exist. MHC class I molecules consist of two polypeptide chains, a heavy chain, α, spanning the membrane and a light chain, β2-microglobulin (β2m). The heavy chain is encoded in the gene complex termed the major histocompatibility complex (MHC), and its extracellular portion comprises three domains, α1, α2 and α3. The β2m chain is not encoded in the MHC gene and consists of a single domain, which together with the α3 domain of the heavy chain make up a folded structure that closely resembles that of the immunoglobulin. The α1 and α2 domains pair to form the peptide binding cleft, consisting of two segmented α helices lying on a sheet of eight β-strands. In humans as well as in mice three different types of MHC class I molecule exist. HLA-A, B, C are found in humans while MHC class I molecules in mice are designated H-2K, H-2D and H-2L.

The MHC class II molecule is composed of two membrane spanning polypeptide chains, α and β, of similar size (about 30000 Da). Genes located in the major histocompatibility complex encode both chains. Each chain consists of two domains, where α1 and β1 forms a 9-pocket peptide-binding cleft, where pocket 1, 4, 6 and 9 are considered as major peptide binding pockets. The α2 and β2, like the α2 and β2m in the MHC class I molecules, have amino acid sequence and structural similarities to immunoglobulin constant domains. In contrast to MHC class I complexes, where the ends of the antigenic peptide is buried, peptide-ends in MHC class II complexes are not. HLA-DR, DQ and DP are the human class II molecules, H-2A, M and E are those of the mice.

A remarkable feature of MHC genes is their polymorphism accomplished by multiple alleles at each gene. The polygenic and polymorphic nature of MHC genes is reflected in the peptide-binding cleft so that different MHC complexes bind different sets of peptides. The variable amino acids in the peptide binding cleft form pockets where the amino acid side chains of the bound peptide can be buried. This permits a specific variant of MHC to bind some peptides better than others.

MHC Multimers

Due to the short half-life of the peptide-MHC-T cell receptor ternary complex (typically between 10 and 25 seconds) it is difficult to label specific T cells with labelled MHC-peptide complexes, and like-wise, it is difficult to employ such monomers of MHC-peptide for therapeutic and vaccine purposes because of their weak binding. In order to circumvent this problem, MHC multimers have been developed. These are complexes that include multiple copies of MHC-peptide complexes, providing these complexes with an increased affinity and half-life of interaction, compared to that of the monomer MHC-peptide complex. The multiple copies of MHC-peptide complexes are attached, covalently or non-covalently, to a multimerization domain. Known examples of such MHC multimers include the following:

-   -   MHC-dimers: Each MHC dimer contains two copies of MHC-peptide.         IgG is used as multimerization domain, and one of the domains of         the MHC protein is covalently linked to IgG.     -   MHC-tetramers: Each MHC-tetramer contains four copies of         MHC-peptide, each of which is biotinylated. The MHC complexes         are held together in a complex by the streptavidin tetramer         protein, providing a non-covalent linkage between a streptavidin         monomer and the MHC protein. Tetramers are described in U.S.         Pat. No. 5,635,363.     -   MHC pentamers: Five copies of MHC-peptide complexes are         multimerised by a self-assembling coiled-coil domain, to form a         MHC pentamer. MHC pentamers are described in the US patent         2004209295     -   MHC dextramers: A large number of MHC-peptide complexes,         typically more than ten, are attached to a dextran polymer.         MHC-dextramers are described in the patent application WO         02/072631 A2.     -   MHC streptamers: 8-12 MHC-peptide complexes attached to         Streptactin. MHC streptamers are described in Knabel M et al.         Reversible MHC multimer staining for functional isolation of         T-cell populations and effective adoptive transfer. Nature         medicine 6. 631-637 (2002).         Use of MHC Multimers in Flow Cytometry and Related Techniques

The concentration of antigen specific T-cells in samples from e.g. peripheral blood can be very low. Flow cytometry and related methods offer the ability to analyze a large number of cells and simultaneously identify the few of interest. MHC multimers have turned out to be very valuable reagents for detection and characterization of antigen specific T-cells in flow cytometer experiments. The relative amount of antigen specific T cells in a sample can be determined and also the affinity of the binding of MHC multimer to the T-cell receptor can be determined.

The basic function of a flow cytometer is its ability to analyse and identify fluorochrome labelled entities in a liquid sample, by means of its excitation, using a light source such as a laser beam and the light emission from the bound fluorochrome.

MHC multimers is used as detections molecule for identification of antigen specific T-cells in flow cytometry, by labelling the MHC multimer with a specific fluorochrome, which is detectable, by the flow cytometer used.

In order to facilitate the identification of a small amount of cells, the cells can be sub-categorized using antibodies or other fluorochrome labelled detections molecules directed against surface markers other than the TCR on the specific T-cells population. Antibodies or other fluorochrome labelled detections molecules can also be used to identify cells known not to be antigen specific T-cells. Both kinds of detections molecules are in the following referred to as gating reagents. Gating reagents, helps identify the “true” antigen specific T cells bound by MHC multimers by identifying specific subpopulations in a sample, e.g. T cells and by excluding cells that for some reason bind MHC multimers without being antigen specific T-cells. Other cytometry methods, e.g. fluorescence microscopy and IHC can like flow cytometry be employed in identification of antigen specific T cells in a cell sample using MHC multimers.

Application of MHC Multimers in Immune Monitoring, Diagnostics, Prognostics, Therapy and Vaccines

T cells are pivotal for mounting an adaptive immune response. It is therefore of importance to be able to measure the number of specific T cells when performing a monitoring of a given immune response, for example in connection with vaccine development, autologous cancer therapy, transplantation, infectious diseases, toxicity studies etc.

Accordingly, the present invention further provides powerful tools in the fields of vaccines, therapy and diagnosis. One objective of the present invention is to provide methods for anti-tumour and anti-virus immunotherapy by generating antigen-specific T-cells capable of inactivating or eliminating undesirable target cells. Another objective is to isolate antigen-specific T-cells and culture these in the presence of co-stimulatory molecules. Ex vivo priming and expansion of T-cell populations allows the T-cells to be used in immunotherapy of various types of cancer and infectious diseases. A third objective of the present invention is to identify and label specific subsets of cells with relevance for the development or treatment of diseases.

SUMMARY OF THE INVENTION

Measurement of antigen specific T cells during an immune response are important parameters in vaccine development, autologous cancer therapy, transplantation, infectious diseases, inflammation, autoimmunity, toxicity studies etc. MHC multimers are crucial reagents in monitoring of antigen specific T cells. The present invention describes novel methods to generate MHC multimers and methods to improve existing and new MHC multimers. The invention also describes improved methods for the use of MHC multimers in analysis of T cells in samples including diagnostic and prognostic methods. Furthermore the use of MHC multimers in therapy are described, e.g. anti-tumour and anti-virus therapy, including isolation of antigen specific T cells capable of inactivation or elimination of undesirable target cells or isolation of specific T cells capable of regulation of other immune cells.

The present invention in one aspect refers to a MHC monomer comprising a-b-P, or a MHC multimer comprising (a-b-P)_(n), wherein n>1,

wherein a and b together form a functional MHC protein capable of binding the peptide P,

wherein (a-b-P) is the MHC-peptide complex formed when the peptide P binds to the functional MHC protein, and

wherein each MHC peptide complex of a MHC multimer is associated with one or more multimerization domains.

MHC monomers and MHC multimers comprising one or more MHC peptide complexes of class 1 or class 2 MHC are covered by the present invention. Accordingly, the peptide P can have a length of e.g. 8, 9, 10, 11, 12, 13, 14, 15, 16, 16-20, or 20-30 amino acid residues.

Examples of the peptide P is provided herein below. In one embodiment, the peptide P can be selected from the group consisting of sequences disclosed in the electronically enclosed “Sequence Listing” and annotated consecutively (using integers) starting with SEQ ID NO:1 and ending with SEQ ID NO:52252.

In another aspect the present invention is directed to a composition comprising a plurality of MHC monomers and/or MHC multimers according to the present invention, wherein the MHC multimers are identical or different, and a carrier.

In yet another aspect there is provided a kit comprising a MHC monomer or a MHC multimer according to the present invention, or a composition according to the present invention, and at least one additional component, such as a positive control and/or instructions for use.

In a still further aspect there is provided a method for immune monitoring one or more diseases comprising monitoring of antigen specific T cells, said method comprising the steps of

-   -   i) providing the MHC monomer or MHC multimer or individual         components thereof according to the present invention, or the         individual components thereof,     -   ii) providing a population of antigen specific T cells or         individual antigen specific T cells, and     -   iii) measuring the number, activity or state and/or presence of         antigen specific of T cells specific for the peptide P of the         said MHC monomer or MHC multimer, thereby immune monitoring said         one or more diseases.

In yet another aspect there is provided a method for diagnosing one or more diseases comprising immune monitoring of antigen specific T cells, said method comprising the following steps: of

-   -   i) providing the MHC monomer or MHC multimer or individual         components thereof according to the present invention, or         individual components thereof,     -   ii) providing a population of antigen specific T cells or         individual antigen specific T cells, and     -   iii) measuring the number, activity or state and/or presence of         T cells specific for said MHC monomer or the peptide P of the         MHC multimer, thereby diagnosing said one or more diseases.

There is also provided a method for isolation of one or more antigen specific T cells, said method comprising the steps of

-   -   i) providing the MHC monomer or MHC multimer or individual         components thereof according to the present invention, or         individual components thereof, and     -   ii) providing a population of antigen specific T cells or         individual antigen specific T cells, and     -   iii) thereby isolating said T cells specific for the peptide P         of the said MHC monomer or MHC multimer.

The present invention makes it possible to pursue different immune monitoring methods using the MHC monomers and MHC multimers according to the present invention. The immune monitoring methods include e.g. flow cytometry, ELISPOT, LDA, Quantaferon and Quantaferon-like methods. Using the above-cited methods, the MHC monomers and/or the MHC multimers can be provided as a MHC peptide complex, or the peptide and the MHC monomer and/or multimer can be provided separately.

Accordingly, recognition of TCR's can be achieved by direct or indirect detection, e.g. by using one or more of the following methods:

ELISPOT technique using indirect detection, e.g. by adding the antigenic peptide optionally associated with a MHC monomer or MHC multimer, followed by measurement of INF-gamma secretion from a population of cells or from individual cells.

Another technique involves a Quantaferon-like detection assays, e.g. by using indirect detection, e.g. by adding the antigenic peptide optionally associated with a MHC monomer or MHC multimer, followed by measurement of INF-gamma secretion from a population of cells or from individual cells.

Flow cytometry offers another alternative for performing detection assays, e.g. by using direct detection (e.g. of MHC tetramers), e.g. by adding the antigenic peptide optionally associated with a MHC monomer or MHC multimer, followed by detection of a fluorescein label, thereby measuring the number of TCRs on specific T-cells.

Flow cytometry can also be used for indirect detection, e.g. by adding the antigenic peptide optionally associated with a MHC monomer or MHC multimer, followed by addition of a “cell-permeabilizing factor”, and subsequent measurement of an intracellular component (e.g. INF-gamma mRNA), from individual cells or populations of cells.

By using the above-mentioned and other techniques, one can diagnose and/or monitor e.g. infectious diseases caused e.g. by mycobacetrium, Gram positive bacteria, Gram negative bacteria, Spirochetes, intracellular bacterium, extracelular bacterium, Borrelia, TB, CMV, HPV, Hepatitis, BK, fungal organisms and microorganisms. The diagnosis and/or monitoring of a particular disease can greatly aid in directing an optimal treatment of said disease in an individual. Cancer diagnostic methods and/or cancer monitoring methods also fall within the scope of the present invention.

In still further aspects of the present invention there is provided a method for performing a vaccination of an individual in need thereof, said method comprising the steps of

-   -   providing a MHC monomer or a MHC multimer according to the         present invention, or the individual components thereof, and     -   administering said MHC monomer or MHC multimer to said         individual and obtaining a protective immune response, thereby         performing a vaccination of the said individual.

In yet another embodiment there is provided a method for performing therapeutic treatment of an individual comprising the steps of

-   -   Providing the MHC multimer according to the present invention,         or individual components thereof, and     -   Isolating or obtaining T-cells from a source, such as an         individual or an ex-vivo library or cell bank, wherein said         isolated or obtained T-cells are specific for said provided MHC         multimer,     -   Optionally manipulating said T-cells, and     -   Introducing said isolated or obtained T-cells into an individual         to be subjected to a therapeutic treatment, wherein the         individual can be the same individual or a different individual         from the source individual.

There is also provided in accordance with the present invention a method for immune monitoring one or more cancer diseases comprising the step of monitoring one or more cancer antigen specific T-cells, said method comprising the steps of

-   -   providing a MHC monomer or MHC multimer, or individual         components thereof, as described herein,     -   providing a population of cancer antigen specific T cells, or         individual cancer antigen specific T cells, and     -   measuring the number and/or presence of cancer antigen specific         T cells specific for the peptide P of the MHC monomer or MHC         multimer, thereby immune monitoring said one or more cancer         diseases.

In a still further aspect there is provided a method for diagnosing one or more cancer diseases in an individual, said method comprising the step of performing an immune monitoration of one or more cancer antigen specific T cell(s), said method comprising the further steps of

-   -   providing the MHC multimer or individual components thereof         according to the present invention,     -   providing a population of cancer antigen specific T cells, or         individual cancer antigen specific T cells, and     -   measuring the number and/or presence of T cells specific for the         peptide P of the MHC monomer or MHC multimer, thereby diagnosing         said one or more cancer diseases.

In yet another aspect of the present invention there is provided a method for performing a cancer vaccination of an individual in need thereof, said method comprising the steps of

-   -   providing a MHC monomer or MHC multimer according to any of the         present invention, and     -   administering said MHC monomer or said MHC multimer to said         individual, thereby performing a cancer vaccination of the said         individual.

In a still further aspect of the present invention there is provided a method for performing a cancer therapeutic treatment of an individual comprising the steps of

-   -   Providing the MHC multimer according to the present invention,         and     -   Isolation of T cells specific for said MHC multimer, and     -   Optionally manipulation of said T cell and     -   Introduction of said T cells into the same or a different         individual to obtain a cancer therapeutic treatment.

There is also provided a method comprising one or more steps for minimizing undesired binding of the MHC multimer according to the present invention. This method is disclosed herein below in more detail.

In further aspects the present invention provides:

A method for performing a control experiment comprising the step of counting of particles comprising the MHC multimer according to the present invention.

A method for performing a control experiment comprising the step of sorting of particles comprising the MHC multimer according to the present invention.

A method for performing a control experiment comprising the step of performing flow cytometry analysis of particles comprising the MHC multimer according to the present invention.

A method for performing a control experiment comprising the step of performing a immunohistochemistry analysis comprising the MHC multimer according to the present invention.

A method for performing a control experiment comprising the step of performing a immunocytochemistry analysis comprising the MHC multimer according to the present invention.

A method for performing a control experiment comprising the step of performing an ELISA analysis comprising the MHC multimer according to the present invention.

In a still further aspect of the present invention there is provided a method for generating MHC multimers according to the present invention, said method comprising the steps of

-   -   i) providing one or more peptides P; and/or     -   ii) providing one or more functional MHC proteins,     -   iii) optionally providing one or more multimerization domains,         and     -   iv) contacting the one or more peptides P and the one or more         functional MHC proteins and the one or more multimerization         domains simultaneously or sequentially in any order, thereby         obtaining MHC multimers according to the present invention.

The method can also be performed by initially providing one or more antigenic peptide(s) P and one or more functional MHC proteins to generate a MHC-peptide complex (a-b-P); subsequently providing one or more multimerisation domain(s); and reacting the one or more MHC-peptide complexes and the one or more multimerization domain(s) to generate a MHC multimer according to the present invention.

Definitions

As used everywhere herein, the term “a”, “an” or “the” is meant to be one or more, i.e. at least one.

Adjuvant: adjuvants are drugs that have few or no pharmacological effects by themselves, but can increase the efficacy or potency of other drugs when given at the same time. In another embodiment, an adjuvant is an agent which, while not having any specific antigenic effect in itself, can stimulate the immune system, increasing the response to a vaccine.

Agonist: agonist as used herein is a substance that binds to a specific receptor and triggers a response in the cell. It mimics the action of an endogenous ligand that binds to the same receptor.

Antagonist: antagonist as used herein is a substance that binds to a specific receptor and blocks the response in the cell. It blocks the action of an endogenous ligand that binds to the same receptor.

Antibodies: As used herein, the term “antibody” means an isolated or recombinant binding agent that comprises the necessary variable region sequences to specifically bind an antigenic epitope. Therefore, an antibody is any form of antibody or fragment thereof that exhibits the desired biological activity, e.g., binding the specific target antigen. Antibodies can derive from multiple species. For example, antibodies include rodent (such as mouse and rat), rabbit, sheep, camel, and human antibodies. Antibodies can also include chimeric antibodies, which join variable regions from one species to constant regions from another species. Likewise, antibodies can be humanized, that is constructed by recombinant DNA technology to produce immunoglobulins which have human framework regions from one species combined with complementarity determining regions (CDR's) from a another species' immunoglobulin. The antibody can be monoclonal or polyclonal.

Antibodies can be divided into isotypes (IgA, IgG, IgM, IgD, IgE, IgG1, IgG2, IgG3, IgG4, IgA1, IgA2, IgM1, IgM2)

Antibodies: In another embodiment the term “antibody” refers to an intact antibody, or a fragment of an antibody that competes with the intact antibody for antigen binding. In certain embodiments, antibody fragments are produced by recombinant DNA techniques. In certain embodiments, antibody fragments are produced by enzymatic or chemical cleavage of intact antibodies. Exemplary antibody fragments include, but are not limited to, Fab, Fab′, F(ab′)2, Fv, and scFv. Exemplary antibody fragments also include, but are not limited to, domain antibodies, nanobodies, minibodies ((scFv-C.sub.H3).sub.2), maxibodies ((scFv-C.sub.H2-C.sub.H3).sub.2), diabodies (noncovalent dimer of scFv).

Antigen presenting cell: An antigen-presenting cell (APC) as used herein is a cell that displays foreign antigen complexed with MHC on its surface.

Antigenic peptide: Any peptide molecule that is bound or able to bind into the binding groove of either MHC class 1 or MHC class 2.

Aptamer: the term aptamer as used herein is defined as oligonucleic acid or peptide molecules that bind a specific target molecule. Aptamers are usually created by selecting them from a large random sequence pool, but natural aptamers also exist. Aptamers can be divided into DNA amtamers, RNA aptamers and peptide aptamers.

Avidin: Avidin as used herein is a glycoprotein found in the egg white and tissues of birds, reptiles and amphibians. It contains four identical subunits having a combined mass of 67,000-68,000 daltons. Each subunit consists of 128 amino acids and binds one molecule of biotin.

Biologically active molecule: A biologically active molecule is a molecule having itself a biological activity/effect or is able to induce a biological activity/effect when administered to a biological system. Biologically active molecules include adjuvants, immune targets (e.g. antigens), enzymes, regulators of receptor activity, receptor ligands, immune potentiators, drugs, toxins, cytotoxic molecules, co-receptors, proteins and peptides in general, sugar moieties, lipid groups, nucleic acids including siRNA, nanoparticles, small molecules.

Bioluminescent: Bioluminescence, as used herein, is the production and emission of light by a living organism as the result of a chemical reaction during which chemical energy is converted to light energy.

Biotin: Biotin, as used herein, is also known as vitamin H or B₇. Niotin has the chemical formula C₁₀H₁₆N₂O₃S.

Bispecific antibodies: The term bispecific antibodies as used herein is defined as monoclonal, preferably but not limited to human or humanized, antibodies that have binding specificities for at least two different antigens. The antibody can also be trispecific or multispecific.

Carrier: A carrier as used herein can be any type of molecule that is directly or indirectly associated with the MHC peptide complex. In this invention, a carrier will typically refer to a functionalized polymer (e.g. dextran) that is capable of reacting with MHC-peptide complexes, thus covalently attaching the MHC-peptide complex to the carrier, or that is capable of reacting with scaffold molecules (e.g. streptavidin), thus covalently attaching streptavidin to the carrier; the streptavidin then may bind MHC-peptide complexes. Carrier and scaffold are used interchangeably herein where scaffold typically refers to smaller molecules of a multimerization domain and carrier typically refers to larger molecule and/or cell like structures.

Chelating chemical compound: Chelating chemical compound, as used herein, is the process of reversible binding of a ligand to a metal ion, forming a metal complex.

Chemiluminescent: Chemiluminescence, as used herein, is the emission of light (luminescence) without emission of heat as the result of a chemical reaction.

Chromophore: A chromophore, as used herein, is the part of a visibly coloured molecule responsible for light absorption over a range of wavelengths thus giving rise to the colour. By extension the term can be applied to uv or it absorbing parts of molecules.

Coiled-coil polypeptide: the term coiled-coil polypeptide as used herein is a structural motif in proteins, in which 2-7 alpha-helices are coiled together like the strands of a rope

Covalent binding: The term covalent binding is used herein to describe a form of chemical bonding that is characterized by the sharing of pairs of electrons between atoms. Attraction-to-repulsion stability that forms between atoms when they share electrons is known as covalent bonding.

Crosslinking is the process of chemically joining two or more molecules by a covalent bond. Crosslinking reagents contain reactive ends to specific functional groups (primary amines, sulfhydryls, etc.) on proteins or other molecules.

Diagnosis: The act or process of identifying or determining the nature and cause of a disease or injury through evaluation

Diabodies: The term “diabodies” refers to small antibody fragments with two antigen-binding sites, which fragments comprise a heavy-chain variable domain (VH) connected to a light-chain variable domain (VL) in the same polypeptide chain (VH-VL). By using a linker that is too short to allow pairing between the two domains on the same chain, the domains are forced to pair with the complementary domains of another chain and create two antigen-binding sites.

Dendritic cell: The term dendritic cell as used herein is a type of immune cells. Their main function is to process antigen material and present it on the surface to other cells of the immune system, thus functioning as antigen-presenting cells.

Detection: In this invention detection means any method capable of measuring one molecule bound to another molecule. The molecules are typically proteins but can be any type of molecule

Dextran: the term dextran as used herein is a complex, branched polysaccharide made of many glucose molecules joined into chains of varying lengths. The straight chain consists of α1→6 glycosidic linkages between glucose molecules, while branches begin from α1→3 linkages (and in some cases, α1→2 and α1→4 linkages as well).

Direct detection of T cells: Direct detection of T cells is used herein interchangeably with direct detection of TCR and direct detection of T cell receptor. As used herein direct detection of T cells is detection directly of the binding interaction between a specific T cell receptor and a MHC multimer.

DNA: The term DNA (Deoxyribonucleic acid) duplex as used herein is a polymer of simple units called nucleotides, with a backbone made of sugars and phosphate atoms joined by ester bonds. Attached to each sugar is one of four types of molecules called bases.

DNA duplex: In living organisms, DNA does not usually exist as a single molecule, but instead as a tightly-associated pair of molecules. These two long strands entwine like vines, in the shape of a double helix.

Electrophilic: electrophile, as used herein, is a reagent attracted to electrons that participates in a chemical reaction by accepting an electron pair in order to bond to a nucleophile.

Enzyme label: enzyme labelling, as used herein, involves a detection method comprising a reaction catalysed by an enzyme.

Epitope-focused antibody: Antibodies also include epitope-focused antibodies, which have at least one minimal essential binding specificity determinant from a heavy chain or light chain CDR3 from a reference antibody, methods for making such epitope-focused antibodies are described in U.S. patent application Ser. No. 11/040,159, which is incorporated herein by reference in its entirety.

Flow cytometry: The analysis of single cells using a flow cytometer.

Flow cytometer: Instrument that measures cell size, granularity and fluorescence due to bound fluorescent marker molecules as single cells pass in a stream past photodectors. A flow cytometer carry out the measurements and/or sorting of individual cells.

Fluorescent: the term fluorescent as used herein is to have the ability to emit light of a certain wavelength when activated by light of another wavelength.

Fluorochromes: fluorochrome, as used herein, is any fluorescent compound used as a dye to mark e.g. protein with a fluorescent label.

Fluorophore: A fluorophore, as used herein, is a component of a molecule which causes a molecule to be fluorescent.

Folding: In this invention folding means in vitro or in vivo folding of proteins in a tertiary structure.

Fusion antibody: As used herein, the term “fusion antibody” refers to a molecule in which an antibody is fused to a non-antibody polypeptide at the N- or C-terminus of the antibody polypeptide.

Glycosylated: Glycosylation, as used herein, is the process or result of addition of saccharides to proteins and lipids.

Hapten: A residue on a molecule for which there is a specific molecule that can bind, e.g. an antibody.

Heteroconjugate antibodies are composed of two covalently joined antibodies. Such antibodies have, for example, been proposed to target immune system cells to unwanted cells.

IgG: IgG as used herein is a monomeric immunoglobulin, built of two heavy chains and two light chains. Each molecule has two antigen binding sites.

Isolated antibody: The term “isolated” antibody as used herein is an antibody which has been identified and separated and/or recovered from a component of its natural environment.

Immunoconjugates: The invention also pertains to immunoconjugates comprising an antibody conjugated to a cytotoxic agent such as a chemotherapeutic agent, toxin (e.g., an enzymatically active toxin of bacterial, fungal, plant, or animal origin, or fragments thereof), or a radioactive isotope (i.e., a radioconjugate) Enzymatically active toxins and fragments thereof that can be used include diphtheria A chain, nonbinding active fragments of diphtheria toxin, exotoxin A chain (from Pseudomonas aeruginosa), ricin A chain, abrin A chain, modeccin A chain, alpha-sarcin, Aleurites fordii proteins, dianthin proteins, Phytolaca americana proteins (PAPI, PAPII, and PAP-S), momordica charantia inhibitor, curcin, crotin, sapaonaria officinalis inhibitor, gelonin, mitogellin, restrictocin, phenomycin, enomycin, and the tricothecenes. A variety of radionuclides are available for the production of radioconjugated antibodies. Conjugates of the antibody and cytotoxic agent are made using a variety of bifunctional protein-coupling agents such as N-succinimidyl-3-(2-pyridyldithiol) propionate (SPDP), iminothiolane (IT), bifunctional derivatives of imidoesters (such as dimethyl adipimidate HCL), active esters (such as disuccinimidyl suberate), aldehydes (such as glutaraldehyde), bis-azido compounds (such as bis(p-azidobenzoyl)hexanediamine), bis-diazonium derivatives (such as bis-(p-diazoniumbenzoyl)-ethylenediamine), diisocyanates (such as tolyene 2,6-diisocyanate), and bis-active fluorine compounds (such as 1,5-difluoro-2,4-dinitrobenzene).

Immune monitoring: Immune monitoring of the present invention refers to testing of immune status in the diagnosis and therapy of diseases like but not limited to cancer, immunoproliferative and immunodeficiency disorders, autoimmune abnormalities, and infectious disease. It also refers to testing of immune status before, during and after vaccination and transplantation procedures.

Immune monitoring process: a series of one or more immune monitoring analysis

Indirect detection of T cells: Indirect detection of T cells is used interchangeably herein with Indirect detection of TCR and indirect detection of T cell receptor. As used herein indirect detection of T cells is detection of the binding interaction between a specific T cell receptor and a MHC multimer by measurement of the effect of the binding interaction.

Ionophore: ionophore, as used herein, is a lipid-soluble molecule usually synthesized by microorganisms capable of transporting ions.

Label: Label herein is used interchangeable with labeling molecule. Label as described herein is an identifiable substance that is detectable in an assay and that can be attached to a molecule creating a labeled molecule. The behavior of the labeled molecule can then be studied.

Labelling: Labelling herein means attachment of a label to a molecule.

Lanthanide: lanthanide, as used herein, series comprises the 15 elements with atomic numbers 57 through 71, from lanthanum to lutetium.

Linker molecule: Linker molecule and linker is used interchangeable herein. A linker molecule is a molecule that covalently or non-covalently connects two or more molecules, thereby creating a larger complex consisting of all molecules including the linker molecule.

Liposomes: The term liposomes as used herein is defined as a spherical vesicle with a membrane composed of a phospholipid and cholesterol bilayer. Liposomes, usually but not by definition, contain a core of aqueous solution; lipid spheres that contain no aqueous material are called micelles.

Immunoliposomes: The antibodies disclosed herein can also be formulated as immunoliposomes. Liposomes comprising the antibody are prepared by methods known in the art, such as described in Epstein et al., Proc. Natl. Acad. Sci. USA 82: 3688 (1985); Hwang et al., Proc. Natl. Acad. Sci. USA 77: 4030 (1980); and U.S. Pat. Nos. 4,485,045 and 4,544,545. Particularly useful liposomes can be generated by the reverse-phase evaporation method with a lipid composition comprising phosphatidylcholine, cholesterol, and PEG-derivatized phosphatidylethanolamine (PEG-PE).

Marker: Marker is used interchangeably with marker molecule herein. A marker is molecule that specifically associates covalently or non-covalently with a molecule belonging to or associated with an entity.

MHC: Denotes the major histocompatibility complex.

A “MHC Class I molecule” as used everywhere herein is defined as a molecule which comprises 1-3 subunits, including a heavy chain, a heavy chain combined with a light chain (beta₂m), a heavy chain combined with a light chain (beta₂m) through a flexible linker, a heavy chain combined with a peptide, a heavy chain combined with a peptide through a flexible linker, a heavy chain/beta₂m dimer combined with a peptide, and a heavy chain/beta₂m dimer with a peptide through a flexible linker to the heavy or light chain. The MHC molecule chain can be changed by substitution of single or by cohorts of native amino acids or by inserts, or deletions to enhance or impair the functions attributed to said molecule. By example, it has been shown that substitution of XX with YY in position nn of human beta₂m enhance the biochemical stability of MHC Class I molecule complexes and thus can lead to more efficient antigen presentation of subdominant peptide epitopes.

MHC complex: MHC complex is herein used interchangeably with MHC-peptide complex, unless it is specified that the MHC complex is empty, i.e. is not complexed with peptide.

MHC Class I like molecules (including non-classical MHC Class I molecules) include CD1d, HLA E, HLA G, HLA F, HLA H, MIC A, MIC B, ULBP-1, ULBP-2, and ULBP-3.

A “MHC Class II molecule” as used everywhere herein is defined as a molecule which comprises 2-3 subunits including an alpha-chain and a beta-chain (alpha/beta-dimer), an alpha/beta dimer with a peptide, and an alpha/beta dimer combined with a peptide through a flexible linker to the alpha or beta chain, an alpha/beta dimer combined through an interaction by affinity tags e.g. jun-fos, an alpha/beta dimer combined through an interaction by affinity tags e.g. jun-fos and further combined with a peptide through a flexible linker to the alpha or beta chain. The MHC molecule chains can be changed by substitution of single or by cohorts of native amino acids or by inserts, or deletions to enhance or impair the functions attributed to said molecule. Under circumstances where the alpha-chain and beta-chain have been fused, to form one subunit, the “MHC Class II molecule” can comprise only 1 subunit.

MHC Class II like molecules (including non-classical MHC Class II molecules) include HLA DM, HLA DO, I-A beta2, and I-E beta2.

A “peptide free MHC Class I molecule” as used everywhere herein is meant to be a MHC Class I molecule as defined above with no peptide.

A “peptide free MHC Class II molecule” as used everywhere herein is meant to be a MHC Class II molecule as defined above with no peptide.

Such peptide free MHC Class I and II molecules are also called “empty” MHC Class I and II molecules.

The MHC molecule may suitably be a vertebrate MHC molecule such as a human, a mouse, a rat, a porcine, a bovine or an avian MHC molecule. Such MHC complexes from different species have different names. E.g. in humans, MHC complexes are denoted HLA. The person skilled in the art will readily know the name of the MHC complexes from various species.

In general, the term “MHC molecule” is intended to include alleles. By way of example, in humans e.g. HLA A, HLA B, HLA C, HLA D, HLA E, HLA F, HLA G, HLA H, HLA DR, HLA DQ and HLA DP alleles are of interest, and in the mouse system, H-2 alleles are of interest. Likewise, in the rat system RT1-alleles, in the porcine system SLA-alleles, in the bovine system BoLA, in the avian system e.g. chicken-B alleles, are of interest.

“MHC complexes” and “MHC constructs” are used interchangeably herein.

“MHC protein” and “MHC molecule” are used interchangeably herein. Accordingly, a functional MHC peptide complex comprises a MHC protein or MHC molecule associated with a peptide to be presented for cells or binding partners having an affinity for said peptide.

By the terms “MHC complexes” and “MHC multimers” as used herein are meant such complexes and multimers thereof, which are capable of performing at least one of the functions attributed to said complex or multimer. The terms include both classical and non-classical MHC complexes. The meaning of “classical” and “non-classical” in connection with MHC complexes is well known to the person skilled in the art. Non-classical MHC complexes are subgroups of MHC-like complexes. The term “MHC complex” includes MHC Class I molecules, MHC Class II molecules, as well as MHC-like molecules (both Class I and Class II), including the subgroup non-classical MHC Class I and Class II molecules.

The MHC molecule can suitably be a vertebrate MHC molecule such as a human, a mouse, a rat, a porcine, a bovine or an avian MHC molecule. Such MHC complexes from different species have different names. E.g. in humans, MHC complexes are denoted HLA. The person skilled in the art will readily know the name of the MHC complexes from various species.

MHC multimer: The terms MHC multimer, MHCmer and MHC′mer herein are used interchangeably, to denote a complex comprising more than one MHC-peptide complexes, held together by covalent or non-covalent bonds.

Monoclonal antibodies: Monoclonal antibodies, as used herein, are antibodies that are identical because they were produced by one type of immune cell and are all clones of a single parent cell.

Monovalent antibodies: The antibodies in the present invention can be monovalent antibodies. Methods for preparing monovalent antibodies are well known in the art. For example, one method involves recombinant expression of immunoglobulin light chain and modified heavy chain. The heavy chain is truncated generally at any point in the Fc region so as to prevent heavy chain crosslinking. Alternatively, the relevant cysteine residues are substituted with another amino acid residue or are deleted so as to prevent crosslinking. In vitro methods are also suitable for preparing monovalent antibodies. Digestion of antibodies to produce fragments thereof, particularly, Fab fragments, can be accomplished using routine techniques known in the art.

Multimerization domain: A multimerization domain is a molecule, a complex of molecules, or a solid support, to which one or more MHC or MHC-peptide complexes can be attached. A multimerization domain consist of one or more carriers and/or one or more scaffolds and may also contain one or more linkers connecting carrier to scaffold, carrier to carrier, scaffold to scaffold. The multimerization domain may also contain one or more linkers that can be used for attachment of MHC complexes and/or other molecules to the multimerization domain. Multimerization domains thus include IgG, streptavidin, streptactin, micelles, cells, polymers, beads and other types of solid support, and small organic molecules carrying reactive groups or carrying chemical motifs that can bind MHC complexes and other molecules.

Nanobodies: Nanobodies as used herein is a type of antibodies derived from camels, and are much smaller than traditional antibodies.

Neutralizing antibodies: neutralizing antibodies as used herein is an antibody which, on mixture with the homologous infectious agent, reduces the infectious titer.

NMR: NMR (Nuclear magnetic resonance), as used herein, is a physical phenomenon based upon the quantum mechanical magnetic properties of an atom's nucleus. NMR refers to a family of scientific methods that exploit nuclear magnetic resonance to study molecules.

Non-covalent: The term noncovalent bond as used herein is a type of chemical bond, that does not involve the sharing of pairs of electrons, but rather involves more dispersed variations of electromagnetic interactions.

Nucleic acid duplex: A nucleic acid is a complex, high-molecular-weight biochemical macromolecule composed of nucleotide chains that convey genetic information. The most common nucleic acids are deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).

Nucleophilic: a nucleophile, as used herein, is a reagent that forms a chemical bond to its reaction partner (the electrophile) by donating both bonding electrons.

“One or more” as used everywhere herein is intended to include one and a plurality.

A “peptide free MHC Class I molecule” as used everywhere herein is meant to be a MHC Class I molecule as defined above with no peptide.

A “peptide free MHC Class II molecule” as used everywhere herein is meant to be a MHC Class II molecule as defined above with no peptide.

Such peptide free MHC Class I and II molecules are also called “empty” MHC Class I and II molecules.

Pegylated: pegylated, as used herein, is conjugation of Polyethylene glycol (PEG) to proteins.

Peptide or protein: Any molecule composed of at least two amino acids. Peptide normally refers to smaller molecules of up to around 30 amino acids and protein to larger molecules containing more amino acids.

Phosphorylated; phosphorylated, as used herein, is the addition of a phosphate (PO₄) group to a protein molecule or a small molecule.

“A plurality” as used everywhere herein should be interpreted as two or more.

PNA: PNA (Peptide nucleic acid) as used herein is a chemical similar to DNA or RNA. PNA is not known to occur naturally in existing life on Earth but is artificially synthesized and used in some biological research and medical treatments. DNA and RNA have a deoxyribose and ribose sugar backbone, respectively, whereas PNA's backbone is composed of repeating N-(2-aminoethyl)-glycine units linked by peptide bonds. The various purine and pyrimidine bases are linked to the backbone by methylene carbonyl bonds. PNAs are depicted like peptides, with the N-terminus at the first (left) position and the C-terminus at the right.

“A plurality” as used everywhere herein should be interpreted as two or more. This applies i.a. to the MHC peptide complex and the binding entity. When a plurality of MHC peptide complexes is attached to the multimerization domain, such as a scaffold or a carrier molecule, the number of MHC peptide complexes need only be limited by the capacity of the multimerization domain.

Polyclonal antibodies: a polyclonal antibody as used herein is an antibody that is derived from different B-cell lines. They are a mixture of immunoglobulin molecules secreted against a specific antigen, each recognising a different epitope.

Polymer: the term polymer as used herein is defined as a compound composed of repeating structural units, or monomers, connected by covalent chemical bonds.

Polypeptide: Peptides are the family of short molecules formed from the linking, in a defined order, of various α-amino acids. The link between one amino acid residue and the next is an amide bond and is sometimes referred to as a peptide bond. Longer peptides are referred to as proteins or polypeptide.

Polysaccharide: The term polysaccharide as used herein is defined as polymers made up of many monosaccharides joined together by glycosidic linkages.

Radicals: radicals, as used herein, are atomic or molecular species with unpaired electrons on an otherwise open shell configuration. These unpaired electrons are usually highly reactive, so radicals are likely to take part in chemical reactions.

Radioactivity: Radioactive decay is the process in which an unstable atomic nucleus loses energy by emitting radiation in the form of particles or electromagnetic waves.

RNA: RNA (Ribonucleic acid) as used herein is a nucleic acid polymer consisting of nucleotide monomers that plays several important roles in the processes that translate genetic information from deoxyribonucleic acid (DNA) into protein products

Scaffold: A scaffold is typically an organic molecule carrying reactive groups, capable of reacting with reactive groups on a MHC-peptide complex. Particularly small organic molecules of cyclic structure (e.g. functionalized cycloalkanes or functionalized aromatic ring structures) are termed scaffolds. Scaffold and carrier are used interchangeably herein where scaffold typically refers to smaller molecules of a multimerization domain and carrier typically refers to larger molecule and/or cell like structures.

Staining: In this invention staining means specific or unspecific labelling of cells by binding labeled molecules to defined proteins or other structures on the surface of cells or inside cells. The cells are either in suspension or part of a tissue. The labeled molecules can be MHC multimers, antibodies or similar molecules capable of binding specific structures on the surface of cells.

Streptavidin: Streptavidin as used herein is a tetrameric protein purified from the bacterium Streptomyces avidinii. Streptavidin is widely use in molecular biology through its extraordinarily strong affinity for biotin.

Sugar: Sugars as used herein include monosaccharides, disaccharides, trisaccharides and the oligosaccharides—comprising 1, 2, 3, and 4 or more monosaccharide units respectively.

Therapy: Treatment of illness or disability

Vaccine: A vaccine is an antigenic preparation used to establish immunity to a disease or illness and thereby protects or cure the body from a specific disease or illness. Vaccines are either prophylactic and prevent disease or therapeutic and treat disease. Vaccines may contain more than one type of antigen and is then called a combined vaccine.

Vaccination: The introduction of vaccine into the body of human or animals for the purpose of inducing immunity.

B.L. is an abbreviation for Bind level.

Aff. is an abbreviation for affinity.

BRIEF DESCRIPTION OF THE DRAWINGS

FIG. 1. Schematic representation of MHC multimer. A MHC multimer consist of a multimerization domain whereto one or more MHC-peptide complexes are attached through one or more linkers. The multimerization domain comprise one or more carriers and/or one or more scaffolds. The MHC-peptide complexes comprise a peptide and a MHC molecule.

FIG. 2. Program for peptide sequence motifs prediction.

FIG. 3. Full List of HLA Class I alleles assigned as of January 2007 from www.anthonynolan.org.uk/HIG/lists/class1list.html.

FIG. 4. List of top 30 HLA class 1 alleles in different human ethnic groups.

FIG. 5. Illustration of selected reaction groups.

FIG. 6. Illustration of selected cleavable linkers.

FIG. 7. Prediction of MHC class 1 mouse virus LCMV gp 1 protein nonamer peptide binders for H-2Kd using the Syfpeithi database. Peptides are ranked according to their binding score. Only peptides with binding scores above the value of 11 are listed. The peptides listed in FIG. 7 correspond to SEQ ID NO:61368 to SEQ ID NO:61663.

FIG. 8. Size exclusion chromatography of folded HLA-A*0201-β2m QLFEELQEL peptide-complex (SEQ ID NO:61664). Purification of HLA-A*0201-β2m QLFEELQEL peptide-complex (SEQ ID NO:61664) by size exclusion chromatography on a HiLoad 16/60 Superdex 75 column. Eluted protein was followed by measurement of the absorbance at 280 nm. The elution profile consisted of 4 peaks, corresponding to aggregated Heavy Chain, correctly folded MHC-complex, β2m and excess biotin and peptide.

FIG. 9. MHC-SHIFT Assay. The SHIFT Assay shows that heavy chain is efficiently biotinylated, since the band corresponding to biotinylated heavy chain (lane 2) is shifted up-wards upon incubation with streptavidin.

Lane 1: Benchmark protein-ladder.

Lane 2: Folded HLA-A*0201-β2m-QLFEELQEL peptide-complex (SEQ ID NO:61664).

Lane 3: Folded HLA-A*0201-β2m-QLFEELQEL peptide-complex (SEQ ID NO:61664) incubated with molar excess Streptavidin.

FIG. 10. Composition of Fluorescein-linker molecule. (A) Schematic representation of an example of a Fluorescein-linker molecule. (B) Composition of a L15 linker.

FIG. 11. List of the 24 MHC class 1 alleles used for peptide prediction by the database www.cbs.dtu.dk/services/NetMHC/ and the 14 MHC class 2 alleles used for peptide prediction by the database www.cbs.dtu.dk/services/NetMHCII/.

FIG. 12. Prediction of MHC class 1 mouse virus LCMV gp 1 protein nonamer peptide binders for H-2Kd using the Syfpeithi database. Peptides are ranked according to their binding score. Only peptides with binding scores above the value of 11 are listed. The peptides listed in FIG. 12 correspond to SEQ ID NO:61665 to SEQ ID NO:61726.

FIG. 13. Full List of HLA Class I alleles assigned as of January 2007 from www.anthonynolan.org.uk/HIG/lists/class1list.html.

FIG. 14. List of top 30 HLA class 1 alleles in different human ethnic groups.

FIG. 15. Ex vivo ELISPOT analysis of BclX(L)-specific, CD8 positive T cells in PBL from a breast cancer patient either with or without the BclX(L) YLNDHLEPWI peptide (SEQ ID NO:61727). Analysis were performed in doublets and number of IFN-gamma producing T-cells are presented. (Reference: Sorensen R B, Hadrup S R, Kollgaard T, Svane I M, Thor Straten P, Andersen M H (2006) Efficient tumor cell lysis mediated by a Bcl-X(L) specific T cell clone isolated from a breast cancer patient. Cancer Immunol Immunother April; 56 (4) 527-33).

FIG. 16. PBL from a breast cancer patient was analyzed by flow cytometry to identify Bcl-X(L)173-182 (peptide YLNDHLEPWI) (SEQ ID NO:61727) specific CD8 T cells using the dextramer complex HLA-A2/Bcl-X(L)173-182-APC, 7-AAD-PerCP, CD3-FITC, and CD8-APC-Cy7. The dextramer complex HLA-A2/HIV-1 pol476-484-APC was used as negative control. (Reference: Sorensen R B, Hadrup S R, Kollgaard T, Svane I M, Thor Straten P, Andersen M H (2006) Efficient tumor cell lysis mediated by a Bcl-X(L) specific T cell clone isolated from a breast cancer patient. Cancer Immunol Immunother April; 56 (4) 527-33).

FIG. 17. Ten expanded T cell clones isolated by Flow sorting and then expanded were tested for their specificity by analysis in a standard 51-Cr release assay. For this purpose, T2 cells loaded with either Bcl-X(L)173-182, YLNDHLEPWI peptide (SEQ ID NO:61727) or an irrelevant peptide (BA4697-105, GLQHWVPEL) (SEQ ID NO:61728 were used as target cells. Reference: Sorensen R B, Hadrup S R, Kollgaard T, Svane I M, Thor Straten P, Andersen M H (2006) Efficient tumor cell lysis mediated by a Bcl-X(L) specific T cell clone isolated from a breast cancer patient. Cancer Immunol Immunother April; 56 (4) 527-33).

FIG. 18. A Bcl-X(L)173-182 specific clone was tested for its cytotoxic potential in 51Cr-release assays. Two assays were performed a Cell lysis of T2 cells pulsed with Bcl-X(L)173-182 peptide or an irrelevant peptide (BA4697-105, GLQHWVPEL) (SEQ ID NO:61728) in three E:T ratios. b Cell lysis of T2 cells pulsed with different concentrations of Bcl-X(L)173-182 peptide at the E:T ratio 1:1. (Reference: Sorensen R B, Hadrup S R, Kollgaard T, Svane I M, Thor Straten P, Andersen M H (2006) Efficient tumor cell lysis mediated by a Bcl-X(L) specific T cell clone isolated from a breast cancer patient. Cancer Immunol Immunother April; 56 (4) 527-33).

FIG. 19. Detection of Borrelia specific T cells using MHC dextramers. Dot plots showing live gated CD3+/CD4− lymphocytes from Borrelia patient stained with (A) Negative Control MHC Dextramer (HLA-A*0201(GLAGDVSAV) (SEQ ID NO:61729) or (B) pool of MHC Dextramers containing peptides from Borrelia antigen Osp A and Fla B. pool of MHC Dextramers containing peptides from Borrelia antigen. 0.05% of the live gated CD3+/CD4− lymphocytes are positive for one or more of the MHC Dextramers in the pool.

FIG. 20. Detection of CMV specific T cells using MHC dextramers Dot plots showing live gated CD3+/CD4− lymphocytes from CMV infected patient stained with (A) Negative Control MHC Dextramers (HLA-A*0201(GLAGDVSAV)) (SEQ ID NO:61729) or (B) MHC Dextramers containing peptides from CMV pp65 antigen (HLA-A*0201(NLVPMVATV)) (SEQ ID NO:61730).

DETAILED DESCRIPTION OF THE INVENTION

In one aspect, the present invention is directed to novel MHC complexes optionally comprising a multimerization domain preferably comprising a carrier molecule and/or a scaffold.

There is also provided a MHC multimer comprising 2 or more MHC-peptide complexes and a multimerization domain to which the 2 or more MHC-peptide complexes are associated. The MHC multimer can generally be formed by association of the 2 or more MHC-peptide complexes with the multimerization domain to which the 2 or more MHC-peptide complexes are capable of associating.

The multimerization domain can be a scaffold associated with one or more MHC-peptide complexes, or a carrier associated with one or more, preferably more than one, MHC-peptide complex(es), or a carrier associated with a plurality of scaffolds each associated with one or more MHC-peptide complexes, such as 2 MHC-peptide complexes, 3 MHC-peptide complexes, 4 MHC-peptide complexes, 5 MHC-peptide complexes or more than 5 MHC-peptide complexes. Accordingly, multimerization domain collectively refers to each and every of the above. It will be clear from the detailed description of the invention provided herein below when the multimerization domain refers to a scaffold or a carrier or a carrier comprising one or more scaffolds.

Generally, when a multimerization domain comprising a carrier and/or a scaffold is present, the MHC complexes can be associated with this domain either directly or via one or more binding entities. The association can be covalent or non-covalent.

Accordingly, there is provided in one embodiment a MHC complex comprising one or more entities (a-b-P)_(n), wherein a and b together form a functional MHC protein capable of binding a peptide P, and wherein (a-b-P) is the MHC-peptide complex formed when the peptide P binds to the functional MHC protein, said MHC complex optionally further comprising a multimerization domain comprising a carrier molecule and/or a scaffold. “MHC complex” refers to any MHC complex, including MHC monomers in the form of a single MHC-peptide complex and MHC multimers comprising a multimerization domain to which more than one MHC peptide complex is associated.

When the invention is directed to complexes comprising a MHC multimer, i.e. a plurality of MHC peptide complexes of the general composition (a-b-P)_(n) associated with a multimerization domain, n is by definition more than 1, i.e. at least 2 or more. Accordingly, the term “MHC multimer” is used herein specifically to indicate that more than one MHC-peptide complex is associated with a multimerization domain, such as a scaffold or carrier or carrier comprising one or more scaffolds. Accordingly, a single MHC-peptide complex can be associated with a scaffold or a carrier or a carrier comprising a scaffold and a MHC-multimer comprising 2 or more MHC-peptide complexes can be formed by association of the individual MHC-peptide complexes with a scaffold or a carrier or a carrier comprising one or more scaffolds each associated with one or more MHC-peptide complexes.

When the MHC complex comprises a multimerization domain to which the n MHC-peptide complexes are associated, the association can be a covalent linkage so that each or at least some of the n MHC-peptide complexes is covalently linked to the multimerization domain, or the association can be a non-covalent association so that each or at least some of the n MHC-peptide complexes are non-covalently associated with the multimerization domain.

The MHC complexes of the invention may be provided in non-soluble or soluble form, depending on the intended application.

Effective methods to produce a variety of MHC complexes comprising highly polymorphic human HLA encoded proteins makes it possible to perform advanced analyses of complex immune responses, which may comprise a variety of peptide epitope specific T-cell clones.

One of the benefits of the MHC complexes of the present invention is that the MHC complexes overcome low intrinsic affinities of monomer ligands and counter receptors. The MHC complexes have a large variety of applications that include targeting of high affinity receptors (e.g. hormone peptide receptors for insulin) on target cells. Taken together poly-ligand binding to target cells has numerous practical, clinical and scientifically uses.

Thus, the present invention provides MHC complexes which present mono-valent or multivalent binding sites for MHC recognising cells, such as MHC complexes optionally comprising a multimerization domain, such as a scaffold or a carrier molecule, which multimerization domain have attached thereto, directly or indirectly via one or more linkers, covalently or non-covalently, one or more MHC peptide complexes. “One or more” as used herein is intended to include one as well as a plurality, such as at least 2. This applies i.a. to the MHC peptide complexes and to the binding entities of the multimerization domain. The scaffold or carrier molecule may thus have attached thereto a MHC peptide complex or a plurality of such MHC peptide complexes, and/or a linker or a plurality of linkers.

Product

The product of the present invention is a MHC multimer as described above. As used in the description of this invention, the term “MHC multimers” will be used interchangeably with the terms MHC′mers and MHCmers, and will include any number, (larger than one) of MHC-peptide complexes, held together in a large complex by covalent or non-covalent interactions between a multimerization domain and one or more MHC-peptide complexes, and will also include the monomeric form of the MHC-peptide complex, i.e. a MHC-peptide complex that is not attached to a multimerization domain. The multimerization domain consists of one or more carriers and/or one or more scaffolds while the MHC-peptide complex consists of MHC molecule and antigenic peptide. MHC-peptide complexes may be attached to the multimerization domain through one or more linkers. A schematic representation of a MHC multimer is presented in FIG. 1.

In one preferred embodiment the MHC multimer is between 50,000 Da and 1,000,000 Da, such as from 50,000 Da to 980,000; for example from 50,000 Da to 960,000; such as from 50,000 Da to 940,000; for example from 50,000 Da to 920,000; such as from 50,000 Da to 900,000; for example from 50,000 Da to 880,000; such as from 50,000 Da to 860,000; for example from 50,000 Da to 840,000; such as from 50,000 Da to 820,000; for example from 50,000 Da to 800,000; such as from 50,000 Da to 780,000; for example from 50,000 Da to 760,000; such as from 50,000 Da to 740,000; for example from 50,000 Da to 720,000; such as from 50,000 Da to 700,000; for example from 50,000 Da to 680,000; such as from 50,000 Da to 660,000; for example from 50,000 Da to 640,000; such as from 50,000 Da to 620,000; for example from 50,000 Da to 600,000; such as from 50,000 Da to 580,000; for example from 50,000 Da to 560,000; such as from 50,000 Da to 540,000; for example from 50,000 Da to 520,000; such as from 50,000 Da to 500,000; for example from 50,000 Da to 480,000; such as from 50,000 Da to 460,000; for example from 50,000 Da to 440,000; such as from 50,000 Da to 420,000; for example from 50,000 Da to 400,000; such as from 50,000 Da to 380,000; for example from 50,000 Da to 360,000; such as from 50,000 Da to 340,000; for example from 50,000 Da to 320,000; such as from 50,000 Da to 300,000; for example from 50,000 Da to 280,000; such as from 50,000 Da to 260,000; for example from 50,000 Da to 240,000; such as from 50,000 Da to 220,000; for example from 50,000 Da to 200,000; such as from 50,000 Da to 180,000; for example from 50,000 Da to 160,000; such as from 50,000 Da to 140,000; for example from 50,000 Da to 120,000; such as from 50,000 Da to 100,000; for example from 50,000 Da to 80,000; such as from 50,000 Da to 60,000; such as from 100,000 Da to 980,000; for example from 100,000 Da to 960,000; such as from 100,000 Da to 940,000; for example from 100,000 Da to 920,000; such as from 100,000 Da to 900,000; for example from 100,000 Da to 880,000; such as from 100,000 Da to 860,000; for example from 100,000 Da to 840,000; such as from 100,000 Da to 820,000; for example from 100,000 Da to 800,000; such as from 100,000 Da to 780,000; for example from 100,000 Da to 760,000; such as from 100,000 Da to 740,000; for example from 100,000 Da to 720,000; such as from 100,000 Da to 700,000; for example from 100,000 Da to 680,000; such as from 100,000 Da to 660,000; for example from 100,000 Da to 640,000; such as from 100,000 Da to 620,000; for example from 100,000 Da to 600,000; such as from 100,000 Da to 580,000; for example from 100,000 Da to 560,000; such as from 100,000 Da to 540,000; for example from 100,000 Da to 520,000; such as from 100,000 Da to 500,000; for example from 100,000 Da to 480,000; such as from 100,000 Da to 460,000; for example from 100,000 Da to 440,000; such as from 100,000 Da to 420,000; for example from 100,000 Da to 400,000; such as from 100,000 Da to 380,000; for example from 100,000 Da to 360,000; such as from 100,000 Da to 340,000; for example from 100,000 Da to 320,000; such as from 100,000 Da to 300,000; for example from 100,000 Da to 280,000; such as from 100,000 Da to 260,000; for example from 100,000 Da to 240,000; such as from 100,000 Da to 220,000; for example from 100,000 Da to 200,000; such as from 100,000 Da to 180,000; for example from 100,000 Da to 160,000; such as from 100,000 Da to 140,000; for example from 100,000 Da to 120,000; such as from 150,000 Da to 980,000; for example from 150,000 Da to 960,000; such as from 150,000 Da to 940,000; for example from 150,000 Da to 920,000; such as from 150,000 Da to 900,000; for example from 150,000 Da to 880,000; such as from 150,000 Da to 860,000; for example from 150,000 Da to 840,000; such as from 150,000 Da to 820,000; for example from 150,000 Da to 800,000; such as from 150,000 Da to 780,000; for example from 150,000 Da to 760,000; such as from 150,000 Da to 740,000; for example from 150,000 Da to 720,000; such as from 150,000 Da to 700,000; for example from 150,000 Da to 680,000; such as from 150,000 Da to 660,000; for example from 150,000 Da to 640,000; such as from 150,000 Da to 620,000; for example from 150,000 Da to 600,000; such as from 150,000 Da to 580,000; for example from 150,000 Da to 560,000; such as from 150,000 Da to 540,000; for example from 150,000 Da to 520,000; such as from 150,000 Da to 500,000; for example from 150,000 Da to 480,000; such as from 150,000 Da to 460,000; for example from 150,000 Da to 440,000; such as from 150,000 Da to 420,000; for example from 150,000 Da to 400,000; such as from 150,000 Da to 380,000; for example from 150,000 Da to 360,000; such as from 150,000 Da to 340,000; for example from 150,000 Da to 320,000; such as from 150,000 Da to 300,000; for example from 150,000 Da to 280,000; such as from 150,000 Da to 260,000; for example from 150,000 Da to 240,000; such as from 150,000 Da to 220,000; for example from 150,000 Da to 200,000; such as from 150,000 Da to 180,000; for example from 150,000 Da to 160,000.

In another preferred embodiment the MHC multimer is between 1,000,000 Da and 3,000,000 Da, such as from 1,000,000 Da to 2,800,000; for example from 1,000,000 Da to 2,600,000; such as from 1,000,000 Da to 2,400,000; for example from 1,000,000 Da to 2,200,000; such as from 1,000,000 Da to 2,000,000; for example from 1,000,000 Da to 1,800,000; such as from 1,000,000 Da to 1,600,000; for example from 1,000,000 Da to 1,400,000.

In the following it is described how to generate the product of the present invention.

Number of MHC Complexes pr Multimer

A non-exhaustive list of possible MHC mono- and multimers illustrates the possibilities.

n indicates the number of MHC complexes comprised in the multimer:

a) n=1, Monomers

b) n=2, Dimers, multimerization can be based on IgG scaffold, SA with two MHC's, coiled-coil dimerization e.g. Fos.Jun dimerization

c) n=3, Trimers, multimerization can be based on SA as scaffold with three MHC's, TNFalpha-MHC hybrids, triplex DNA-MHC conjugates or other trimer structures

d) n=4, Tetramers, multimerization can be based on SA with all four binding sites occupied by MHC molecules or on dimeric IgA

e) n=5, Pentamers, multimerization can take place around a pentameric coil-coil structure

f) n=6, Hexamers

g) n=7, Heptamers

h) n=8-12, Octa-dodecamers, multimerization can take place using Streptactin

i) n=10, Decamers, multimerization could take place using IgM

j) 1<n<100, Dextramers, as multimerization domain polymers such as polypeptide, polysaccharides and Dextrans can be used.

k) 1<n<1000, Multimerization make use of DC, APC, micelles, liposomes, beads, surfaces e.g. microtiterplate, tubes, microarray devices, micro-fluidic systems

l) 1<n, n in billions or trillions or higher, multimerization take place on beads, and surfaces e.g. microtiterplate, tubes, microarray devices, micro-fluidic systems

MHC Origin

Any of the three components of a MHC complex can be of any of the below mentioned origins. The list is non-exhaustive. A complete list would encompass all Chordate species. By origin is meant that the sequence is identical or highly homologous to a naturally occurring sequence of the specific species.

List of Origins:

-   -   Human     -   Mouse     -   Primate         -   Chimpansee         -   Gorilla         -   Orang Utan     -   Monkey         -   Macaques     -   Porcine (Swine/Pig)     -   Bovine (Cattle/Antilopes)     -   Equine (Horse)     -   Camelides (Camels)     -   Ruminants (Deears)     -   Canine (Dog)     -   Feline (Cat)     -   Bird         -   Chicken         -   Turkey     -   Fish     -   Reptiles     -   Amphibians         Generation of MHC Multimers

Different approaches to the generation of various types of MHC multimers are described in U.S. Pat. No. 5,635,363 (Altmann et al.), patent application WO 02/072631 A2 (Winther et al.), patent application WO 99/42597, US patent 2004209295, U.S. Pat. No. 5,635,363, and is described elsewhere in the present patent application as well. In brief, MHC multimers can be generated by first expressing and purifying the individual protein components of the MHC protein, and then combining the MHC protein components and the peptide, to form the MHC-peptide complex. Then an appropriate number of MHC-peptide complexes are linked together by covalent or non-covalent bonds to a multimerization domain. This can be done by chemical reactions between reactive groups of the multimerization domain (e.g. vinyl sulfone functionalities on a dextran polymer) and reactive groups on the MHC protein (e.g. amino groups on the protein surface), or by non-covalent interaction between a part of the MHC protein (e.g. a biotinylated peptide component) and the multimerization domain (e.g. four binding sites for biotin on the strepavidin tetrameric protein). As an alternative, the MHC multimer can be formed by the non-covalent association of amino acid helices fused to one component of the MHC protein, to form a pentameric MHC multimer, held together by five helices in a coiled-coil structure making up the multimerization domain.

Appropriate chemical reactions for the covalent coupling of MHC and the multimerization domain include nucleophilic substitution by activation of electrophiles (e.g. acylation such as amide formation, pyrazolone formation, isoxazolone formation; alkylation; vinylation; disulfide formation), addition to carbon-hetero multiple bonds (e.g. alkene formation by reaction of phosphonates with aldehydes or ketones; arylation; alkylation of arenes/hetarenes by reaction with alkyl boronates or enolethers), nucleophilic substitution using activation of nucleophiles (e.g. condensations; alkylation of aliphatic halides or tosylates with enolethers or enamines), and cycloadditions.

Appropriate molecules, capable of providing non covalent interactions between the multimerization domain and the MHC-peptide complex, involve the following molecule pairs and molecules: streptavidin/biotin, avidin/biotin, antibody/antigen, DNA/DNA, DNA/PNA, DNA/RNA, PNA/PNA, LNA/DNA, leucine zipper e.g. Fos/Jun, IgG dimeric protein, IgM multivalent protein, acid/base coiled-coil helices, chelate/metal ion-bound chelate, streptavidin (SA) and avidin and derivatives thereof, biotin, immunoglobulins, antibodies (monoclonal, polyclonal, and recombinant), antibody fragments and derivatives thereof, leucine zipper domain of AP-1 (jun and fos), hexa-his (metal chelate moiety), hexa-hat GST (glutathione S-transferase) glutathione affinity, Calmodulin-binding peptide (CBP), Strep-tag, Cellulose Binding Domain, Maltose Binding Protein, S-Peptide Tag, Chitin Binding Tag, Immuno-reactive Epitopes, Epitope Tags, E2Tag, HA Epitope Tag, Myc Epitope, FLAG Epitope, AU1 and AU5 Epitopes, Glu-Glu Epitope, KT3 Epitope, IRS Epitope, Btag Epitope, Protein Kinase-C Epitope, VSV Epitope, lectins that mediate binding to a diversity of compounds, including carbohydrates, lipids and proteins, e.g. Con A (Canavalia ensiformis) or WGA (wheat germ agglutinin) and tetranectin or Protein A or G (antibody affinity). Combinations of such binding entities are also comprised. In particular, when the MHC complex is tagged, the binding entity can be an “anti-tag”. By “anti-tag” is meant an antibody binding to the tag and any other molecule capable of binding to such tag.

Generation of Components of MHC

When employing MHC multimers for diagnostic purposes, it is preferable to use a MHC allele that corresponds to the tissue type of the person or animal to be diagnosed. Once the MHC allele has been chosen, a peptide derived from the antigenic protein may be chosen. The choice will depend on factors such as known or expected binding affinity of the MHC protein and the various possible peptide fragments that may be derived from the full sequence of the antigenic peptide, and will depend on the expected or known binding affinity and specificity of the MHC-peptide complex for the TCR. Preferably, the affinity of the peptide for the MHC molecule, and the affinity and specificity of the MHC-peptide complex for the TCR, should be high.

Similar considerations apply to the choice of MHC allele and peptide for therapeutic and vaccine purposes. In addition, for some of these applications the effect of binding the MHC multimer to the TCR is also important. Thus, in these cases the effect on the T-cell's general state must be considered, e.g. it must be decided whether the desired end result is apoptosis or proliferation of the T-cell.

Likewise, it must be decided whether stability is important. For some applications low stability may be an advantage, e.g. when a short-term effect is desired; in other instances, a long-term effect is desired and MHC multimers of high stability is desired. Stabilities of the MHC protein and of the MHC-peptide complex may be modified as described elsewhere herein.

Finally, modifications to the protein structure may be advantageous for some diagnostics purposes, because of e.g. increased stability, while in for vaccine purposes modifications to the MHC protein structure may induce undesired allergenic responses.

Generation of Protein Chains of MHC

Generation of MHC Class I Heavy Chain and β2-Microglobulin

MHC class I heavy chain (HC) and β2-mircroglobulin (β2m) can be obtained from a variety of sources.

-   -   a) Natural sources by means of purification from eukaryotic         cells naturally expressing the MHC class 1 or β2m molecules in         question.     -   b) The molecules can be obtained by recombinant means e.g.         using.         -   a. in vitro translation of mRNA obtained from cells             naturally expressing the MHC or β2m molecules in question         -   b. by expression and purification of HC and/or β2m gene             transfected cells of mammalian, yeast, bacterial or other             origin. This last method will normally be the method of             choice. The genetic material used for             transfection/transformation can be:             -   i. of natural origin isolated from cells, tissue or                 organisms             -   ii. of synthetical origin i.e. synthetic genes identical                 to the natural DNA sequence or it could be modified to                 introduce molecular changes or to ease recombinant                 expression.                 -   The genetic material can encode all or only a                     fragment of β2m, all or only a fragment of MHC class                     1 heavy chain. Of special interest are MHC class 1                     heavy chain fragments consisting of, the complete                     chain minus the intramembrane domain, a chain                     consisting of only the extracellular α1 and α2 class                     1 heavy chain domains, or any of the mentioned β2m                     and heavy chain fragments containing modified or                     added designer domain(s) or sequence(s).                     Generation of MHC Class 2 α- and β-Chains

MHC class 2 α- and β-chains can be obtained from a variety of sources:

-   -   a) Natural sources by means of purification from eukaryotic         cells naturally expressing the MHC class 2 molecules in         question.     -   b) By recombinant means e.g. using:         -   a. in vitro translation of mRNA obtained from cells             naturally expressing the MHC class 2 molecules in question         -   b. By purification from MHC class 2 gene transfected cells             of mammalian, yeast, bacterial or other origin. This last             method will normally be the method of choice. The genetic             material used for transfection/transformation can be             -   i. of natural origin isolated from cells, tissue or                 organisms             -   ii. of synthetical origin i.e. synthetic genes identical                 to the natural DNA sequence or it could be modified to                 introduce molecular changes or to ease recombinant                 expression.                 -   The genetic material can encode all or only a                     fragment of MHC class 2 α- and β-chains. Of special                     interest are MHC class 2 α- and β-chain fragments                     consisting of, the complete α- and β-chains minus                     the intramembrane domains of either or both chains;                     and α- and β-chains consisting of only the                     extracellular domains of either or both, i.e α1 plus                     α2 and β1 plus β2 domains, respectively.                 -   The genetic material can be modified to encode the                     interesting MHC class 2 molecule fragments                     consisting of domains starting from the amino                     terminal in consecutive order, MHC class 2 β1 plus                     MHC class 2 α1 plus MHC class 1 α3 domains or in                     alternative order, MHC class 2 α1 plus MHC class 2                     β1 plus MHC class 1 α3 domains.                 -   Lastly, the genetic material can encode any of the                     above mentioned MHC class 2 α- and β-chain molecules                     or fragments containing modified or added designer                     domain(s) or sequence(s).     -   c) The MHC material may also be of exclusively synthetic origin         manufactured by solid phase protein synthesis. Any of the above         mentioned molecules can be made this way.         Modified MHC I or MHC II Complexes

MHC I and MHC II complexes modified in any way as described above, can bind TCR. Modifications include mutations (substitutions, deletions or insertions of natural or non-natural amino acids, or any other organic molecule. The mutations are not limited to those that increase the stability of the MHC complex, and could be introduced anywhere in the MHC complex. One example of special interest is mutations introduced in the α3 subunit of MHC I heavy chain. The α3-subunit interacts with CD8 molecules on the surface of T cells. To minimize binding of MHC multimer to CD8 molecules on the surface of non-specific T cells, amino acids in α3 domain involved in the interaction with CD8 can be mutated. Such a mutation can result in altered or abrogated binding of MHC to CD8 molecules. Another example of special interest is mutations in areas of the β2-domain of MHC II molecules responsible for binding CD4 molecules.

Another embodiment is chemically modified MHC complexes where the chemical modification could be introduced anywhere in the complex, e.g. a MHC complex where the peptide in the peptide-binding cleft has a dinitrophenyl group attached.

Modified MHC complexes could also be MHC I or MHC II fusion proteins where the fusion protein is not necessarily more stable than the native protein. Of special interest is MHC complexes fused with genes encoding an amino acid sequence capable of being biotinylated with a Bir A enzyme (Schatz, P. J., (1993), Biotechnology 11(10):1138-1143). This biotinylation sequence could be fused with the COOH-terminal of β2m or the heavy chain of MHC I molecules or the COOH-terminal of either the α-chain or β-chain of MHC II. Similarly, other sequences capable of being enzymatically or chemically modified, can be fused to the NH₂ or COOH-terminal ends of the MHC complex.

Stabilization of Empty MHC Complexes and MHC-Peptide Complexes.

Classical MHC complexes are in nature embedded in the membrane. A preferred embodiment includes multimers comprising a soluble form of MHC II or I where the transmembrane and cytosolic domains of the membrane-anchored MHC complexes are removed. The removal of the membrane-anchoring parts of the molecules can influence the stability of the MHC complexes. The stability of MHC complexes is an important parameter when generating and using MHC multimers.

MHC I complexes consist of a single membrane-anchored heavy chain that contains the complete peptide binding groove and is stable in the soluble form when complexed with β2m. The long-term stability is dependent on the binding of peptide in the peptide-binding groove. Without a peptide in the peptide binding groove the heavy chain and β2m tend to dissociate. Similarly, peptides with high affinity for binding in the peptide-binding groove will typically stabilize the soluble form of the MHC complex while peptides with low affinity for the peptide-binding groove will typically have a smaller stabilizing effect.

In contrast, MHC II complexes consist of two membrane-anchored chains of almost equal size. When not attached to the cell membrane the two chains tend to dissociate and are therefore not stable in the soluble form unless a high affinity peptide is bound in the peptide-binding groove or the two chains are held together in another way.

In nature MHC I molecules consist of a heavy chain combined with β2m, and a peptide of typically 8-11 amino acids. Herein, MHC I molecules also include molecules consisting of a heavy chain and β2m (empty MHC), or a heavy chain combined with a peptide or a truncated heavy chain comprising α1 and α2 subunits combined with a peptide, or a full-length or truncated heavy chain combined with a full-length or truncated β2m chain. These MHC I molecules can be produced in E. coli as recombinant proteins, purified and refolded in vitro (Garboczi et al., (1992), Proc. Natl. Acad. Sci. 89, 3429-33). Alternatively, insect cell systems or mammalian cell systems can be used. To produce stable MHC I complexes and thereby generate reliable MHC I multimers several strategies can be followed. Stabilization strategies for MHC I complexes are described in the following.

Stabilization Strategies for MHC I Complexes

Generation of Covalent Protein-Fusions.

-   -   MHC I molecules can be stabilized by introduction of one or more         linkers between the individual components of the MHC I complex.         This could be a complex consisting of a heavy chain fused with         β2m through a linker and a soluble peptide, a heavy chain fused         to β2m through a linker, a heavy chain/β2m dimer covalently         linked to a peptide through a linker to either heavy chain or         β2m, and where there can or can not be a linker between the         heavy chain and β2m, a heavy chain fused to a peptide through a         linker, or the α1 and α2 subunits of the heavy chain fused to a         peptide through a linker. In all of these example         protein-fusions, each of the heavy chain, β2m and the peptide         can be truncated.     -   The linker could be a flexible linker, e.g. made of glycine and         serine and e.g. between 5-20 residues long. The linker could         also be rigid with a defined structure, e.g. made of amino acids         like glutamate, alanine, lysine, and leucine creating e.g. a         more rigid structure.     -   In heavy chain-β2m fusion proteins the COOH terminus of β2m can         be covalently linked to the NH₂ terminus of the heavy chain, or         the NH₂ terminus of β2m can be linked to the COOH terminus of         the heavy chain. The fusion-protein can also comprise a β2m         domain, or a truncated β2m domain, inserted into the heavy         chain, to form a fusion-protein of the form “heavy chain (first         part)-β2m-heavy chain (last part)”.     -   Likewise, the fusion-protein can comprise a heavy chain domain,         or a truncated heavy chain, inserted into the β2m chain, to form         a fusion-protein of the form “β2m(first part)-heavy         chain-β2m(last part)”.     -   In peptide-β2m fusion proteins the COOH terminus of the peptide         is preferable linked to the NH₂ terminus of β2m but the peptide         can also be linked to the COOH terminal of β2m via its NH₂         terminus. In heavy chain-peptide fusion proteins it is preferred         to fuse the NH₂ terminus of the heavy chain to the COOH terminus         of the peptide, but the fusion can also be between the COOH         terminus of the heavy chain and the NH₂ terminus of the peptide.         In heavy chain-β2m-peptide fusion proteins the NH₂ terminus of         the heavy chain can be fused to the COOH terminus of β2m and the         NH₂ terminus of β2m can be fused to the COOH terminus of the         peptide.

Non-Covalent Stabilization by Binding to an Unnatural Component

-   -   Non-covalent binding of unnatural components to the MHC I         complexes can lead to increased stability. The unnatural         component can bind to both the heavy chain and the β2m, and in         this way promote the assemble of the complex, and/or stabilize         the formed complex. Alternatively, the unnatural component can         bind to either β2m or heavy chain, and in this way stabilize the         polypeptide in its correct conformation, and in this way         increase the affinity of the heavy chain for β2m and/or peptide,         or increase the affinity of β2m for peptide.     -   Here, unnatural components mean antibodies, peptides, aptamers         or any other molecule with the ability to bind peptides         stretches of the MHC complex. Antibody is here to be understood         as truncated or full-length antibodies (of isotype IgG, IgM,         IgA, IgE), Fab, scFv or bi-Fab fragments or diabodies.     -   An example of special interest is an antibody binding the MHC I         molecule by interaction with the heavy chain as well as β2m. The         antibody can be a bispecific antibody that binds with one arm to         the heavy chain and the other arm to the β2m of the MHC complex.         Alternatively the antibody can be monospecific, and bind at the         interface between heavy chain and β2m.     -   Another example of special interest is an antibody binding the         heavy chain but only when the heavy chain is correct folded.         Correct folded is here a conformation where the MHC complex is         able to bind and present peptide in such a way that a restricted         T cell can recognize the MHC-peptide complex and be activated.         This type of antibody can be an antibody like the one produced         by the clone W6/32 (M0736 from Dako, Denmark) that recognizes a         conformational epitope on intact human and some monkey MHC         complexes containing β2m, heavy chain and peptide.

Generation of Modified Proteins or Protein Components

-   -   One way to improve stability of a MHC I complex am to increase         the affinity of the binding peptide for the MHC complex. This         can be done by mutation/substitution of amino acids at relevant         positions in the peptide, by chemical modifications of amino         acids at relevant positions in the peptide or introduction by         synthesis of non-natural amino acids at relevant positions in         the peptide. Alternatively, mutations, chemical modifications,         insertion of natural or non-natural amino acids or deletions         could be introduced in the peptide binding cleft, i.e. in the         binding pockets that accommodate peptide side chains responsible         for anchoring the peptide to the peptide binding cleft.         Moreover, reactive groups can be introduced into the antigenic         peptide; before, during or upon binding of the peptide, the         reactive groups can react with amino acid residues of the         peptide binding cleft, thus covalently linking the peptide to         the binding pocket.     -   Mutations/substitutions, chemical modifications, insertion of         natural or non-natural amino acids or deletions could also be         introduced in the heavy chain and/or β2m at positions outside         the peptide-binding cleft. By example, it has been shown that         substitution of XX with YY in position nn of human β₂m enhance         the biochemical stability of MHC Class I molecule complexes and         thus may lead to more efficient antigen presentation of         subdominant peptide epitopes.     -   A preferred embodiment is removal of “unwanted cysteine         residues” in the heavy chain by mutation, chemical modification,         amino acid exchange or deletion. “Unwanted cysteine residues” is         here to be understood as cysteines not involved in the correct         folding of the final MHC I molecule. The presence of cysteine         not directly involved in the formation of correctly folded MHC I         molecules can lead to formation of intra molecular disulfide         bridges resulting in a non correct folded MHC complex during in         vitro refolding.     -   Another method for covalent stabilization of MHC I complex am to         covalently attach a linker between two of the subunits of the         MHC complex. This can be a linker between peptide and heavy         chain or between heavy chain and beta2microglobulin.         Stabilization with Soluble Additives.     -   The stability of proteins in aqueous solution depends on the         composition of the solution. Addition of salts, detergents         organic solvent, polymers etc. can influence the stability. Of         special interest are additives that increase surface tension of         the MHC molecule without binding the molecule. Examples are         sucrose, mannose, glycine, betaine, alanine, glutamine, glutamic         acid and ammoniumsulfate. Glycerol, mannitol and sorbitol are         also included in this group even though they are able to bind         polar regions.     -   Another group of additives of special interest are able to         increase surface tension of the MHC molecule and simultaneously         interact with charged groups in the protein. Examples are MgSO₄,         NaCl, polyethylenglycol, 2-methyl-2,4-pentandiol and         guanidiniumsulfate.     -   Correct folding of MHC I complexes is very dependent on binding         of peptide in the peptide-binding cleft and the peptide binding         stabilises correct conformation. Addition of molar excess of         peptide will force the equilibrium against correct folded         MHC-peptide complexes. Likewise is excess β2m also expected to         drive the folding process in direction of correct folded MHC I         complexes. Therefore peptide identical to the peptide bound in         the peptide-binding cleft and β2m are included as stabilizing         soluble additives.     -   Other additives of special interest for stabilization of MHC I         molecules are BSA, fetal and bovine calf serum or individual         protein components in serum with a protein stabilizing effect.     -   All of the above mentioned soluble additives could be added to         any solution containing MHC I molecules in order to increase the         stability of the molecule. That could be during the refolding         process, to the soluble monomer or to a solutions containing MHC         I bound to a carrier.

MHC II molecules as used herein are defined as classical MHC II molecule consisting of a α-chain and a β-chain combined with a peptide. It could also be a molecule only consisting of α-chain and β-chain (α/β dimer or empty MHC II), a truncated α-chain (e.g. α1 domain alone) combined with full-length β-chain either empty or loaded with a peptide, a truncated β-chain (e.g. β1 domain alone) combined with a full-length α-chain either empty or loaded with a peptide or a truncated α-chain combined with a truncated β-chain (e.g. α1 and β1 domain) either empty or loaded with a peptide.

In contrast to MHC I molecules MHC II molecules are not easily refolded in vitro. Only some MHC II alleles may be produced in E. coli followed by refolding in vitro.

Therefore preferred expression systems for production of MHC II molecules are eukaryotic systems where refolding after expression of protein is not necessary. Such expression systems could be stable Drosophila cell transfectants, baculovirus infected insect cells, CHO cells or other mammalian cell lines suitable for expression of proteins.

Stabilization of soluble MHC II molecules is even more important than for MHC I molecules since both α- and β-chain are participants in formation of the peptide binding groove and tend to dissociate when not embedded in the cell membrane.

Stabilization Strategies for MHC II Complexes

Generation of Covalent Protein-Fusions.

-   -   MHC II complexes can be stabilized by introduction of one or         more linkers between the individual components of the MHC II         complex. This can be a α/β dimer with a linker between α-chain         and β-chain; a α/β dimer covalently linked to the peptide via a         linker to either the α-chain or β-chain; a α/β dimer, covalently         linked by a linker between the α-chain and β-chain, and where         the dimer is covalently linked to the peptide; a α/β dimer with         a linker between α-chain and β-chain, where the dimer is         combined with a peptide covalently linked to either α-chain or         β-chain.     -   The linker can be a flexible linker, e.g. made of glycine and         serine, and is typically between 5-20 residues long, but can be         shorter or longer. The linker can also be more rigid with a more         defined structure, e.g. made of amino acids like glutamate,         alanine, lysine, and leucine.     -   The peptides can be linked to the NH₂- or COOH-terminus of         either α-chain or β-chain. Of special interest are peptides         linked to the NH₂-terminus of the β-chain via their         COOH-terminus, since the linker required is shorter than if the         peptide is linked to the COOH-terminus of the β-chain.     -   Linkage of α-chain to β-chain can be via the COOH-terminus of         the β-chain to the NH₂-terminus of the α-chain or from the         COOH-terminus of the α-chain to the NH₂-terminus of the β-chain.     -   In a three-molecule fusion protein consisting of α-chain,         β-chain and peptide a preferred construct is where one linker         connect the COOH-terminus of the β-chain with the NH₂-terminus         of the α-chain and another linker connects the COOH-terminal of         the peptide with the NH₂-terminal of the β-chain. Alternatively         one linker joins the COOH-terminus of the α-chain with the         NH₂-terminus of the β-chain and the second linker joins the         NH₂-terminus of the peptide with the COOH-terminus of the         β-chain. The three peptides of the MHC complex can further be         linked as described above for the three peptides of the MHC         complex, including internal fusion points for the proteins.

Non-Covalent Stabilization by Binding Ligand.

-   -   Non-covalent binding of ligands to the MHC II complex can         promote assembly of α- and β-chain by bridging the two chains,         or by binding to either of the α- or β-chains, and in this way         stabilize the conformation of α or β, that binds β or α,         respectively, and/or that binds the peptide. Ligands here mean         antibodies, peptides, aptamers or any other molecules with the         ability to bind proteins.     -   A particular interesting example is an antibody binding the MHC         complex distal to the interaction site with TCR, i.e. distal to         the peptide-binding cleft. An antibody in this example can be         any truncated or full length antibody of any isotype (e.g. IgG,         IgM, IgA or IgE), a bi-Fab fragment or a diabody. The antibody         could be bispecific with one arm binding to the α-chain and the         other arm binding to the β-chain. Alternatively the antibody         could be monospecific and directed to a sequence fused to the         α-chain as well as to the β-chain.     -   Another example of interest is an antibody binding more central         in the MHC II molecule, but still interacting with both α- and         β-chain. Preferable the antibody binds a conformational epitope,         thereby forcing the MHC molecule into a correct folded         configuration. The antibody can be bispecific binding with one         arm to the α-chain and the other arm to the β-chain.         Alternatively the antibody is monospecific and binds to a         surface of the complex that involves both the α- and β-chain,         e.g. both the α2- and β2-domain or both the α1- and β1-domain.     -   The antibodies described above can be substituted with any other         ligand that binds at the α-/β-chain interface, e.g. peptides and         aptamers. The ligand can also bind the peptide, although, in         this case it is important that the ligand does not interfere         with the interaction of the peptide or binding cleft with the         TCR.

Non-Covalent Stabilization by Induced Multimerization.

-   -   In nature the anchoring of the α- and β-chains in the cell         membrane stabilizes the MHC II complexes considerably. As         mentioned above, a similar concept for stabilization of the         α/β-dimer was employed by attachment of the MHC II chains to the         Fc regions of an antibody, leading to a stable α/β-dimer, where         α and β are held together by the tight interactions between two         Fc domains of an antibody. Other dimerization domains can be         used as well.     -   In one other example of special interest MHC II molecules are         incorporated into artificial membrane spheres like liposomes or         lipospheres. MHC II molecules can be incorporated as monomers in         the membrane or as dimers like the MHC II-antibody constructs         describes above. In addition to stabilization of the MHC II         complex an increased avidity is obtained. The stabilization of         the dimer will in most cases also stabilize the trimeric         MHC-peptide complex.     -   Induced multimerization can also be achieved by biotinylation of         α- as well as β-chain and the two chains brought together by         binding to streptavidin. Long flexible linkers such as extended         glycine-serine tracts can be used to extend both chains, and the         chains can be biotinylated at the end of such extended linkers.         Then streptavidin can be used as a scaffold to bring the chains         together in the presence of the peptide, while the flexible         linkers still allow the chains to orientate properly.

Generation of Modified Proteins or Protein Components

-   -   Stability of MHC II complexes can be increased by covalent         modifications of the protein. One method is to increase the         affinity of the peptide for the MHC complex. This can be done by         exchange of the natural amino acids with other natural or         non-natural amino acids at relevant positions in the peptide or         by chemical modifications of amino acids at relevant positions         in the peptide. Alternatively, mutations, chemical         modifications, insertion of natural or non-natural amino acids         or deletions can be introduced in the peptide-binding cleft.     -   Mutations, chemical modifications, insertion of natural or         non-natural amino acids or deletions can alternatively be         introduced in α- and/or β-chain at positions outside the         peptide-binding cleft.     -   In this respect a preferred embodiment is to replace the         hydrophobic transmembrane regions of α-chain and β-chain by         leucine zipper dimerisation domains (e.g. Fos-Jun leucine         zipper; acid-base coiled-coil structure) to promote assembly of         α-chain and β-chain.     -   Another preferred embodiment is to introduce one or more         cysteine residues by amino acid exchange at the COOH-terminal of         both α-chain and β-chain, to create disulfide bridges between         the two chains upon assembly of the MHC complex.     -   Another embodiment is removal of “unwanted cysteine residues” in         either of the chains by mutation, chemical modification, amino         acid exchange or deletion. “Unwanted cysteine residues” is here         to be understood as cysteines not involved in correct folding of         the MHC II-peptide complex. The presence of cysteines not         directly involved in the formation of correctly folded MHC II         complexes can lead to formation of intra molecular disulfide         bridges and incorrectly folded MHC complexes.     -   MHC II complexes can also be stabilized by chemically linking         together the subunits and the peptide. That can be a linker         between peptide and α-chain, between peptide and β-chain,         between α-chain and β-chain, and combination thereof.     -   Such linkages can be introduced prior to folding by linking two         of the complex constituents together, then folding this covalent         hetero-dimer in the presence of the third constituent. An         advantage of this method is that it only requires complex         formation between two, rather than three species.     -   Another possibility is to allow all three constituents to fold,         and then to introduce covalent cross-links on the folded         MHC-complex, stabilizing the structure. An advantage of this         method is that the two chains and the peptide will be correctly         positioned relatively to each other when the cross linkages are         introduced.

Stabilization with Soluble Additives.

-   -   Salts, detergents, organic solvent, polymers and any other         soluble additives can be added to increase the stability of MHC         complexes. Of special interest are additives that increase         surface tension of the MHC complex. Examples are sucrose,         mannose, glycine, betaine, alanine, glutamine, glutamic acid and         ammonium sulfate. Glycerol, mannitol and sorbitol are also         included in this group even though they are able to bind polar         regions.     -   Another group of additives of special interest increases surface         tension of the MHC complex and simultaneously can interact with         charged groups in the protein. Examples are MgSO₄, NaCl,         polyethylenglycol, 2-methyl-2,4-pentanediol and         guanidiniumsulphate.     -   Correct formation of MHC complexes is dependent on binding of         peptide in the peptide-binding cleft; the bound peptide appears         to stabilize the complex in its correct conformation. Addition         of molar excess of peptide will force the equilibrium towards         correctly folded MHC-peptide complexes. Likewise, excess β2m is         also expected to drive the folding process in direction of         correctly folded MHC complexes. Therefore peptide identical to         the peptide bound in the peptide-binding cleft and β2m can be         included as stabilizing soluble additives.     -   Other additives of special interest for stabilization of MHC         complexes are BSA, fetal and bovine calf serum, and other         protein components in serum with a protein stabilizing effect.     -   All of the above mentioned soluble additives could be added to         any solution containing MHC complexes in order to increase the         stability of the molecule. This can be during the refolding         process, to the formed MHC complex or to a solution of MHC         multimers comprising several MHC complexes That could be to the         soluble monomer, to a solution containing MHC II bound to a         carrier or to solutions used during analysis of MHC II specific         T cells with MHC II multimers.     -   Other additives of special interest for stabilization of MHC II         molecules are BSA, fetal and bovine calf serum or individual         protein components in serum with a protein stabilizing effect.     -   All of the above mentioned soluble additives could be added to         any solution containing MHC II molecules in order to increase         the stability of the molecule. That could be to the soluble         monomer, to a solution containing MHC II bound to a carrier or         to solutions used during analysis of MHC II specific T cells         with MHC II multimers.

Chemically Modified MHC I and II Complexes

-   -   There are a number of amino acids that are particularly reactive         towards chemical cross linkers. In the following, chemical         reactions are described that are particularly preferable for the         cross-linking or modification of MHC I or MHC II complexes.     -   The amino group at the N-terminal of both chains and of the         peptide, as well as amino groups of lysine side chains, are         nucleophilic and can be used in a number of chemical reactions,         including nucleophilic substitution by activation of         electrophiles (e.g. acylation such as amide formation,         pyrazolone formation, isoxazolone formation; alkylation;         vinylation; disulfide formation), addition to carbon-hetero         multiple bonds (e.g. alkene formation by reaction of         phosphonates with aldehydes or ketones; arylation; alkylation of         arenes/hetarenes by reaction with alkyl boronates or         enolethers), nucleophilic substitution using activation of         nucleophiles (e.g. condensations; alkylation of aliphatic         halides or tosylates with enolethers or enamines), and         cycloadditions. Example reagents that can be used in a reaction         with the amino groups are activated carboxylic acids such as         NHS-ester, tetra and pentafluoro phenolic esters, anhydrides,         acid chlorides and fluorides, to form stable amide bonds.         Likewise, sulphonyl chlorides can react with these amino groups         to form stable sulphone-amides. Iso-Cyanates can also react with         amino groups to form stable ureas, and isothiocyanates can be         used to introduce thio-urea linkages.     -   Aldehydes, such as formaldehyde and glutardialdehyde will react         with amino groups to form shiff's bases, than can be further         reduced to secondary amines.     -   The guanidino group on the side chain of arginine will undergo         similar reactions with the same type of reagents.     -   Another very useful amino acid is cysteine. The thiol on the         side chain is readily alkylated by maleimides, vinyl sulphones         and halides to form stable thioethers, and reaction with other         thiols will give rise to disulphides.     -   Carboxylic acids at the C-terminal of both chains and peptide,         as well as on the side chains of glutamic and aspartic acid, can         also be used to introduce cross-links. They will require         activation with reagents such as carbodiimides, and can then         react with amino groups to give stable amides.     -   Thus, a large number of chemistries can be employed to form         covalent cross-links. The crucial point is that the chemical         reagents are bi-functional, being capable of reacting with two         amino acid residues.     -   They can be either homo bi-functional, possessing two identical         reactive moieties, such as glutardialdehyde or can be hetero         bi-functional with two different reactive moieties, such as GMBS         (MaleimidoButyryloxy-Succinimide ester).     -   Alternatively, two or more reagents can be used; i.e. GMBS can         be used to introduce maleimides on the α-chain, and         iminothiolane can be used to introduce thiols on the β-chain;         the malemide and thiol can then form a thioether link between         the two chains. For the present invention some types of         cross-links are particularly useful. The folded MHC-complex can         be reacted with dextrans possessing a large number (up to many         hundreds) of vinyl sulphones. These can react with lysine         residues on both the α and β chains as well as with lysine         residues on the peptide protruding from the binding site,         effectively cross linking the entire MHC-complex. Such cross         linking is indeed a favored reaction because as the first lysine         residue reacts with the dextran, the MHC-complex becomes         anchored to the dextran favoring further reactions between the         MHC complex and the dextran multimerization domain. Another         great advantage of this dextran chemistry is that it can be         combined with fluorochrome labelling; i.e. the dextran is         reacted both with one or several MHC-complexes and one or more         fluorescent protein such as APC.     -   Another valuable approach is to combine the molecular biological         tools described above with chemical cross linkers. As an         example, one or more lysine residues can be inserted into the         α-chain, juxtaposed with glutamic acids in the β-chain, where         after the introduced amino groups and carboxylic acids are         reacted by addition of carbodiimide. Such reactions are usually         not very effective in water, unless as in this case, the groups         are well positioned towards reaction. This implies that one         avoids excessive reactions that could otherwise end up         denaturing or changing the conformation of the MHC-complex.     -   Likewise a dextran multimerization domain can be cross-linked         with appropriately modified MHC-complexes; i.e. one or both         chains of the MHC complex can be enriched with lysine residues,         increasing reactivity towards the vinylsulphone dextran. The         lysine's can be inserted at positions opposite the peptide         binding cleft, orienting the MHC-complexes favorably for T-cell         recognition.     -   Another valuable chemical tool is to use extended and flexible         cross-linkers. An extended linker will allow the two chains to         interact with little or no strain resulting from the linker that         connects them, while keeping the chains in the vicinity of each         other should the complex dissociate. An excess of peptide should         further favor reformation of dissociated MHC-complex.         Other TCR Binding Molecules

MHC I and MHC II complexes bind to TCRs. However, other molecules also bind TCR. Some TCR-biding molecules are described in the following. MHC I and MHC II complexes binding to TCRs may be substituted with other molecules capable of binding TCR or molecules that have homology to the classical MHC molecules and therefore potentially could be TCR binding molecules. These other TCR binding or MHC like molecules include:

Non-Classical MHC Complexes and Other MHC-Like Molecules:

Non-classical MHC complexes include protein products of MHC Ib and MHC IIb genes. MHC Ib genes encode β2m-associated cell-surface molecules but show little polymorphism in contrast to classical MHC class I genes. Protein products of MHC class Ib genes include HLA-E, HLA-G, HLA-F, HLA-H, MIC A, MIC B, ULBP-1, ULBP-2, ULBP-3 in humans and H2-M, H2-Q, H2-T and Rae1 in mice.

Non-classical MHC II molecules (protein products of MHC IIb genes) include HLA-DM, HLA-DO in humans and H2-DM and H2-DO in mice that are involved in regulation of peptide loading into MHC II molecules.

Another MHC-like molecule of special interest is the MHC I-like molecule CD1. CD1 is similar to MHC I molecules in its organization of subunits and association with β2m but presents glycolipids and lipids instead of peptides.

Artificial Molecules Capable of Binding Specific TCRs

Of special interest are antibodies that bind TCRs. Antibodies herein include full length antibodies of isotype IgG, IgM, IgE, IgA and truncated versions of these, antibody fragments like Fab fragments and scFv. Antibodies also include antibodies of antibody fragments displayed on various supramolecular structures or solid supports, including filamentous phages, yeast, mammalian cells, fungi, artificial cells or micelles, and beads with various surface chemistries.

Peptide Binding TCR

Another embodiment of special interest is peptides that bind TCRs. Peptides herein include peptides composed of natural, non-natural and/or chemically modified amino acids with a length of 8-20 amino acid. The peptides could also be longer than 20 amino acids or shorter than 8 amino acids. The peptides can or can not have a defined tertiary structure.

Aptamers

Aptamers are another preferred group of TCR ligands. Aptamers are herein understood as natural nucleic acids (e.g. RNA and DNA) or unnatural nucleic acids (e.g. PNA, LNA, morpholinos) capable of binding TCR. The aptamer molecules consist of natural or modified nucleotides in various lengths.

Other TCR-binding molecules can be ankyrin repeat proteins or other repeat proteins, Avimers, or small chemical molecules, as long as they are capable of binding TCR with a dissociation constant smaller than 10⁻³ M.

Generation of Antigenic Peptide

Approaches and Methods for the Identification and Design of Appropriate Peptides

MHC class 1 molecules normally binds octa-, nona-, deca- or ondecamer (8-, 9-, 10, -11-mer) peptides in their peptide binding groove. The individual MHC class 1 alleles have individual preferences for the peptide length within the given range. MHC class 2 molecules bind peptides most often with a total length of 13-18 amino acids around a 9-mer core motif containing the important amino acid anchor residues. However the total length is not strictly defined as for most MHC class 1 molecules.

For some of the MHC alleles the optimal peptide length is known and also the demands for specific amino acid residues in the so called anchor positions.

To identify binding peptides derived from a specific protein for a given MHC allele it is necessary to systematically work through the amino acid sequence of the protein to identify the putative binding peptides. Although a given peptide is a binder it is not necessarily a functional T-cell epitope. Functionality needs to be confirmed by a functional analysis e.g. ELISPOT, CTL killing assay or flow cytometry assay.

A measure for binding affinity of the peptide to the MHC molecules can for some MHC molecules be found in databases such as www.syfpeithi.de; www-bimas.cit.nih.gov/molbio/hla_bind/; www.cbs.dtu.dk/services/NetMHC/; www.cbs.dtu.dk/services/NetMHCII/.

Design of Binding Peptides

a) From Genomic DNA Sequences without Introns

When only the genomic DNA sequences are known and thereby reading frame and direction of transcription of the genes are unknown, the DNA sequence needs to be translated in all three reading frames in both directions leading to a total of six amino acid sequences for a given genome. From these amino acid sequences binding peptides can then be identified.

b) From Genomic DNA Sequences with Introns

In organisms having intron/exon gene structure the present approach will not be able to identify peptide sequence motifs that are derived by combination of amino acid sequences derived partly from two separate introns.

c) From cDNA Sequences

cDNA sequences can be translated into the actual amino acid sequences to allow peptide identification.

d) From Known Amino Acid Sequences

In the case of known protein sequences these can directly be applied to software analysis for prediction of peptide epitopes.

Binding peptide sequences can be predicted from any protein sequence by either a total approach generating binding peptide sequences for potentially any MHC allele or by a directed approach using software that specifically can predict the binding peptide sequences for a subset of MHC alleles for which the binding characteristics of the peptide is known.

Design of MHC Class 1 Binding Peptide Sequence

a) Total Approach

The MHC class 1 binding peptide prediction is done as follows using the total approach. The actual protein sequence is split up into 8-, 9-, 10-, and 11-mer peptide sequences. This is performed by starting at amino acid position 1 identifying the first 8-mer; then move the start position by one amino acid identifying the second 8-mer; then move the start position by one amino acid, identifying the third 8-mer. This procedure continues by moving start position by one amino acid for each round of peptide identification. Generated peptides will be amino acid position 1-8, 2-9, 3-10 etc. All peptides carrying one or more stop codons are omitted for further consideration. This procedure can be carried out manually or by means of a software program (FIG. 2). This procedure is then repeated in an identical fashion for 9-, 10 and 11-mers, respectively.

b) Directed Approach

Using a directed approach is only possible when working on prediction of peptide sequences binding to MHC class I alleles with known binding preferences. Examples of such programs are www.syfpeithi.de; www.imtech.res.in/raghava/propred1/index.html; www.cbs.dtu.dk/services/NetMHC/. Identified peptides can then be tested for biological relevance in functional assays such as Cytokine release assays, ELISPOT and CTL killing assays.

Prediction of good HLA class 1 peptide binders can be done at the HLA superfamily level even taking the combined action of endocolic and membrane bound protease activities as well as the TAP1 and TAP2 transporter specificities into consideration using the program www.cbs.dtu.dk/services/NetCTL/.

Design of MHC Class 2 Binding Peptide Sequence.

a) Total Approach and b) Directed Approach

The approach to predict putative peptide binders for MHC class 2 is similar as given above for MHC class 1 binding peptide prediction. The only change is the different size of the peptides, which is preferably 13-16 amino acids long for MHC class 2. The putative binding peptide sequences only describe the central part of the peptide including the 9-mer core peptide; in other words, the peptide sequences shown represent the core of the binding peptide with a few important flanking amino acids, which in some cases may be of considerably length generating binding peptides longer than the 13-16 amino acids.

Choice of MHC Allele

More than 600 MHC alleles (class 1 and 2) are known in humans; for many of these, the peptide binding characteristics are known. FIG. 3 presents an updated list of the HLA class 1 alleles. The frequency of the different HLA alleles varies considerably, also between different ethnic groups (FIG. 4). Thus it is of outmost importance to carefully select the MHC alleles that corresponds to the human group that one wish to study.

Peptide Modifications

Homologous Peptides

Predictions of the primary amino acid sequence for the binding peptides of MHC class I and class II molecules can be done as described above on the basis of the genetic information. Peptides homologous to the predicted peptide sequences may also be bound if they are sufficiently homologous i.e. are having an amino acid sequence identity greater than e.g. more than 90%, more than 80% or more than 70%. Identity being most important for the anchor residues.

Homologues MHC peptide sequences may arise from the existence of multiple strongly homologous alleles, from small insertions, deletions, inversions or substitutions.

Uncommon Amino Acids

Peptides having un-common amino acids may be bound in the MHC groove as well. Two un-common amino acids found in nature are selenocysteine and pyrrolysine.

Artificial Amino Acids

Artificial amino acids e.g. having the isomeric D-form may also make up isomeric D-peptides that can bind in the binding groove of the MHC molecules.

Chemically Modified Amino Acids

Bound peptides may also contain amino acids that are chemically modified or being linked to reactive groups that can be activated to induce changes in or disrupt the peptide.

Split or Combinatorial Peptide

A MHC binding peptide may also be of split- or combinatorial epitope origin i.e. formed by linkage of peptide fragments derived from two different peptide fragments and/or proteins. Such peptides can be the result of either genetic recombination on the DNA level or due to peptide fragment association during the complex break down of proteins during protein turnover. Possibly it could also be the result of faulty reactions during protein synthesis i.e. caused by some kind of mixed RNA handling. A kind of combinatorial peptide epitope can also be seen if a portion of a longer peptide make a loop out leaving only the terminal part of the peptide bound in the groove.

Position in Peptide of Amino Acid Change

Any of the mentioned changes of the bound peptide amino acid sequence, can be found individually or in combination at any position of the peptide e.g. position 1, 2, 3, 4, 5, 6, etc up to n, n being the final amino acid of the peptide.

TABLE 1 Post translational modification of peptides Protein primary structure and posttranslational modifications N-terminus Acetylation, Formylation, Pyroglutamate, Methylation, Glycation, Myristoylation (Gly), carbamylation C-terminus Amidation, Glycosyl phosphatidylinositol (GPI), O-methylation, Glypiation, Ubiquitmation, Sumoylation. Lysine Methylation, Acetylation, Acylation, Hydroxylation, Ubiquitination, SUMOylation, Desmosine formation, ADP-ribosylation, Deamination and Oxidation to aldehyde Cysteine Disulfide bond, Prenylation, Palmitoylation Serine/Threonine Phosphorylation, Glycosylation Tyrosine Phosphorylation, Sulfation, Porphyrin ring linkage, Flavin linkage GFP prosthetic group (Thr-Tyr-Gly sequence) formation, Lysine tyrosine quinone (LTQ) formation, Topaquinone (TPQ) formation Asparagine Deamidation, Glycosylation Aspartate Succinimide formation Glutamine Transglutamination Glutamate Carboxylation, Methylation, Polyglutamylation, Polyglycylation Arginine Citrullination, Methylation Proline Hydroxylation Post Translationally Modified Peptides

The amino acids of the MHC bound peptides can also be modified in various ways dependent on the amino acid in question or the modification can affect the amino- or carboxy-terminal end of the peptide. See table 1. Such peptide modifications are occurring naturally as the result of post translational processing of the parental protein. A non-exhaustive description of the major post translational modifications is given below, divided into three main types

a) Involving Addition Include:

-   -   acylation, the addition of an acetyl group, usually at the         N-terminus of the protein     -   alkylation, the addition of an alkyl group (e.g. methyl, ethyl).         Methylation, the addition of a methyl group, usually at lysine         or arginine residues is a type of alkylation. Demethylation         involves the removal of a methyl-group.     -   amidation at C-terminus     -   biotinylation, acylation of conserved lysine residues with a         biotin appendage     -   formylation     -   gamma-carboxylation dependent on Vitamin K     -   glutamylation, covalent linkage of glutamic acid residues to         tubulin and some other proteins by means of tubulin         polyglutamylase     -   glycosylation, the addition of a glycosyl group to either         asparagine, hydroxylysine, serine, or threonine, resulting in a         glycoprotein. Distinct from glycation, which is regarded as a         nonenzymatic attachment of sugars.     -   glycylation, covalent linkage of one to more than 40 glycine         residues to the tubulin C-terminal tail     -   heme moiety may be covalently attached     -   hydroxylation, is any chemical process that introduces one or         more hydroxyl groups (—OH) into a compound (or radical) thereby         oxidizing it. The principal residue to be hydroxylated is         Proline. The hydroxilation occurs at the C^(γ) atom, forming         hydroxyproline (Hyp). In some cases, proline may be hydroxylated         instead on its C^(β) atom. Lysine may also be hydroxylated on         its C^(δ) atom, forming hydroxylysine (Hyl).     -   iodination (e.g. of thyroid hormones)     -   isoprenylation, the addition of an isoprenoid group (e.g.         farnesol and geranylgeraniol)     -   lipoylation, attachment of a lipoate functionality, as in         prenylation, GPI anchor formation, myristoylation,         farnesylation, geranylation     -   nucleotides or derivatives thereof may be covalently attached,         as in ADP-ribosylation and flavin attachment     -   oxidation, lysine can be oxidized to aldehyde     -   pegylation, addition of poly-ethylen-glycol groups to a protein.         Typical reactive amino acids include lysine, cysteine,         histidine, arginine, aspartic acid, glutamic acid, serine,         threonine, tyrosine. The N-terminal amino group and the         C-terminal carboxylic acid can also be used     -   phosphatidylinositol may be covalently attached     -   phosphopantetheinylation, the addition of a         4′-phosphopantetheinyl moiety from coenzyme A, as in fatty acid,         polyketide, non-ribosomal peptide and leucine biosynthesis     -   phosphorylation, the addition of a phosphate group, usually to         serine, tyrosine, threonine or histidine     -   pyroglutamate formation as a result of N-terminal glutamine         self-attack, resulting in formation of a cyclic pyroglutamate         group.     -   racemization of proline by prolyl isomerase     -   tRNA-mediated addition of amino acids such as arginylation     -   sulfation, the addition of a sulfate group to a tyrosine.     -   Selenoylation (co-translational incorporation of selenium in         selenoproteins)         b) Involving Addition of Other Proteins or Peptides     -   ISGylation, the covalent linkage to the ISG15 protein         (Interferon-Stimulated Gene 15)     -   SUMOylation, the covalent linkage to the SUMO protein (Small         Ubiquitin-related MOdifier)     -   ubiquitination, the covalent linkage to the protein ubiquitin.         c) Involving Changing the Chemical Nature of Amino Acids     -   citrullination, or deimination the conversion of arginine to         citrulline     -   deamidation, the conversion of glutamine to glutamic acid or         asparagine to aspartic acid

The peptide modifications can occur as modification of a single amino acid or more than one i.e. in combinations. Modifications can be present on any position within the peptide i.e. on position 1, 2, 3, 4, 5, etc. for the entire length of the peptide.

Sources of Peptides

a) From Natural Sources

Peptides can be obtained from natural sources by enzymatic digestion or proteolysis of natural proteins or proteins derived by in vitro translation of mRNA. Peptides may also be eluted from the MHC binding groove.

b) From Recombinant Sources

1) As Monomeric or Multimeric Peptide

Alternatively peptides can be produced recombinantly by transfected cells either as monomeric antigenic peptides or as multimeric (contatemeric) antigenic peptides.

2) As Part of a Bigger Recombinant Protein

Binding peptides may also constitute a part of a bigger recombinant protein e.g. consisting of,

2a) For MHC Class 1 Binding Peptides,

Peptide-linker-β2m, β2m being full length or truncated;

Peptide-linker-MHC class 1 heavy chain, the heavy chain being full length or truncated. Most importantly the truncated class I heavy chain will consist of the extracellular part i.e the α1, α2, and a domains. The heavy chain fragment may also only contain the α1 and α2 domains, or α1 domain alone, or any fragment or full length β2m or heavy chain attached to a designer domain(s) or protein fragment(s).

2b) for MHC Class 2 Binding Peptides the Recombinant Construction can Consist of,

Peptide-linker-MHC class 2 □-chain, full length or truncated;

Peptide-linker-MHC class 2 □-chain, full length or truncated;

Peptide-linker-MHC class 2 □-chain-linker-MHC class 2 □-chain, both chains can be full length or truncated, truncation may involve, omission of □- and/or □-chain intermembrane domain, or omission of □- and/or □-chain intermembrane plus cytoplasmic domains. MHC class 2 part of the construction may consist of fused domains from NH2-terminal, MHC class 2 □/domain-MHC class 2 □/domain-constant □3 of MHC class 1, or alternatively of fused domains from NH2-terminal, MHC class 2 □1domain-MHC class 2 □1domain-constant □3 of MHC class 1. In both cases □2m will be associated non-covalently in the folded MHC complex. □2m can also be covalently associated in the folded MHC class 2 complex if the following constructs are used from NH2 terminal, MHC class 2 □1domain-MHC class 2 □1domain-constant □3 of MHC class 1-linker-□2m, or alternatively of fused domains from NH2-terminal, MHC class 2 □1domain-MHC class 2 □1domain-constant □3 of MHC class 1-linker-□2m; the construct may also consist of any of the above MHC class 2 constructs with added designer domain(s) or sequence(s). c) From Chemical Synthesis

MHC binding peptide may also be chemically synthesized by solid phase or fluid phase synthesis.

Loading of the Peptide into the MHCmer

Loading of the peptides into the MHCmer being either MHC class 1 or class 2 can be performed in a number of ways depending on the source of the peptide and the MHC. MHC class 2 molecules can in principle be loaded with peptides in similar ways as MHC class 1. However, due to complex instability the most successful approach have been to make the complexes recombinant in toto in eukaryotic cells from a gene construct encoding the following form □ chain-flexible linker-□ chain-flexible linker-peptide

a) During MHC Complex Folding

a1) As a Free Peptide

MHC class I molecules are most often loaded with peptide during assembly in vitro by the individual components in a folding reaction i.e. consisting of purified recombinant heavy chain □ with the purified recombinant □2 microglobulin and a peptide or a peptide mix.

a2) As Part of a Recombinant Protein Construct

Alternatively the peptide to be folded into the binding groove can be encoded together with e.g. the □ heavy chain or fragment hereof by a gene construct having the structure, heavy chain-flexible linker-peptide. This recombinant molecule is then folded in vitro with □2-microglobulin.

b) By Exchange Reaction

b1) In Solution

Loading of desired peptide can also be made by an in vitro exchange reaction where a peptide already in place in the binding groove are being exchanged by another peptide species.

b2) “In Situ”

Peptide exchange reactions can also take place when the parent molecule is attached to other molecules, structures, surfaces, artificial or natural membranes and nano-particles.

b3) By Aided Exchange

This method can be refined by making the parent construct with a peptide containing a meta-stable amino acid analog that is split by either light or chemically induction thereby leaving the parent structure free for access of the desired peptide in the binding groove.

b4) By In Vivo Loading

Loading of MHC class I and II molecules expressed on the cell surface with the desired peptides can be performed by an exchange reaction. Alternatively cells can be transfected by the peptides themselves or by the mother proteins that are then being processed leading to an in vivo analogous situation where the peptides are bound in the groove during the natural cause of MHC expression by the transfected cells. In the case of professional antigen presenting cells e.g. dendritic cells, macrophages, Langerhans cells, the proteins and peptides can be taken up by the cells themselves by phagocytosis and then bound to the MHC complexes the natural way and expressed on the cell surface in the correct MHC context.

Verification of Correctly Folded MHC-Peptide Complexes

Quantitative ELISA and Other Techniques to Quantify Correctly Folded MHC Complexes

When producing MHC multimers, it is desirable to determine the degree of correctly folded MHC.

The fraction or amount of functional and/or correctly folded MHC can be tested in a number of different ways, including:

-   -   Measurement of correctly folded MHC in a quantitative ELISA,         e.g. where the MHC bind to immobilized molecules recognizing the         correctly folded complex.     -   Measurement of functional MHC in an assay where the total         protein concentration is measured before functional MHC is         captured, by binding to e.g. immobilized TCR, and the excess,         non-bound protein are measured. If the dissociation constant for         the interaction is known, the amount of total and the amount of         non-bound protein can be determined. From these numbers, the         fraction of functional MHC complex can be determined.     -   Measurement of functional MHC complex by a non-denaturing         gel-shift assay, where functional MHC complexes bind to TCR (or         another molecule that recognize correctly folded MHC complex),         and thereby shifts the TCR to another position in the gel.         Multimerization Domain

A number of MHC complexes associate with a multimerization domain to form a MHC multimer. The size of the multimerization domain spans a wide range, from multimerisation domains based on small organic molecule scaffolds to large multimers based on a cellular structure or solid support. The multimerization domain may thus be based on different types of carriers or scaffolds, and likewise, the attachment of MHC complexes to the multimerization domain may involve covalent or non-covalent linkers.

Characteristics of different kinds of multimerization domains are described below.

Molecular Weight of Multimerization Domain.

-   -   In one embodiment the multimerization domain(s) in the present         invention is preferably less than 1,000 Da (small molecule         scaffold). Examples include short peptides (e.g. comprising 10         amino acids), and various small molecule scaffolds (e.g.         aromatic ring structures).     -   In another embodiment the multimerization domain(s) is         preferably between 1,000 Da and 10,000 Da (small molecule         scaffold, small peptides, small polymers). Examples include         polycyclic structures of both aliphatic and aromatic compounds,         peptides comprising e.g. 10-100 amino acids, and other polymers         such as dextran, polyethylenglycol, and polyureas.     -   In another embodiment the multimerization domain(s) is between         10,000 Da and 100,000 Da (Small molecule scaffold, polymers e.g.         dextran, streptavidin, IgG, pentamer structure). Examples         include proteins and large polypeptides, small molecule         scaffolds such as steroids, dextran, dimeric streptavidin, and         multi-subunit proteins such as used in Pentamers.     -   In another embodiment the multimerization domain(s) is         preferably between 100,000 Da and 1,000,000 Da (Small molecule         scaffold, polymers e.g. dextran, streptavidin, IgG, pentamer         structure). Typical examples include larger polymers such as         dextran (used in e.g. Dextramers), and streptavidin tetramers.     -   In another embodiment the multimerization domain(s) is         preferably larger than 1,000,000 Da (Small molecule scaffold,         polymers e.g. dextran, streptavidin, IgG, pentamer structure,         cells, liposomes, artificial lipid bilayers, polystyrene beads         and other beads. Most examples of this size involve cells or         cell-based structures such as micelles and liposomes, as well as         beads and other solid supports.

As mentioned elsewhere herein multimerisation domains can comprise carrier molecules, scaffolds or combinations of the two.

Type of Multimerization Domain.

In principle any kind of carrier or scaffold can be used as multimerization domain, including any kind of cell, polymer, protein or other molecular structure, or particles and solid supports. Below different types and specific examples of multimerization domains are listed.

-   -   Cell. Cells can be used as carriers. Cells can be either alive         and mitotic active, alive and mitotic inactive as a result of         irradiation or chemically treatment, or the cells may be dead.         The MHC expression may be natural (i.e. not stimulated) or may         be induced/stimulated by e.g. Inf-γ. Of special interest are         natural antigen presenting cells (APCs) such as dendritic cells,         macrophages, Kupfer cells, Langerhans cells, B-cells and any MHC         expressing cell either naturally expressing, being transfected         or being a hybridoma.     -   Cell-like structures. Cell-like carriers include membrane-based         structures carrying MHC-peptide complexes in their membranes         such as micelles, liposomes, and other structures of membranes,         and phages such as filamentous phages.     -   Solid support. Solid support includes beads, particulate matters         and other surfaces. A preferred embodiment include beads         (magnetic or non-magnetic beads) that carry electrophilic groups         e.g. divinyl sulfone activated polysaccharide, polystyrene beads         that have been functionalized with tosyl-activated esters,         magnetic polystyrene beads functionalized with tosyl-activated         esters), and where MHC complexes may be covalently immobilized         to these by reaction of nucleophiles comprised within the MHC         complex with the electrophiles of the beads. Beads may be made         of sepharose, sephacryl, polystyrene, agarose, polysaccharide,         polycarbamate or any other kind of beads that can be suspended         in aqueous buffer.     -   Another embodiment includes surfaces, i.e. solid supports and         particles carrying immobilized MHC complexes on the surface. Of         special interest are wells of a microtiter plate or other plate         formats, reagent tubes, glass slides or other supports for use         in microarray analysis, tubings or channels of micro fluidic         chambers or devices, Biacore chips and beads     -   Molecule. Multimerization domains may also be molecules or         complexes of molecules held together by non-covalent bonds. The         molecules constituting the multimerization domain can be small         organic molecules or large polymers, and may be flexible linear         molecules or rigid, globular structures such as e.g. proteins.         Different kinds of molecules used in multimerization domains are         described below.         -   Small organic molecules. Small organic molecules here             includes steroids, peptides, linear or cyclic structures,             and aromatic or aliphatic structures, and many others. The             prototypical small organic scaffold is a functionalized             benzene ring, i.e. a benzene ring functionalized with a             number of reactive groups such as amines, to which a number             of MHC molecules may be covalently linked. However, the             types of reactive groups constituting the linker connecting             the MHC complex and the multimerization domain, as well as             the type of scaffold structure, can be chosen from a long             list of chemical structures. A non-comprehensive list of             scaffold structures are listed below.         -   Typical scaffolds include aromatic structures,             benzodiazepines, hydantoins, piperazines, indoles, furans,             thiazoles, steroids, diketopiperazines, morpholines,             tropanes, coumarines, qinolines, pyrroles, oxazoles, amino             acid precursors, cyclic or aromatic ring structures, and             many others.         -   Typical carriers include linear and branched polymers such             as peptides, polysaccharides, nucleic acids, and many             others. Multimerization domains based on small organic or             polymer molecules thus include a wealth of different             structures, including small compact molecules, linear             structures, polymers, polypeptides, polyureas,             polycarbamates, cyclic structures, natural compound             derivatives, alpha-, beta-, gamma-, and omega-peptides,             mono-, di- and tri-substituted peptides, L- and D-form             peptides, cyclohexane- and cyclopentane-backbone modified             beta-peptides, vinylogous polypeptides, glycopolypeptides,             polyamides, vinylogous sulfonamide peptide,             Polysulfonamide-conjugated peptide (i.e., having prosthetic             groups), Polyesters, Polysaccharides such as dextran and             aminodextran, polycarbamates, polycarbonates, polyureas,             poly-peptidylphosphonates, Azatides, peptoids (oligo             N-substituted glycines), Polyethers, ethoxyformacetal             oligomers, poly-thioethers, polyethylene, glycols (PEG),             polyethylenes, polydisulfides, polyarylene sulfides,             Polynucleotides, PNAs, LNAs, Morpholinos, oligo pyrrolinone,             polyoximes, Polyimines, Polyethyleneimine, Polyacetates,             Polystyrenes, Polyacetylene, Polyvinyl, Lipids,             Phospholipids, Glycolipids, polycycles, (aliphatic),             polycycles (aromatic), polyheterocycles, Proteoglycan,             Polysiloxanes, Polyisocyanides, Polyisocyanates,             polymethacrylates, Monofunctional, Difunctional,             Trifunctional and Oligofunctional open-chain hydrocarbons,             Monofunctional, Difunctional, Trifunctional and             Oligofunctional Nonaromat Carbocycles, Monocyclic, Bicyclic,             Tricyclic and Polycyclic Hydrocarbons, Bridged Polycyclic             Hydrocarbones, Monofunctional, Difunctional, Trifunctional             and Oligofunctional Nonaromatic, Heterocycles, Monocyclic,             Bicyclic, Tricyclic and Polycyclic Heterocycles, bridged             Polycyclic Heterocycles, Monofunctional, Difunctional,             Trifunctional and Oligofunctional Aromatic Carbocycles,             Monocyclic, Bicyclic, Tricyclic and Polycyclic Aromatic             Carbocycles, Monofunctional, Difunctional, Trifunctional and             Oligofunctional Aromatic Hetero-cycles. Monocyclic,             Bicyclic, Tricyclic and Polycyclic Heterocycles. Chelates,             fullerenes, and any combination of the above and many             others.         -   Biological polymers. Biological molecules here include             peptides, proteins (including antibodies, coiled-coil             helices, streptavidin and many others), nucleic acids such             as DNA and RNA, and polysaccharides such as dextran. The             biological polymers may be reacted with MHC complexes (e.g.             a number of MHC complexes chemically coupled to e.g. the             amino groups of a protein), or may be linked through e.g.             DNA duplex formation between a carrier DNA molecule and a             number of DNA oligonucleotides each coupled to a MHC             complex. Another type of multimerization domain based on a             biological polymer is the streptavidin-based tetramer, where             a streptavidin binds up to four biotinylated MHC complexes,             as described above (see Background of the invention).         -   Self-assembling multimeric structures. Several examples of             commercial MHC multimers exist where the multimer is formed             through self-assembling. Thus, the Pentamers are formed             through formation of a coiled-coil structure that holds             together 5 MHC complexes in an apparently planar structure.             In a similar way, the Streptamers are based on the             Streptactin protein which oligomerizes to form a MHC             multimer comprising several MHC complexes (see Background of             the invention).

In the following, alternative ways to make MHC multimers based on a molecule multimerization domain are described. They involve one or more of the abovementioned types of multimerization domains.

MHC dextramers can be made by coupling MHC complexes to dextran via a streptavidin-biotin interaction. In principle, biotin-streptavidin can be replaced by any dimerization domain, where one half of the dimerization domain is coupled to the MHC-peptide complex and the other half is coupled to dextran. For example, an acidic helix (one half of a coiled-coil dimer) is coupled or fused to MHC, and a basic helix (other half of a coiled-coil dimmer) is coupled to dextran. Mixing the two results in MHC binding to dextran by forming the acid/base coiled-coil structure.

Antibodies can be used as scaffolds by using their capacity to bind to a carefully selected antigen found naturally or added as a tag to a part of the MHC molecule not involved in peptide binding. For example, IgG and IgE will be able to bind two MHC molecules, IgM having a pentameric structure will be able to bind 10 MHC molecules. The antibodies can be full-length or truncated; a standard antibody-fragment includes the Fab2 fragment.

Peptides involved in coiled-coil structures can act as scaffold by making stable dimeric, trimeric, tetrameric and pentameric interactions. Examples hereof are the Fos-Jun heterodimeric coiled coil, the E. coli homo-trimeric coiled-coil domain Lpp-56, the engineered Trp-zipper protein forming a discrete, stable, α-helical pentamer in water at physiological pH.

Further examples of suitable scaffolds, carriers and linkers are streptavidin (SA) and avidin and derivatives thereof, biotin, immunoglobulins, antibodies (monoclonal, polyclonal, and recombinant), antibody fragments and derivatives thereof, leucine zipper domain of AP-1 (jun and fos), hexa-his (metal chelate moiety), hexa-hat GST (glutathione S-tranferase), glutathione, Calmodulin-binding peptide (CBP), Strep-tag, Cellulose Binding Domain, Maltose Binding Protein, S-Peptide Tag, Chitin Binding Tag, Immuno-reactive Epitopes, Epitope Tags, E2Tag, HA Epitope Tag, Myc Epitope, FLAG Epitope, AU1 and AU5 Epitopes, Glu-Glu Epitope, KT3 Epitope, IRS Epitope, Btag Epitope, Protein Kinase-C Epitope, VSV Epitope, lectins that mediate binding to a diversity of compounds, including carbohydrates, lipids and proteins, e.g. Con A (Canavalia ensiformis) or WGA (wheat germ agglutinin) and tetranectin or Protein A or G (antibody affinity). Combinations of such binding entities are also comprised. Non-limiting examples are streptavidin-biotin and jun-fos. In particular, when the MHC molecule is tagged, the binding entity may be an “anti-tag”. By “anti-tag” is meant an antibody binding to the tag, or any other molecule capable of binding to such tag.

MHC complexes can be multimerized by other means than coupling or binding to a multimerization domain. Thus, the multimerization domain may be formed during the multimerization of MHCs. One such method is to extend the bound antigenic peptide with dimerization domains. One end of the antigenic peptide is extended with dimerization domain A (e.g. acidic helix, half of a coiled-coil dimer) and the other end is extended with dimerization domain B (e.g. basic helix, other half of a coiled-coil dimer). When MHC complexes are loaded/mixed with these extended peptides the following multimer structure will be formed: A-MHC-BA-MHC-BA-MHC-B etc. The antigenic peptides in the mixture can either be identical or a mixture of peptides with comparable extended dimerization domains. Alternatively both ends of a peptide are extended with the same dimerization domain A and another peptide (same amino acid sequence or a different amino acid sequence) is extended with dimerization domain B. When MHC and peptides are mixed the following structures are formed: A-MHC-AB-MHC-BA-MHC-AB-MHC-B etc. Multimerization of MHC complexes by extension of peptides are restricted to MHC II molecules since the peptide binding groove of MHC I molecules is typically closed in both ends thereby limiting the size of peptide that can be embedded in the groove, and therefore preventing the peptide from extending out of the groove.

Another multimerization approach applicable to both MHC I and MHC II complexes is based on extension of N- and C-terminal of the MHC complex. For example the N-terminal of the MHC complex is extended with dimerization domain A and the C-terminal is extended with dimerization domain B. When MHC complexes are incubated together they pair with each other and form multimers like: A-MHC-BA-MHC-BA-MHC-BA-MHC-B etc. Alternatively the N-terminal and the C-terminal of a MHC complex are both extended with dimerization domain A and the N-terminal and C-terminal of another preparation of MHC complex (either the same or a different MHC) are extended with dimerization domain B. When these two types of MHC complexes are incubated together multimers will be formed: A-MHC-AB-MHC-BA-MHC-AB-MHC-B etc.

In all the above-described examples the extension can be either chemically coupled to the peptide/MHC complex or introduced as extension by gene fusion.

Dimerization domain AB can be any molecule pair able to bind to each other, such as acid/base coiled-coil helices, antibody-antigen, DNA-DNA, PNA-PNA, DNA-PNA, DNA-RNA, LNA-DNA, leucine zipper e.g. Fos/Jun, streptavidin-biotin and other molecule pairs as described elsewhere herein.

Linker Molecules.

A number of MHC complexes associate with a multimerization domain to form a MHC multimer. The attachment of MHC complexes to the multimerization domain may involve covalent or non-covalent linkers, and may involve small reactive groups as well as large protein-protein interactions.

The coupling of multimerization domains and MHC complexes involve the association of an entity X (attached to or part of the multimerization domain) and an entity Y (attached to or part of the MHC complex). Thus, the linker that connects the multimerization domain and the MHC complex comprises an XY portion.

-   -   Covalent linker. The XY linkage can be covalent, in which case X         and Y are reactive groups. In this case, X can be a nucleophilic         group (such as —NH₂, —OH, —SH, —NH—NH₂), and Y an electrophilic         group (such as CHO, COOH, CO) that react to form a covalent bond         XY; or Y can be a nucleophilic group and X an electrophilic         group that react to form a covalent bond XY. Other possibilities         exist, e.g either of the reactive groups can be a radical,         capable of reacting with the other reactive group. A number of         reactive groups X and Y, and the bonds that are formed upon         reaction of X and Y, are shown in FIG. 5.     -   X and Y can be reactive groups naturally comprised within the         multimerization domain and/or the MHC complex, or they can be         artificially added reactive groups. Thus, linkers containing         reactive groups can be linked to either of the multimerization         domain and MHC complex; subsequently the introduced reactive         group(s) can be used to covalently link the multimerization         domain and MHC complex.     -   Example natural reactive groups of MHC complexes include amino         acid side chains comprising —NH₂, —OH, —SH, and —NH—. Example         natural reactive groups of multimerization domains include         hydroxyls of polysaccharides such as dextrans, but also include         amino acid side chains comprising —NH₂, —OH, —SH, and —NH— of         polypeptides, when the polypeptide is used as a multimerization         domain. In some MHC multimers, one of the polypeptides of the         MHC complex (i.e. the β2M, heavy chain or the antigenic peptide)         is linked by a protein fusion to the multimerization domain.         Thus, during the translation of the fusion protein, an acyl         group (reactive group X or Y) and an amino group (reactive group         Y or X) react to form an amide bond. Example MHC multimers where         the bond between the multimerization domain and the MHC complex         is covalent and results from reaction between natural reactive         groups, include MHC-pentamers (described in US         patent 2004209295) and MHC-dimers, where the linkage between         multimerization domain and MHC complex is in both cases         generated during the translation of the fusion protein.     -   Example artificial reactive groups include reactive groups that         are attached to the multimerization domain or MHC complex,         through association of a linker molecule comprising the reactive         group. The activation of dextran by reaction of the dextran         hydroxyls with divinyl sulfone, introduces a reactive vinyl         group that can react with e.g. amines of the MHC complex, to         form an amine that now links the multimerization domain (the         dextran polymer) and the MHC complex. An alternative activation         of the dextran multimerization domain involves a multistep         reaction that results in the decoration of the dextran with         maleimide groups, as described in the patent Siiman et al. U.S.         Pat. No. 6,387,622. In this approach, the amino groups of MHC         complexes are converted to —SH groups, capable of reacting with         the maleimide groups of the activated dextran. Thus, in the         latter example, both the reactive group of the multimerization         domain (the maleimide) and the reactive group of the MHC complex         (the thiol) are artificially introduced.     -   Sometimes activating reagents are used in order to make the         reactive groups more reactive. For example, acids such as         glutamate or aspartate can be converted to activated esters by         addition of e.g. carbodiimid and NHS or nitrophenol, or by         converting the acid moiety to a tosyl-activated ester. The         activated ester reacts efficiently with a nucleophile such as         —NH₂, —SH, —OH, etc.     -   For the purpose of this invention, the multimerization domains         (including small organic scaffold molecules, proteins, protein         complexes, polymers, beads, liposomes, micelles, cells) that         form a covalent bond with the MHC complexes can be divided into         separate groups, depending on the nature of the reactive group         that the multimerization domain contains. One group comprise         multimerization domains that carry nucleophilic groups (e.g.         —NH₂, —OH, —SH, —CN, —NH—NH₂), exemplified by polysaccharides,         polypeptides containing e.g. lysine, serine, and cysteine;         another group of multimerization domains carry electrophilic         groups (e.g. —COOH, —CHO, —CO, NHS-ester, tosyl-activated ester,         and other activated esters, acid-anhydrides), exemplified by         polypeptides containing e.g. glutamate and aspartate, or vinyl         sulfone activated dextran; yet another group of multimerization         domains carry radicals or conjugated double bonds.     -   The multimerization domains appropriate for this invention thus         include those that contain any of the reactive groups shown in         FIG. 5 or that can react with other reactive groups to form the         bonds shown in FIG. 5.     -   Likewise, MHC complexes can be divided into separate groups,         depending on the nature of the reactive group comprised within         the MHC complex. One group comprise MHCs that carry nucleophilic         groups (e.g. —NH₂, —OH, —SH, —CN, —NH—NH₂), e.g. lysine, serine,         and cysteine; another group of MHCs carry electrophilic groups         (e.g. —COOH, —CHO, —CO, NHS-ester, tosyl-activated ester, and         other activated esters, acid-anhydrides), exemplified by e.g.         glutamate and aspartate; yet another group of MHCs carry         radicals or conjugated double bonds.     -   The reactive groups of the MHC complex are either carried by the         amino acids of the MHC-peptide complex (and may be comprised by         any of the peptides of the MHC-peptide complex, including the         antigenic peptide), or alternatively, the reactive group of the         MHC complex has been introduced by covalent or non-covalent         attachment of a molecule containing the appropriate reactive         group.     -   Preferred reactive groups in this regard include —CSO₂OH,         phenylchloride, —SH, —SS, aldehydes, hydroxyls, isocyanate,         thiols, amines, esters, thioesters, carboxylic acids, triple         bonds, double bonds, ethers, acid chlorides, phosphates,         imidazoles, halogenated aromatic rings, any precursors thereof,         or any protected reactive groups, and many others. Example pairs         of reactive groups, and the resulting bonds formed, are shown in         FIG. 5.     -   Reactions that may be employed include acylation (formation of         amide, pyrazolone, isoxazolone, pyrimidine, comarine,         quinolinon, phthalhydrazide, diketopiperazine, benzodiazepinone,         and hydantoin), alkylation, vinylation, disulfide formation,         Wittig reaction, Horner-Wittig-Emmans reaction, arylation         (formation of biaryl or vinylarene), condensation reactions,         cycloadditions ((2+4), (3+2)), addition to carbon-carbon         multiplebonds, cycloaddition to multiple bonds, addition to         carbon-hetero multiple bonds, nucleophilic aromatic         substitution, transition metal catalyzed reactions, and may         involve formation of ethers, thioethers, secondary amines,         tertiary amines, beta-hydroxy ethers, beta-hydroxy thioethers,         beta-hydroxy amines, beta-amino ethers, amides, thioamides,         oximes, sulfonamides, di- and tri-functional compounds,         substituted aromatic compounds, vinyl substituted aromatic         compounds, alkyn substituted aromatic compounds, biaryl         compounds, hydrazines, hydroxylamine ethers, substituted         cycloalkenes, substituted cyclodienes, substituted 1, 2, 3         triazoles, substituted cycloalkenes, beta-hydroxy ketones,         beta-hydroxy aldehydes, vinyl ketones, vinyl aldehydes,         substituted alkenes, substituted alkenes, substituted amines,         and many others.     -   MHC dextramers can be made by covalent coupling of MHC complexes         to the dextran backbone, e.g. by chemical coupling of MHC         complexes to dextran backbones. The MHC complexes can be coupled         through either heavy chain or β2-microglobulin if the MHC         complexes are MHC I or through α-chain or β-chain if the MHC         complexes are MHC II. MHC complexes can be coupled as folded         complexes comprising heavy chain/beta2microglobulin or         α-chain/β-chain or either combination together with peptide in         the peptide-binding cleft. Alternatively either of the protein         chains can be coupled to dextran and then folded in vitro         together with the other chain of the MHC complex not coupled to         dextran and together with peptide. Direct coupling of MHC         complexes to dextran multimerization domain can be via an amino         group or via a sulphide group. Either group can be a natural         component of the MHC complex or attached to the MHC complex         chemically. Alternatively, a cysteine may be introduced into the         genes of either chain of the MHC complex.     -   Another way to covalently link MHC complexes to dextran         multimerization domains is to use the antigenic peptide as a         linker between MHC and dextran. Linker containing antigenic         peptide at one end is coupled to dextran. Antigenic peptide here         means a peptide able to bind MHC complexes in the         peptide-binding cleft. As an example, 10 or more antigenic         peptides may be coupled to one dextran molecule. When MHC         complexes are added to such peptide-dextran construct the MHC         complexes will bind the antigenic peptides and thereby         MHC-peptide complexes are displayed around the dextran         multimerization domain. The antigenic peptides can be identical         or different from each other. Similarly MHC complexes can be         either identical or different from each other as long as they         are capable of binding one or more of the peptides on the         dextran multimerization domain.     -   Non-covalent linker. The linker that connects the         multimerization domain and the MHC complex comprises an XY         portion. Above different kinds of covalent linkages XY were         described. However, the XY linkage can also be non-covalent.     -   Non-covalent XY linkages can comprise natural dimerization pairs         such as antigen-antibody pairs, DNA-DNA interactions, or can         include natural interactions between small molecules and         proteins, e.g. between biotin and streptavidin. Artificial XY         examples include XY pairs such as His₆ tag (X) interacting with         Ni-NTA (Y) and PNA-PNA interactions.     -   Protein-protein interactions. The non-covalent linker may         comprise a complex of two or more polypeptides or proteins, held         together by non-covalent interactions. Example polypeptides and         proteins belonging to this group include Fos/Jun, Acid/Base         coiled coil structure, antibody/antigen (where the antigen is a         peptide), and many others.     -   A preferred embodiment involving non-covalent interactions         between polypeptides and/or proteins are represented by the         Pentamer structure described in US patent 2004209295.     -   Another preferred embodiment involves the use of antibodies,         with affinity for the surface of MHC opposite to the         peptide-binding groove. Thus, an anti-MHC antibody, with its two         binding site, will bind two MHC complexes and in this way         generate a bivalent MHC multimer. In addition, the antibody can         stabilize the MHC complex through the binding interactions. This         is particularly relevant for MHC class II complexes, as these         are less stable than class I MHC complexes.     -   Polynucleotide-polynucleotide interactions. The non-covalent         linker may comprise nucleotides that interact non-covalently.         Example interactions include PNA/PNA, DNA/DNA, RNA/RNA, LNA/DNA,         and any other nucleic acid duplex structure, and any combination         of such natural and unnatural polynucleotides such as DNA/PNA,         RNA/DNA, and PNA/LNA.     -   Protein-small molecule interactions. The non-covalent linker may         comprise a macromolecule (e.g. protein, polynucleotide) and a         small molecule ligand of the macromolecule. The interaction may         be natural (i.e., found in Nature, such as the         Streptavidin/biotin interaction) or non-natural (e.g. His-tag         peptide/Ni-NTA interaction). Example interactions include         Streptavidin/biotin and anti-biotin antibody/biotin.     -   Combinations—non-covalent linker molecules. Other combinations         of proteins, polynucleotides, small organic molecules, and other         molecules, may be used to link the MHC to the multimerization         domain. These other combinations include protein-DNA         interactions (e.g. DNA binding protein such as the gene         regulatory protein CRP interacting with its DNA recognition         sequence), RNA aptamer-protein interactions (e.g. RNA aptamer         specific for growth hormone interacting with growth hormone)     -   Synthetic molecule-synthetic molecule interaction. The         non-covalent linker may comprise a complex of two or more         organic molecules, held together by non-covalent interactions.         Example interactions are two chelate molecules binding to the         same metal ion (e.g. EDTA-Ni⁺⁺-NTA), or a short polyhistidine         peptide (e.g. His₆) bound to NTA-Ni⁺⁺.

In another preferred embodiment the multimerization domain is a bead. The bead is covalently or non-covalently coated with MHC multimers or single MHC complexes, through non-cleavable or cleavable linkers. As an example, the bead can be coated with streptavidin monomers, which in turn are associated with biotinylated MHC complexes; or the bead can be coated with streptavidin tetramers, each of which are associated with 0, 1, 2, 3, or 4 biotinylated MHC complexes; or the bead can be coated with MHC-dextramers where e.g. the reactive groups of the MHC-dextramer (e.g. the divinyl sulfone-activated dextran backbone) has reacted with nucleophilic groups on the bead, to form a covalent linkage between the dextran of the dextramer and the beads.

In another preferred embodiment, the MHC multimers described above (e.g. where the multimerization domain is a bead) further contains a flexible or rigid, and water soluble, linker that allows for the immobilized MHC complexes to interact efficiently with cells, such as T-cells with affinity for the MHC complexes. In yet another embodiment, the linker is cleavable, allowing for release of the MHC complexes from the bead. If T-cells have been immobilized, by binding to the MHC complexes, the T-cells can very gently be released by cleavage of this cleavable linker Appropriate cleavable linkers are shown in FIG. 6. Most preferably, the linker is cleaved at physiological conditions, allowing for the integrity of the isolated cells.

Further examples of linker molecules that may be employed in the present invention include Calmodulin-binding peptide (CBP), 6×HIS, Protein A, Protein G, biotin, Avidine, Streptavidine, Strep-tag, Cellulose Binding Domain, Maltose Binding Protein, S-Peptide Tag, Chitin Binding Tag, Immuno-reactive Epitopes, Epitope Tags, GST tagged proteins, E2Tag, HA Epitope Tag, Myc Epitope, FLAG Epitope, AU1 and AU5 Epitopes, Glu-Glu Epitope, KT3 Epitope, IRS Epitope, Btag Epitope, Protein Kinase-C Epitope, VSV Epitope.

The list of dimerization- and multimerization domains, described elsewhere in this document, define alternative non-covalent linkers between the multimerization domain and the MHC complex.

The abovementioned dimerization- and multimerization domains represent specific binding interactions. Another type of non-covalent interactions involves the non-specific adsorption of e.g. proteins onto surfaces. As an example, the non-covalent adsorption of proteins onto glass beads represents this class of XY interactions. Likewise, the interaction of MHC complexes (comprising full-length polypeptide chains, including the transmembrane portion) with the cell membrane of for example dendritic cells is an example of a non-covalent, primarily non-specific XY interaction.

In some of the abovementioned embodiments, several multimerization domains (e.g. streptavidin tetramers bound to biotinylated MHC complexes) are linked to another multimerization domain (e.g. the bead). For the purpose of this invention we shall call both the smaller and the bigger multimerization domain, as well as the combined multimerization domain, for multimerization domain

Additional Features of Product

Additional components may be coupled to carrier or added as individual components not coupled to carrier

Attachment of Biologically Active Molecules to MHC Multimers

Engagement of MHC complex to the specific T cell receptor leads to a signaling cascade in the T cell. However, T-cells normally respond to a single signal stimulus by going into apoptosis. T cells needs a second signal in order to become activated and start development into a specific activation state e.g. become an active cytotoxic T cell, helper T cell or regulatory T cell.

It is to be understood that the MHC multimer of the invention may further comprise one or more additional substituents. The definition of the terms “one or more”, “a plurality”, “a”, “an”, and “the” also apply here. Such biologically active molecules may be attached to the construct in order to affect the characteristics of the constructs, e.g. with respect to binding properties, effects, MHC molecule specificities, solubility, stability, or detectability. For instance, spacing could be provided between the MHC complexes, one or both chromophores of a Fluorescence Resonance Energy Transfer (FRET) donor/acceptor pair could be inserted, functional groups could be attached, or groups having a biological activity could be attached.

MHC multimers can be covalently or non-covalently associated with various molecules: having adjuvant effects; being immune targets e.g. antigens; having biological activity e.g. enzymes, regulators of receptor activity, receptor ligands, immune potentiators, drugs, toxins, co-receptors, proteins and peptides in general; sugar moieties; lipid groups; nucleic acids including siRNA; nano particles; small molecules. In the following these molecules are collectively called biologically active molecules. Such molecules can be attached to the MHC multimer using the same principles as those described for attachment of MHC complexes to multimerisation domains as described elsewhere herein. In brief, attachment can be done by chemical reactions between reactive groups on the biologically active molecule and reactive groups of the multimerisation domain and/or between reactive groups on the biologically active molecule and reactive groups of the MHC-peptide complex. Alternatively, attachment is done by non-covalent interaction between part of the multimerisation domain and part of the biological active molecule or between part of the MHC-peptide complex and part of the biological active molecule. In both covalent and non-covalent attachment of the biologically molecule to the multimerisation domain a linker molecule can connect the two. The linker molecule can be covalent or non-covalent attached to both molecules. Examples of linker molecules are described elsewhere herein. Some of the MHCmer structures better allows these kind of modifications than others.

Biological active molecules can be attached repetitively aiding to recognition by and stimulation of the innate immune system via Toll or other receptors.

MHC multimers carrying one or more additional groups can be used as therapeutic or vaccine reagents.

In particular, the biologically active molecule may be selected from

proteins such as MHC Class I-like proteins like MIC A, MIC B, CD1d, HLA E, HLA F, HLA G, HLA H, ULBP-1, ULBP-2, and ULBP-3,

co-stimulatory molecules such as CD2, CD3, CD4, CD5, CD8, CD9, CD27, CD28, CD30, CD69, CD134 (OX40), CD137 (4-1BB), CD147, CDw150 (SLAM), CD152 (CTLA-4), CD153 (CD30L), CD40L (CD154), NKG2D, ICOS, HVEM, HLA Class II, PD-1, Fas (CD95), FasL expressed on T and/or NK cells, CD40, CD48, CD58, CD70, CD72, B7.1 (CD80), B7.2 (CD86), B7RP-1, B7-H3, PD-L1, PD-L2, CD134L, CD137L, ICOSL, LIGHT expressed on APC and/or tumour cells, cell modulating molecules such as CD16, NKp30, NKp44, NKp46, NKp80, 2B4, KIR, LIR, CD94/NKG2A, CD94/NKG2C expressed on NK cells, IFN-alpha, IFN-beta, IFN-gamma, IL-1, IL-2, IL-3, IL-4, IL-6, IL-7, IL-8, IL-10, IL-11, IL-12, IL-15, CSFs (colony-stimulating factors), vitamin D3, IL-2 toxins, cyclosporin, FK-506, rapamycin, TGF-beta, clotrimazole, nitrendipine, and charybdotoxin, accessory molecules such as LFA-1, CD11a/18, CD54 (ICAM-1), CD106 (VCAM), and CD49a,b,c,d,e,f/CD29 (VLA-4), adhesion molecules such as ICAM-1, ICAM-2, GlyCAM-1, CD34, anti-LFA-1, anti-CD44, anti-beta7, chemokines, CXCR4, CCR5, anti-selectin L, anti-selectin E, and anti-selectin P, toxic molecules selected from toxins, enzymes, antibodies, radioisotopes, chemiluminescent substances, bioluminescent substances, polymers, metal particles, and haptens, such as cyclophosphamide, methrotrexate, Azathioprine, mizoribine, 15-deoxuspergualin, neomycin, staurosporine, genestein, herbimycin A, Pseudomonas exotoxin A, saporin, Rituxan, Ricin, gemtuzumab ozogamicin, Shiga toxin, heavy metals like inorganic and organic mercurials, and FN18-CRM9, radioisotopes such as incorporated isotopes of iodide, cobalt, selenium, tritium, and phosphor, and haptens such as DNP, and digoxiginin, and combinations of any of the foregoing, as well as antibodies (monoclonal, polyclonal, and recombinant) to the foregoing, where relevant. Antibody derivatives or fragments thereof may also be used. Design and Generation of Product to be Used for Immune Monitoring, Diagnosis, Therapy or Vaccination

The product of the present invention may be used for immune monitoring, diagnosis, therapy and/or vaccination. Generation of a useful product includes the following basic steps:

-   -   1. Design of antigenic peptides     -   2. Choice of MHC allele     -   3. Generation of product     -   4. Validation and optimization of product

In the following strategies for generation of products are given:

How to Make a MHC Multimer Diagnostic or Immune Monitoring Reagent

-   -   1. Identify disease of interest. Most relevant diseases in this         regard are infectious-, cancer-, auto immune-, transplantation-,         or immuno-suppression-related diseases.     -   2. Identify relevant protein targets. This may be individual         proteins, a group of proteins from a given tissue or all or         subgroups of proteins from a complete organism.     -   3. Identify the protein sequence. Amino acid sequences can be         directly found in databases or deduced from gene- or mRNA         sequence e.g. using the following link         www.ncbi.nlm.nih.gov/Genbank/index.html. If not in databases         relevant proteins or genes encoding relevant proteins may be         isolated and sequenced. In some cases only DNA sequences will be         available without knowing which part of the sequence is protein         coding. Then DNA sequence is translated into amino acid sequence         in all reading frames.     -   4. Choose MHC allele. Decide on needed MHC allele population         coverage. If a broad coverage of a given population is needed         (i.e. when a generally applicable reagent is sought) the most         frequently expressed MHC alleles by the population of interest         may be chosen e.g. using the database         www.allelefrequencies.net/test/default1.asp or         epitope.liai.org:8080/tools/population/iedb_input.         -   In case of personalized medicine the patient is tissue typed             (HLA type) and then MHC alleles may be selected according to             that.     -   5. Run the general peptide epitope generator program described         elsewhere herein on all selected amino acid sequences from step         3, thereby generating all possible epitopes of defined length         (8, 9, 10 and/or 11′mers). This procedure is particularly useful         when the amino acid sequence is derived from a DNA sequence not         knowing the protein encoding areas.     -   6. If searching for broadly applicable epitope sequences, a good         alternative to step 5 is to run the “intelligent” peptide         epitope prediction programs on the selected amino acid sequences         of step 3 using the selected MHC alleles from step 4 e.g. using         epitope prediction programs like www.syfpeithi.de/,         www.cbs.dtu.dk/services/NetMHC/, and         www.cbs.dtu.dk/services/NetMHCII/.     -   7. If searching for broadly applicable epitope sequences, select         the best peptide epitopes (the epitopes with highest binding         score) for the chosen MHC alleles and run them through the BLAST         program (www.ncbi.nlm.nih.gov/blast/Blast.cgi) to validate the         uniqueness of the peptides. If the peptide sequences are present         in other species, evaluate the potential risk of disease states         caused by the non-relevant species in relation to causing false         positive results. If considered being a potential problem for         evaluating the future analysis outcome, leave out the peptide.         In general, favour unique peptide sequences only present in the         selected protein.     -   8. Make selected peptides as described elsewhere herein, and         optionally test for binding to the desired MHC alleles by e.g in         vitro folding, peptide exchange of already preloaded MHC         complexes or another method able to test of peptide binding to         MHC I or II molecules.     -   9. Generate desired MHC multimer as described elsewhere herein         and test efficacy in detecting specific T-cells using methods         described in the section “Detection”.         -   The MHC multimer reagents may be used in a diagnostic             procedure or kit for testing patient and control samples             e.g. by flow cytometry, immune histochemistry, Elispot or             other methods as described herein.             How to Make a MHC Multimer Therapeutic Reagent     -   1. As step 1-8 above for diagnostic reagent.     -   9. Select additional molecules (e.g. biologically active         molecules, toxins) to attach to the MHC multimer as described         elsewhere herein. The additional molecules can have different         functionalities as e.g. adjuvants, specific activators, toxins         etc.     -   10. Test the therapeutic reagent following general guidelines     -   11. Use for therapy

Processes Involving MHC Multimers

Thus, the present invention relates to methods for detecting the presence of MHC recognising cells in a sample comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC multimer as defined above, and

(c) determining any binding of the MHC multimer, which binding indicates the presence of MHC recognising cells.

Such methods are a powerful tool in diagnosing various diseases. Establishing a diagnosis is important in several ways. A diagnosis gives information about the disease, thus the patient can be offered a suitable treatment regime. Also, establishing a more specific diagnosis may give important information about a subtype of a disease for which a particular treatment will be beneficial (i.e. various subtypes of diseases may involve display of different peptides which are recognised by MHC recognising cells, and thus treatment can be targeted effectively against a particular subtype). In this way, it may also be possible to gain information about aberrant cells, which emerge through the progress of the disease or condition, or to investigate whether and how T-cell specificity is affected. The binding of the MHC multimer makes possible these options, since the binding is indicative for the presence of the MHC recognising cells in the sample, and accordingly the presence of MHC multimeres displaying the peptide.

The present invention also relates to methods for monitoring MHC recognising cells comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC complex as defined above, and

(c) determining any binding of the MHC multimer, thereby monitoring MHC recognising cells.

Such methods are a powerful tool in monitoring the progress of a disease, e.g. to closely follow the effect of a treatment. The method can i.a. be used to manage or control the disease in a better way, to ensure the patient receives the optimum treatment regime, to adjust the treatment, to confirm remission or recurrence, and to ensure the patient is not treated with a medicament which does not cure or alleviate the disease. In this way, it may also be possible to monitor aberrant cells, which emerge through the progress of the disease or condition, or to investigate whether and how T-cell specificity is affected during treatment. The binding of the MHC multimer makes possible these options, since the binding is indicative for the presence of the MHC recognising cells in the sample, and accordingly the presence of MHC multimers displaying the peptide.

The present invention also relates to methods for establishing a prognosis of a disease involving MHC recognising cells comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC multimer as defined above, and

(c) determining any binding of the MHC multimer, thereby establishing a prognosis of a disease involving MHC recognising cells.

Such methods are a valuable tool in order to manage diseases, i.a. to ensure the patient is not treated without effect, to ensure the disease is treated in the optimum way, and to predict the chances of survival or cure. In this way, it may also be possible to gain information about aberrant cells, which emerge through the progress of the disease or condition, or to investigate whether and how T-cell specificity is affected, thereby being able to establish a prognosis. The binding of the MHC multimer makes possible these options, since the binding is indicative for the presence of the MHC recognising cells in the sample, and accordingly the presence of MHC complexes displaying the peptide.

The present invention also relates to methods for determining the status of a disease involving MHC recognising cells comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC complex as defined above, and

(c) determining any binding of the MHC complex, thereby determining the status of a disease involving MHC recognising cells.

Such methods are a valuable tool in managing and controlling various diseases. A disease could, e.g. change from one stage to another, and thus it is important to be able to determine the disease status. In this way, it may also be possible to gain information about aberrant cells which emerge through the progress of the disease or condition, or to investigate whether and how T-cell specificity is affected, thereby determining the status of a disease or condition. The binding of the MHC complex makes possible these options, since the binding is indicative for the presence of the MHC recognising cells in the sample, and accordingly the presence of MHC complexes displaying the peptide.

The present invention also relates to methods for the diagnosis of a disease involving MHC recognising cells comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC multimer as defined above, and

(c) determining any binding of the MHC multimer, thereby diagnosing a disease involving MHC recognising cells.

Such diagnostic methods are a powerful tool in the diagnosis of various diseases. Establishing a diagnosis is important in several ways. A diagnosis gives information about the disease, thus the patient can be offered a suitable treatment regime. Also, establishing a more specific diagnosis may give important information about a subtype of a disease for which a particular treatment will be beneficial (i.e. various subtypes of diseases may involve display of different peptides which are recognised by MHC recognising cells, and thus treatment can be targeted effectively against a particular subtype). Valuable information may also be obtained about aberrant cells emerging through the progress of the disease or condition as well as whether and how T-cell specificity is affected. The binding of the MHC multimer makes possible these options, since the binding is indicative for the presence of the MHC recognising cells in the sample, and accordingly the presence of MHC multimers displaying the peptide.

The present invention also relates to methods of correlating cellular morphology with the presence of MHC recognising cells in a sample comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC multimer as defined above, and

(c) determining any binding of the MHC multimer, thereby correlating the binding of the MHC multimer with the cellular morphology.

Such methods are especially valuable as applied in the field of histochemical methods, as the binding pattern and distribution of the MHC multimeres can be observed directly. In such methods, the sample is treated so as to preserve the morphology of the individual cells of the sample. The information gained is important i.a. in diagnostic procedures as sites affected can be observed directly.

The present invention also relates to methods for determining the effectiveness of a medicament against a disease involving MHC recognising cells comprising the steps of

(a) providing a sample from a subject receiving treatment with a medicament,

(b) contacting the sample with a as defined herein, and

(c) determining any binding of the MHC multimer, thereby determining the effectiveness of the medicament.

Such methods are a valuable tool in several ways. The methods may be used to determine whether a treatment is effectively combating the disease. The method may also provide information about aberrant cells which emerge through the progress of the disease or condition as well as whether and how T-cell specificity is affected, thereby providing information of the effectiveness of a medicament in question. The binding of the MHC multimer makes possible these options, since the binding is indicative for the presence of the MHC recognising cells in the sample, and accordingly the presence of MHC multimeres displaying the peptide.

The present invention also relates to methods for manipulating MHC recognising cells populations comprising the steps of

(a) providing a sample comprising MHC recognising cells,

(b) contacting the sample with a MHC multimer immobilised onto a solid support as defined above,

(c) isolating the relevant MHC recognising cells, and

(d) expanding such cells to a clinically relevant number, with or without further manipulation.

Such ex vivo methods are a powerful tool to generate antigen-specific, long-lived human effector T-cell populations that, when re-introduced to the subject, enable killing of target cells and has a great potential for use in immunotherapy applications against various types of cancer and infectious diseases.

As used everywhere herein, the term “MHC recognising cells” are intended to mean such which are able to recognise and bind to MHC multimeres. The intended meaning of “MHC multimeres” is given above. Such MHC recognising cells may also be called MHC recognising cell clones, target cells, target MHC recognising cells, target MHC molecule recognising cells, MHC molecule receptors, MHC receptors, MHC peptide specific receptors, or peptide-specific cells. The term “MHC recognising cells” is intended to include all subsets of normal, abnormal and defect cells, which recognise and bind to the MHC molecule. Actually, it is the receptor on the MHC recognising cell that binds to the MHC molecule.

As described above, in diseases and various conditions, peptides are displayed by means of MHC multimeres, which are recognised by the immune system, and cells targeting such MHC multimeres are produced (MHC recognising cells). Thus, the presence of such MHC protein recognising cells is a direct indication of the presence of MHC multimeres displaying the peptides recognised by the MHC protein recognising cells. The peptides displayed are indicative and may involved in various diseases and conditions.

For instance, such MHC recognising cells may be involved in diseases of inflammatory, auto-immune, allergic, viral, cancerous, infectious, allo- or xenogene (graft versus host and host versus graft) origin.

The MHC multimeres of the present invention have numerous uses and are a valuable and powerful tool e.g. in the fields of therapy, diagnosis, prognosis, monitoring, stratification, and determining the status of diseases or conditions. Thus, the MHC multimeres may be applied in the various methods involving the detection of MHC recognising cells.

Furthermore, the present invention relates to compositions comprising the MHC multimeres in a solubilising medium. The present invention also relates to compositions comprising the MHC multimeres immobilised onto a solid or semi-solid support.

The MHC multimers can be used in a number of applications, including analyses such as flow cytometry, immunohistochemistry (IHC), and ELISA-like analyses, and can be used for diagnostic, prognostic or therapeutic purposes including autologous cancer therapy or vaccines such as HIV vaccine or cancer vaccine.

The MHC multimeres are very suitable as detection systems. Thus, the present invention relates to the use of the MHC multimeres as defined herein as detection systems.

In another aspect, the present invention relates to the general use of MHC peptide complexes and multimers of such MHC peptide complexes in various methods. These methods include therapeutic methods, diagnostic methods, prognostic methods, methods for determining the progress and status of a disease or condition, and methods for the stratification of a patient.

The MHC multimeres of the present invention are also of value in testing the expected efficacy of medicaments against or for the treatment of various diseases. Thus, the present invention relates to methods of testing the effect of medicaments or treatments, the methods comprising detecting the binding of the MHC multimeres to MHC recognising cells and establishing the effectiveness of the medicament or the treatment in question based on the specificity of the MHC recognising cells.

As mentioned above, the present invention also relates generally to the field of therapy. Thus, the present invention relates per se to the MHC multimer as defined herein for use as medicaments, and to the MHC multimeres for use in in vivo and ex vivo therapy.

The present invention relates to therapeutic compositions comprising as active ingredients the MHC multimeres as defined herein.

An important aspect of the present invention is therapeutic compositions comprising as active ingredients effective amounts of MHC recognising cells obtained using the MHC multimeres as defined herein to isolate relevant MHC recognising cells, and expanding such cells to a clinically relevant number.

The present invention further relates to methods for treating, preventing or alleviating diseases, methods for inducing anergy of cells, as well as to methods for up-regulating, down-regulating, modulating, stimulating, inhibiting, restoring, enhancing and/or otherwise manipulating immune responses.

The invention also relates to methods for obtaining MHC recognising cells by using the MHC multimeres as described herein.

Also encompassed by the present invention are methods for preparing the therapeutic compositions of the invention.

The present invention is also directed to generating MHC multimeres for detecting and analysing receptors on MHC recognising cells, such as epitope specific T-cell clones or other immune competent effector cells.

It is a further object of the present invention to provide new and powerful strategies for the development of curative vaccines. This in turn will improve the possibilities for directed and efficient immune manipulations against diseases caused by tumour genesis or infection by pathogenic agent like viruses and bacteria. HIV is an important example. The ability to generate and optionally attach recombinant MHC multimeres to multimerization domains, such as scaffolds and/or carrier molecules, will enable the development of a novel analytical and therapeutical tool for monitoring immune responses and contribute to a rational platform for novel therapy and “vaccine” applications.

Therapeutic compositions (e.g. “therapeutical vaccines”) that stimulate specific T-cell proliferation by peptide-specific stimulation is indeed a possibility within the present invention. Thus, quantitative analysis and ligand-based detection of specific T-cells that proliferate by the peptide specific stimulation should be performed simultaneously to monitoring the generated response.

For all of those applications, it is important to choose the right MHC allele as well as a peptide that binds well to the MHC protein. It is also important that the chosen MHC allele and peptide forms a MHC-peptide complex that is efficiently and specifically recognized by the TCR. For applications that involve binding as well as activation of cells, further restrictions on the choice of MHC and peptide can apply.

Application of MHC Multimers in Immune Monitoring, Diagnostics, Therapy, Vaccine

MHC multimers detect antigen specific T cells of the various T cell subsets. T cells are pivotal for mounting an adaptive immune response. It is therefore of importance to be able to measure the number of specific T cells when performing a monitoring of a given immune response. Typically, the adaptive immune response is monitored by measuring the specific antibody response, which is only one of the effector arms of the immune system. This can lead to miss-interpretation of the actual clinical immune status.

In many cases intruders of the organism can hide away inside the cells, which can not provoke a humoral response. In other cases, e.g. in the case of certain viruses the intruder mutates fast, particularly in the genes encoding the proteins that are targets for the humoral response. Examples include the influenza and HIV viruses. The high rate of mutagenesis renders the humoral response unable to cope with the infection. In these cases the immune system relies on the cellular immune response. When developing vaccines against such targets one needs to provoke the cellular response in order to get an efficient vaccine.

Developing vaccines that should give rise to lifelong protection is another case where the cellular immune system needs to be activated. Commonly, various childhood vaccines are expected to give lifelong protection but will only come to trial many years after the vaccination has been performed and then there is only to hope that it actually have created effective immunity.

Therapeutically cancer vaccines generally rely on cytotoxic effector T cells and have short duration of function. Therefore, continuous monitoring is important.

MHC multimers are therefore very important for immune monitoring of vaccine responses both during vaccine development, as a means to verify the obtained immunity for lifelong vaccines and to follow cancer patients under treatment with therapeutically cancer vaccines.

The number of antigen specific cytotoxic T cells can be used as surrogate markers for the overall wellness of the immune system. The immune system can be compromised severely by natural causes such as HIV infections or big traumas or by immuno suppressive therapy in relation to transplantation. The efficacy of an anti HIV treatment can be evaluated by studying the number of common antigen-specific cytotoxic T cells, specific against for example Cytomegalovirus (CMV) and Epstein-Barr virus. In this case the measured T cells can be conceived as surrogate markers. The treatment can then be corrected accordingly and a prognosis can be made.

A similar situation is found for patients undergoing transplantation as they are severely immune compromised due to pharmaceutical immune suppression to avoid organ rejection. The suppression can lead to outbreak of opportunistic infections caused by reactivation of otherwise dormant viruses residing in the transplanted patients or the grafts. This can be the case for CMV and EBV viruses. Therefore measurement of the number of virus specific T cells can be used to give a prognosis for the outcome of the transplantation and adjustment of the immune suppressive treatment. Similarly, the BK virus has been implied as a causative reagent for kidney rejection. Therefore measurement of BK-virus specific T cells can have prognostic value.

In relation to transplantation, the presence of specific T cells directed against minor histocompatibility antigens (mHAgs) are important as they can cause graft versus host reaction/disease that can develop to a fatal situation for the patient. Again, a well-adjusted immune suppressive treatment is important. A similar reaction denoted graft versus cancer is sometimes employed in the treatment of malignancies of the lymphoid system. It is evident that such treatment is balancing on the edge of a knife and will benefit of specific measurement of relevant effector T cells.

Due to lack of organs, transplantations across greater mismatches are increasingly making harsher immune suppressive treatment more common. This calls for more efficient methods to monitor the immune status of the patient so that corrective measures in the treatment can be applied in due cause.

MHC multimers can be of importance in diagnosis of infections caused by bacteria, virus and parasites that hide away inside cells. Serum titers can be very low and direct measurement of the disease-causing organisms by PCR can be very difficult because the host cells are not identified or are inaccessible. Other clinical symptoms of a chronical infection can be unrecognizable in an otherwise healthy individuals, even though such persons still are disease-carriers and at risk of becoming spontaneously ill if being compromised by other diseases or stress. Likewise, cancers can also be diagnosed early in its development if increased numbers of cancer specific T cells can be measured in circulation, even though the tumor is not yet localized.

Antigen specific tumor infiltrating lymphocytes can be used to identify tumor lesions and metastases as the antigen specific T cells will migrate/home to the tumor site to exert their help or immuno modulatory action (CD4+ T helper cells) or cytotoxic killing of tumor cells expressing the tumor specific/tumor associated peptide MHC multimer (CD8+ T-cells). Likewise identification of sites of infection tumor lesions can be identified as they typically attract antigen specific T-cells.

Localization of tumors and sites of infection can be carried out using antigen specific T-cells labelled with a paramagnetic isotope in conjunction with magnetic resonance imaging (MRI) or electron spin resonance (ESR). In general, any conventional method for diagnostic imaging visualization can be utilized. Usually gamma and positron emitting radioisotopes are used for camera and paramagnetic isotopes for MRI.

For peripheral cancer lesion in skin (e.g. melanoma) fluorescently labeled antigen specific T-cells can be used likewise.

MHC multimers may be used to label the tumor infiltration lymphocytes, e.g. MHC multimers may be labeled with a paramagnetic isotope are injected into the patient, the labeled MHC multimer binds specific T cells and are then internalized thereby introducing the paragmagnetic isotope to the T cell in this way labelling the T cell.

Antigen-specific T helper cells and regulatory T cells have been implicated in the development of autoimmune disorders. In most cases the timing of events leading to autoimmune disease is unknown and the exact role of the immune cells not clear. Use of MHC multimers to study these diseases will lead to greater understanding of the disease-causing scenario and make provisions for development of therapies and vaccines for these diseases.

Therapeutically use of MHC multimers can be possible, either directly or as part of therapeutically vaccines. When performing autologous cancer therapy it is often recognized that the in vitro amplified cancer-specific effector T cells do not home effectively to the correct target sites but ends up in the lungs. If the molecules responsible for interaction with the correct homing receptor can be identified these can be added to the MHC multimer making a dual, triple or multiple molecular structure that are able to aid the antigen-specific T cells home to the correct target, as the MHC multimer will bind to the specific T cell and the additional molecules will mediate binding to the target cells.

In a preferable embodiment, MHC multimers bound to other functional molecules are employed to directly block, regulate or kill these cells.

When it become possible to identify and pinpoint the exact function of regulatory T cells it may be possible to directly block, regulate or kill these cells by means of MHCmers bound other functional molecules. The MHC multimeres specifically recognize the target T cells and direct the action of the other molecules to the target.

Derivatives of MHC multimers can be useful as vaccines, as vaccine components or as engineered intelligent adjuvant. The possibility of combining MHC multimeres that specifically bind certain T cells with molecules that trigger, e.g. the humoral response or the innate immune response, can accelerate vaccine development and improve the efficiency of vaccines.

Diseases

In relation to the use and application of MHCmers in immune monitoring, diagnostics, prognostics, therapy and vaccines in relation to diseases several organisms and human proteins are of relevance, comprising but not limited to the following;

Infectious Diseases

a) caused by virus such as,

Adenovirus (subgropus A-F), BK-virus, CMV (Cytomegalo virus, HHV-5), EBV (Epstein Barr Virus, HHV-4), HBV (Hepatitis B Virus), HCV (Hepatitis C virus), HHV-6a and b (Human Herpes Virus-6a and b), HHV-7, HHV-8, HSV-1 (Herpes simplex virus-1, HHV-1), HSV-2 (HHV-2), JC-virus, SV-40 (Simian virus 40), VZV (Varizella-Zoster-Virus, HHV-3), Parvovirus B19, Haemophilus influenza, HIV-1 (Human immunodeficiency Virus-1), HTLV-1 (Human T-lymphotrophic virus-1), HPV (Human Papillomavirus giving rise to clinical manifestions such as Hepatitis, AIDS, Measles, Pox, Chicken pox, Rubella, Herpes and others

b) caused by bacteria such as,

Gram positive bacteria, gram negative bacteria, intracellular bacterium, extracellular bacterium, Mycobacterium tuberculosis, Mycobacterium bovis, Mycobacterium avium subsp. paratuberculosis Borrelia burgdorferi, other spirochetes, Helicobacter pylori, Streptococcus pneumoniae, Listeria monocytogenes, Histoplasma capsulatum, Bartonella henselae, Bartonella quintana giving rise to clinical manifestations such as Tuberculosis, Pneumonia, Stomach ulcers, Paratuberculosis and others

c) caused by fungus such as,

Aspergillus fumigatus, Candida albicans, Cryptococcus neoformans, Pneumocystis carinii giving rise to clinical manifestations such as skin-, nail-, and mucosal infections, Meningitis, Sepsis and others

Parasitic diseases caused by parasites such as,

Plasmodium falciparum, Plasmodium vivax, Plasmodium malariae, Schistosoma mansoni, Schistosoma japonicum, Schistosoma haematobium, Trypanosoma cruzi, Trypanosoma rhodesiense, Trypanosoma gambiense, Leishmania donovani, Leishmania tropica giving rise to clinical manifestations such as

Allergic diseases caused by allergens such as,

Birch, Hazel, Elm, Ragweed, Wormwood, Grass, Mould, Dust Mite giving rise to clinical manifestations such as Asthma

Transplantation related disease caused by

reactions to minor histocompatibility antigens such as HA-1, HA-8, USP9Y, SMCY, TPR-protein, HB-1Y and other antigens in relation to, Graft-versus-host-related disease, allo- or xenogene reactions i.e. graft-versus-host and host-versus-graft disease.

Cancerous diseases associated with antigens such as

Survivin, Survivin-2B, Livin/ML-IAP, Bcl-2, Mcl-1, Bcl-X(L), Mucin-1, NY-ESO-1, Telomerase, CEA, MART-1, HER-2/neu, bcr-abl, PSA, PSCA, Tyrosinase, p53, hTRT, Leukocyte Proteinase-3, hTRT, gp100, MAGE antigens, GASC, JMJD2C, JARD2 (JMJ), JHDM3a, WT-1, CA 9, Protein kinases, in relation to clinical manifestations such as malignant melanoma, renal carcinoma, breast cancer, lung cancer, cancer of the uterus, cervical cancer, prostatic cancer, pancreatic cancer, brain cancer, head and neck cancer, leukemia, cutaneous lymphoma, hepatic carcinoma, colorectal cancer, bladder cancer

Autoimmune and inflammatory diseases, associated with antigens such as

GAD64, Collagen, human cartilage glycoprotein 39, □-amyloid, A□42, APP, Presenilin 1, in relation to clinical manifestations such as Diabetes type 1, Rheumatoid arthritis, Alzheimer, chronic inflammatory bowel disease, Crohn's disease, ulcerative colitis uterosa, Multiple Sclerosis, Psoriasis Approaches to the Analysis or Treatment of Diseases.

For each application of a MHC multimer, a number of choices must be made. These include:

-   -   A. Disease (to be e.g. treated, prevented, diagnosed,         monitored).     -   B. Application (e.g. analyze by flow cytometry, isolate specific         cells, induce an immune response)     -   C. Label (e.g. should the MHC multimer be labelled with a         fluorophore or a chromophore)     -   D. Biologically active molecule (e.g. should a biologically         active molecule such as an interleukin be added or chemically         linked to the complex)     -   E. Peptide (e.g. decide on a peptide to be complexed with MHC)     -   F. MHC (e.g. use a MHC allele that does not interfere with the         patient's immune system in an undesired way).

A number of diseases A₁-A_(n), relevant in connection with MHC multimeres, have been described herein; a number of applications B₁-B_(n), relevant in connection with MHC multimeres, have been described herein; a number of Labels C₁-C_(n), relevant in connection with MHC multimeres, have been described herein; a number of biologically active molecules D₁-D_(n), relevant in connection with MHC multimeres, have been described herein; a number of peptides E₁-E_(n), relevant in connection with MHC multimeres, have been described herein; and a number of MHC molecules F₁-F_(n), relevant in connection with MHC multimeres, have been described herein.

Thus, each approach involves a choice to be made regarding all or some of the parameters A-F. A given application and the choices it involves can thus be described as follows: Ai×Bi×Ci×Di×Ei×Fi

Where i specifies a number between 1 and n. n is different for different choices A, B, C, D, E, or F. Consequently, the present invention describes a large number of approaches to the diagnosis, monitoring, prognosis, therapeutic or vaccine treatment of diseases. The total number of approaches, as defined by these parameters, are n(A)×n(B)×n(C)×n(D)×n(E)×n(F), where n(A) describes the number of different diseases A described herein, n(B) describes the number of different applications B described herein, etc. Detection

Diagnostic procedures, immune monitoring and some therapeutic processes all involve identification and/or enumeration and/or isolation of antigen specific T cells. Identification and enumeration of antigen specific T cells may be done in a number of ways, and several assays are currently employed to provide this information.

In the following it is described how MHC multimers as described in the present invention can be used to detect specific T cell receptors (TCRs) and thereby antigen specific T cells in a variety of methods and assays. In the present invention detection includes detection of the presence of antigen specific T cell receptors/T cells in a sample, detection of and isolation of cells or entities with antigen specific T cell receptor from a sample and detection and enrichment of cells or entities with antigen specific T cell receptor in a sample.

The sample may be a biologic sample including solid tissue, solid tissue section or a fluid such as, but not limited to, whole blood, serum, plasma, nasal secretions, sputum, urine, sweat, saliva, transdermal exudates, pharyngeal exudates, bronchoalveolar lavage, tracheal aspirations, cerebrospinal fluid, synovial fluid, fluid from joints, vitreous fluid, vaginal or urethral secretions, or the like. Herein, disaggregated cellular tissues such as, for example, hair, skin, synovial tissue, tissue biopsies and nail scrapings are also considered as biological samples.

Many of the assays are particularly useful for assaying T-cells in blood samples. Blood samples are whole blood samples or blood processed to remove erythrocytes and platelets (e.g., by Ficoll density centrifugation or other such methods known to one of skill in the art) and the remaining PBMC sample, which includes the T-cells of interest, as well as B-cells, macrophages and dendritic cells, is used directly.

In order to be able to measure detection of specific T cells by MHC multimers, labels and marker molecules can be used.

Marker Molecules

Marker molecules are molecules or complexes of molecules that bind to other molecules. Marker molecules thus may bind to molecules on entities, including the desired entities as well as undesired entities. Labeling molecules are molecules that may be detected in a certain analysis, i.e. the labeling molecules provide a signal detectable by the used method. Marker molecules, linked to labeling molecules, constitute detection molecules. Likewise labeling molecules linked to MHC multimers also constitute detection molecules but in contrast to detection molecules made up of marker and labeling molecule labeled MHC multimers are specific for TCR.

Sometimes a marker molecule in itself provides a detectable signal, wherefore attachment to a labeling molecule is not necessary.

Marker molecules are typically antibodies or antibody fragments but can also be aptamers, proteins, peptides, small organic molecules, natural compounds (e.g. steroids), non-peptide polymers, or any other molecules that specifically and efficiently bind to other molecules are also marker molecules.

Labelling Molecules

Labelling molecules are molecules that can be detected in a certain analysis, i.e. the labelling molecules provide a signal detectable by the used method. The amount of labelling molecules can be quantified.

The labelling molecule is preferably such which is directly or indirectly detectable.

The labelling molecule may be any labelling molecule suitable for direct or indirect detection. By the term “direct” is meant that the labelling molecule can be detected per se without the need for a secondary molecule, i.e. is a “primary” labelling molecule. By the term “indirect” is meant that the labelling molecule can be detected by using one or more “secondary” molecules, i.e. the detection is performed by the detection of the binding of the secondary molecule(s) to the primary molecule.

The labelling molecule may further be attached via a suitable linker. Linkers suitable for attachment to labelling molecules would be readily known by the person skilled in the art and as described elsewhere herein for attachment of MHC molecules to multimerisation domains.

Examples of such suitable labelling compounds are fluorescent labels, enzyme labels, radioisotopes, chemiluminescent labels, bioluminescent labels, polymers, metal particles, haptens, antibodies, and dyes.

The labelling compound may suitably be selected:

from fluorescent labels such as 5-(and 6)-carboxyfluorescein, 5- or 6-carboxyfluorescein, 6-(fluorescein)-5-(and 6)-carboxamido hexanoic acid, fluorescein isothiocyanate (FITC), rhodamine, tetramethylrhodamine, and dyes such as Cy2, Cy3, and Cy5, optionally substituted coumarin including AMCA, PerCP, phycobiliproteins including R-phycoerythrin (RPE) and allophycoerythrin (APC), Texas Red, Princeston Red, Green fluorescent protein (GFP) and analogues thereof, and conjugates of R-phycoerythrin or allophycoerythrin and e.g. Cy5 or Texas Red, and inorganic fluorescent labels based on semiconductor nanocrystals (like quantum dot and Qdot™ nanocrystals), and time-resolved fluorescent labels based on lanthanides like Eu3+ and Sm3+, from haptens such as DNP, biotin, and digoxiginin, from enzymic labels such as horse radish peroxidase (HRP), alkaline phosphatase (AP), beta-galactosidase (GAL), glucose-6-phosphate dehydrogenase, beta-N-acetylglucosaminidase, β-glucuronidase, invertase, Xanthine Oxidase, firefly luciferase and glucose oxidase (GO), from luminiscence labels such as luminol, isoluminol, acridinium esters, 1,2-dioxetanes and pyridopyridazines, and from radioactivity labels such as incorporated isotopes of iodide, cobalt, selenium, tritium, and phosphor.

Radioactive labels may in particular be interesting in connection with labelling of the peptides harboured by the MHC multimeres.

Different principles of labelling and detection exist, based on the specific property of the labelling molecule. Examples of different types of labelling are emission of radioactive radiation (radionuclide, isotopes), absorption of light (e.g. dyes, chromophores), emission of light after excitation (fluorescence from fluorochromes), NMR (nuclear magnetic resonance form paramagnetic molecules) and reflection of light (scatter from e.g. such as gold-, plastic- or glass-beads/particles of various sizes and shapes). Alternatively, the labelling molecules can have an enzymatic activity, by which they catalyze a reaction between chemicals in the near environment of the labelling molecules, producing a signal, which include production of light (chemi-luminescence), precipitation of chromophor dyes, or precipitates that can be detected by an additional layer of detection molecules. The enzymatic product can deposit at the location of the enzyme or, in a cell based analysis system, react with the membrane of the cell or diffuse into the cell to which it is attached. Examples of labelling molecules and associated detection principles are shown in table 2 below.

TABLE 2 Examples of labelling molecules and associated detection principles. Labelling substance Effect Assay-principle Fluorochromes emission of light ^(¤)Photometry, having a Microscopy, specific spectra spectroscopy PMT, photographic film, CCD's (Color- Capture Device or Charge-coupled device). Radionuclide irradiation, α, β Scintillation or gamma rays counting, GM-tube, photographic film, excitation of phosphor-imager screen Enzyme; catalysis of H₂O₂ ^(¤)Photometry, HRP, (horse reduction using Microscopy, reddish luminol as Oxygen spectroscopy peroxidase), acceptor, resulting PMT, photographic peroxidases in oxidized film, CCD's (Colour- in general luminal + light Capture Device or catalysis of H₂O₂ Charge-coupled reduction using a device), soluble dye, or Secondary label molecule containing linked antibody a hapten, such as a biotin residue as Oxygen acceptor, resulting in precipitation. The habten can be recognized by a detection molecule. Particles; gold, Change of scatter, Microscopy, polystyrene reflection and cytometry, beads, pollen and transparency of electron other particles the associated entity microscopy PMT's, light detecting devices, flowcytometry scatter AP (Alkaline Catalyze a chemical ^(¤)Photometry, Phosphatase) conversion of a non- Microscopy, detectable to a spectroscopy precipitated Secondary label detectable linked antibody molecule, such as a dye or a hapten Ionophores or Change in absorption ^(¤)Photometry, chelating chemical and emission Cytometry, compounds binding to spectrums when spectroscopy specific ions, e.g. Ca²⁺ binding. Change in intensity Lanthanides Fluorescence ^(¤)photometry, Phosphorescence cytometry, spectroscopy Paramagnetic NMR (Nuclear magnetic resonance) DNA fluorescing Propidium iodide ^(¤)Photometry, stains Hoechst stain cytometry, DAPI spectroscopy AMC DraQ5 ™ Acridine orange 7-AAD ^(¤)Photometry; is to be understood as any method that can be applied to detect the intensity, analyze the wavelength spectra, and or measure the accumulation of light derived form a source emitting light of one or multiple wavelength or spectra.

Labelling molecules can be used to label MHC multimers as well as other reagents used together with MHC multimers, e.g. antibodies, aptamers or other proteins or molecules able to bind specific structures in another protein, in sugars, in DNA or in other molecules. In the following molecules able to bind a specific structure in another molecule are named a marker. Labelling molecules can be attached to a given MHC multimer or any other protein marker by covalent linkage as described for attachment of MHC multimeres to multimerization domains elsewhere herein. The attachment can be directly between reactive groups in the labelling molecule and reactive groups in the marker molecule or the attachment can be through a linker covalently attached to labelling molecule and marker, both as described elsewhere herein. When labelling MHC multimers the label can be attached either to the MHC complex (heavy chain, β2m or peptide) or to the multimerization domain.

In particular,

one or more labelling molecules may be attached to the carrier molecule, or

one or more labelling molecules may be attached to one or more of the scaffolds, or

one or more labelling compounds may be attached to one or more of the MHC complexes, or

one or more labelling compounds may be attached to the carrier molecule and/or one or more of the scaffolds and/or one or more of the MHC complexes, or

one or more labelling compounds may be attached to the peptide harboured by the MHC molecule.

A single labelling molecule on a marker does not always generate sufficient signal intensity. The signal intensity can be improved by assembling single label molecules into large multi-labelling compounds, containing two or more label molecule residues. Generation of multi-label compounds can be achieved by covalent or non-covalent, association of labelling molecules with a major structural molecule. Examples of such structures are synthetic or natural polymers (e.g. dextramers), proteins (e.g. streptavidin), or polymers. The labelling molecules in a multi-labelling compound can all be of the same type or can be a mixture of different labelling molecules.

In some applications, it may be advantageous to apply different MHC complexes, either as a combination or in individual steps. Such different MHC multimeres can be differently labelled (i.e. by labelling with different labelling compounds) enabling visualisation of different target MHC recognising cells. Thus, if several different MHC multimeres with different labelling compounds are present, it is possible simultaneously to identify more than one specific receptor, if each of the MHC multimeres present a different peptide.

Detection principles, such as listed in Table 2, can be applied to flow cytometry, stationary cytometry, and batch-based analysis. Most batch-based approaches can use any of the labelling substances depending on the purpose of the assay. Flow cytometry primarily employs fluorescence, whereas stationary cytometry primarily employs light absorption, e.g. dyes or chromophore deposit from enzymatic activity. In the following section, principles involving fluorescence detection will be exemplified for flow cytometry, and principles involving chromophore detection will be exemplified in the context of stationary cytometry. However, the labelling molecules can be applied to any of the analyses described in this invention.

Labelling molecules of particular utility in Flow Cytometry:

In flow cytometry the typical label is detected by its fluorescence. Most often a positive detection is based on the presents of light from a single fluorochrome, but in other techniques the signal is detected by a shift in wavelength of emitted light; as in FRET based techniques, where the exited fluorochrome transfer its energy to an adjacent bound fluorochrome that emits light, or when using Ca²⁺ chelating fluorescent props, which change the emission (and absorption) spectra upon binding to calcium.

Preferably labelling molecules employed in flow cytometry are illustrated in Table 3 and 4 and described in the following.

Simple fluorescent labels:

-   -   Fluor dyes, Pacific Blue™, Pacific Orange™, Cascade Yellow™,     -   AlexaFluor® (AF);         -   AF405, AF488, AF500, AF514, AF532, AF546, AF555, AF568,             AF594, AF610, AF633, AF635, AF647, AF680, AF700, AF710,             AF750, AF800     -   Quantum Dot based dyes, QDot® Nanocrystals (Invitrogen,         MolecularProbs)         -   Qdot®525, Qdot®565, Qdot®585, Qdot®605, Qdot®655, Qdot®705,             Qdot®800     -   DyLight™ Dyes (Pierce) (DL);         -   DL549, DL649, DL680, DL800     -   Fluorescein (Flu) or any derivate of that, ex. FITC     -   Cy-Dyes         -   Cy2, Cy3, Cy3.5, Cy5, Cy5.5, Cy7     -   Fluorescent Proteins;         -   RPE, PerCp, APC         -   Green fluorescent proteins;             -   GFP and GFP derivated mutant proteins; BFP, CFP, YFP,                 DsRed, T1, Dimer2, mRFP1, MBanana, mOrange, dTomato,                 tdTomato, mTangerine, mStrawberry, mCherry     -   Tandem dyes:         -   RPE-Cy5, RPE-Cy5.5, RPE-Cy7, RPE-AlexaFluor® tandem             conjugates; RPE-Alexa610, RPE-TxRed         -   APC-Aleca600, APC-Alexa610, APC-Alexa750, APC-Cy5, APC-Cy5.5     -   Ionophors; ion chelating fluorescent props         -   Props that change wavelength when binding a specific ion,             such as Calcium Props that change intensity when binding to             a specific ion, such as Calcium     -   Combinations of fluorochromes on the same marker. Thus, the         marker is not identified by a single fluorochrome but by a code         of identification being a specific combination of fluorochromes,         as well as inter related ratio of intensities.     -   Example: Antibody Ab1 and Ab2, are conjugated to both. FITC and         BP but Ab1 have 1 FITC to 1 BP whereas Ab2 have 2 FITC to 1 BP.         Each antibody may then be identified individually by the         relative intensity of each fluorochrome. Any such combinations         of n fluorochromes with m different ratios can be generated.

TABLE 3 Examples of preferable fluorochromes Excitation Emission Fluorofor/Fluorochrome nm nm 2-(4′-maleimidylanilino)naphthalene-6- 322 417 sulfonic acid, sodium salt 5-((((2-iodoacetyl)amino)ethyl)amino) 336 490 naphthalene-1-sulfonic acid Pyrene-1-butanoic acid 340 376 AlexaFluor 350 (7-amino-6-sulfonic acid-4- 346 442 methyl coumarin-3-acetic acid) AMCA (7-amino-4-methyl coumarin-3-acetic 353 442 acid) 7-hydroxy-4-methyl coumarin-3-acetic acid 360 455 Marina Blue (6,8-difluoro-7-hydroxy-4-methyl 362 459 coumarin-3-acetic acid) 7-dimethylamino-coumarin-4-acetic acid 370 459 Fluorescamin-N-butyl amine adduct 380 464 7-hydroxy-coumarine-3-carboxylic acid 386 448 CascadeBlue (pyrene-trisulphonic acid acetyl 396 410 azide) Cascade Yellow 409 558 Pacific Blue (6,8 difluoro-7-hydroxy coumarin- 416 451 3-carboxylic acid) 7-diethylamino-coumarin-3-carboxylic acid 420 468 N-(((4-azidobenzoyl)amino)ethyl)-4-amino- 426 534 3,6-disulfo-1,8-naphthalimide, dipotassium salt Alexa Fluor 430 434 539 3-perylenedodecanoic acid 440 448 8-hydroxypyrene-1,3,6-trisulfonic acid, 454 511 trisodium salt 12-(N-(7-nitrobenz-2-oxa-1,3-diazol-4- 467 536 yl)amino)dodecanoic acid N,N′-dimethyl-N-(iodoacetyl)-N′-(7-nitrobenz- 478 541 2-oxa-1,3-diazol-4-yl)ethylenediamine Oregon Green 488 (difluoro carboxy 488 518 fluorescein) 5-iodoacetamidofluorescein 492 515 propidium iodide-DNA adduct 493 636 Carboxy fluorescein 495 519

TABLE 4 Examples of preferable fluorochrome families Fluorochrome family Example fluorochrome AlexaFluor ®(AF) AF ®350, AF405, AF430, AF488, AF500, AF514, AF532, AF546, AF555, AF568, AF594, AF610, AF633, AF635, AF647, AF680, AF700, AF710, AF750, AF800 Quantum Dot Qdot ®525, Qdot ®565, Qdot ®585, (Qdot ®) based Qdot ®605, Qdot ®655, Qdot ®705, dyes Qdot ®800 DyLight ™ DL549, DL649, DL680, DL800 Dyes (DL) Small FITC, Pacific Blue ™, Pacific Orange ™, fluorescing dyes Cascade Yellow ™, Marina blue ™, DSred, DSred-2, 7-AAD, TO-Pro-3, Cy-Dyes Cy2, Cy3, Cy3.5, Cy5, Cy5.5, Cy7 Phycobili R-Phycoerythrin (RPE), PerCP, Proteins: Allophycocyanin (APC), B-Phycoerythrin, C-Phycocyanin Fluorescent (E)GFP and GFP ((enhanced) green Proteins fluorescent protein) derived mutant proteins; BFP, CFP, YFP, DsRed, Ti, Dimer2, mRFP1,MBanana, mOrange, dTomato, tdTomato, mTangerine, mStrawberry, mCherry Tandem dyes RPE-Cy5, RPE-Cy5.5, RPE-Cy7, RPE- with RPE AlexaFluor ® tandem conjugates; RPE- Alexa610, RPE-TxRed Tandem dyes APC-Aleca600, APC-Alexa610, APC- with APC Alexa750, APC-Cy5, APC-Cy5.5 Calcium dyes Indo-1-Ca2+ Indo-2-Ca2+ Preferably Labelling Molecules Employed in Stationary Cytometry and IHC

-   -   Enzymatic labelling, as exemplified in Table 5:         -   Horse radish peroxidase; reduces peroxides (H₂O₂), and the             signal is generated by the Oxygen acceptor when being             oxidized.             -   Precipitating dyes; Dyes that when they are reduced they                 are soluble, and precipitate when oxidized, generating a                 coloured deposit at the site of the reaction.             -   Precipitating agent, carrying a chemical residue, a                 hapten, for second layer binding of marker molecules,                 for amplification of the primary signal.             -   Luminol reaction, generating a light signal at the site                 of reaction.         -   Other enzymes, such as Alkaline Phosphatase, capable of             converting a chemical compound from a non-detectable             molecule to a precipitated detectable molecule, which can be             coloured, or carries a hapten as described above.     -   Fluorescent labels, as exemplified in Table 3 and 4; as those         described for Flow cytometry are likewise important for used in         stationary cytometry, such as in fluorescent microscopy.

TABLE 5 Examples of preferable labels for stationary cytometry Enzyme substrate, Precipitate or Oxygen acceptor Residue, hapten* for Binding Chromogen/ secondary detection partner Label precipitating agent layer to hapten HRP diaminobenzidine Colored — (DAB) precipitate HRP 3-amino-9-ethyl- Colored — carbazole (AEC+) precipitate AP Fast red dye Red precipitate — HRP biotinyl tyramide Exposed Biotin Streptavidin, residue avidine HRP fluorescein Exposed Anti- tyramide Fluorescein Fluorecein residue Antibody “Enzyme” Substrate that Primary label; Secondary when reacted being a dye, label in case precipitate chemiluminescence's , the primary or exposure of a hapten label is a hapten Detection Methods and Principles

Detection of TCRs with multimers may be direct or indirect.

Direct Detection

Direct detection of TCRs is detection directly of the binding interaction between the specific T cell receptor and the MHC multimer. Direct detection includes detection of TCR when TCR is attached to lipid bilayer, when TCR is attached to or in a solid medium or when TCR is in solution.

Direct Detection of TCR Attached to Lipid Bilayer

One type of TCRs to detect and measure are TCRs attached to lipid bilayer including but is not limited to naturally occurring T cells (from blood, spleen, lymphnode, brain or any other tissue containing T cells), TCR transfected cells, T cell hybridomas, TCRs embedded in liposomes or any other membrane structure. In the following methods for direct detection of entities of TCRs attached to lipid bilayer will be described and any entity consisting of TCR attached to lipid bilayer will be referred to as T cells.

T cells can be directly detected either when in a fluid solution or when immobilized to a support.

Direct Detection of T Cells in Fluid Sample.

T cells can be detected in fluid samples as described elsewhere herein and in suspension of disrupted tissue, in culture media, in buffers or in other liquids. T cells in fluid samples can be detected individually or detected as populations of T cells. In the following different methods for direct detection of T cells in fluid samples are shown.

Direct Detection of Individual T Cells

Direct Detection of Individual T Cells Using Flow Cytometry.

-   -   A suspension of T cells are added MHC multimers, the sample         washed and then the amount of MHC multimer bound to each cell         are measured. Bound MHC multimers may be labelled directly or         measured through addition of labelled marker molecules. The         sample is analyzed using a flow cytometer, able to detect and         count individual cells passing in a stream through a laser beam.         For identification of specific T cells using MHC multimers,         cells are stained with fluorescently labeled MHC multimer by         incubating cells with MHC multimer and then forcing the cells         with a large volume of liquid through a nozzle creating a stream         of spaced cells. Each cell passes through a laser beam and any         fluorochrome bound to the cell is excited and thereby         fluoresces. Sensitive photomultipliers detect emitted         fluorescence, providing information about the amount of MHC         multimer bound to the cell. By this method MHC multimers can be         used to identify specific T cell populations in liquid samples         such as synovial fluid or blood.     -   When analyzing blood samples whole blood can be used with or         without lysis of red blood cells. Alternatively lymphocytes can         be purified before flow cytometry analysis using standard         procedures like a Ficoll-Hypaque gradient. Another possibility         is to isolate T cells from the blood sample for example by         binding to antibody coated plastic surfaces, followed by elution         of bound cells. This purified T cell population can then be used         for flow cytometry analysis together with MHC multimers. Instead         of actively isolating T cells unwanted cells like B cells and NK         cells can be removed prior to the analysis. One way to do this         is by affinity chromatography using columns coated with         antibodies specific for the unwanted cells. Alternatively,         specific antibodies can be added to the blood sample together         with complement, thereby killing cells recognized by the         antibodies.     -   Various gating reagents can be included in the analysis. Gating         reagents here means labeled antibodies or other labeled markers         identifying subsets of cells by binding to unique surface         proteins. Preferred gating reagents when using MHC multimers are         antibodies directed against CD3, CD4, and CD8 identifying major         subsets of T cells. Other preferred gating reagents are         antibodies against CD14, CD15, CD19, CD25, CD56, CD27, CD28,         CD45, CD45RA, CD45RO, CCR7, CCR5, CD62L, Foxp3 recognizing         specific proteins unique for different lymphocytes of the immune         system. Following labelling with MHC multimers and before         analysis on a flow cytometer stained cells can be treated with a         fixation reagent like formaldehyde to cross-link bound MHC         multimer to the cell surface. Stained cells can also be analyzed         directly without fixation.     -   The number of cells in a sample can vary. When the target cells         are rare, it is preferable to analyze large amounts of cells. In         contrast, fewer cells are required when looking at T cell lines         or samples containing many cells of the target cell type.     -   The flow cytometer can be equipped to separate and collect         particular types of cells. This is called cell sorting. MHC         multimers in combination with sorting on a flow cytometer can be         used to isolate specific T cell populations. Isolated specific T         cell populations can then be expanded in vitro. This can be         useful in autologous cancer therapy.     -   Direct determination of the concentration of MHC-peptide         specific T cells in a sample can be obtained by staining blood         cells or other cell samples with MHC multimers and relevant         gating reagents followed by addition of an exact amount of         counting beads of known concentration. Counting beads is here to         be understood as any fluorescent bead with a size that can be         visualized by flow cytometry in a sample containing T cells. The         beads could be made of polystyrene with a size of about 1-10 μm.         They could also be made of agarose, polyacrylamide, silica, or         any other material, and have any size between 0.1 μm and 100 m.         The counting beads are used as reference population to measure         the exact volume of analyzed sample. The sample are analyzed on         a flow cytometer and the amount of MHC-specific T cell         determined using a predefined gating strategy and then         correlating this number to the number of counted counting beads         in the same sample using the following equation: Amounts of         MHC-peptide specific T cells in a blood sample can be determined         by flow cytometry by calculating the amount of MHC′mer labeled         cells in a given volume of sample with a given cell density and         then back calculate. Exact enumeration of specific T cells is         better achieved by staining with MHC′mers together with an exact         amount of counting beads followed by flow cytometry analysis.         The amount of T cells detected can then be correlated with the         amount of counting beads in the same volume of the sample and an         exact number of MHC-peptide specific T cells determined:         Concentration of MHC-specific T-cell in sample=(number of         MHC-peptide specific T cells counted/number of counting beads         counted)×concentration of counting beads in sample

Direct Detection of Individual T Cells in Fluid Sample by Microscopy

-   -   A suspension of T cells are added MHC multimers, the sample         washed and then the amount of MHC multimer bound to each cell         are measured. Bound MHC multimers may be labelled directly or         measured through addition of labelled marker molecules. The         sample is then spread out on a slide or similar in a thin layer         able to distinguish individual cells and labelled cells         identified using a microscope. Depending on the type of label         different types of microscopes may be used, e.g. if fluorescent         labels are used a fluorescent microscope is used for the         analysis. For example MHC multimers can be labeled with a         fluorochrome or bound MHC multimer detected with a fluorescent         antibody. Cells with bound fluorescent MHC multimers can then be         visualized using an immunofluorescence microscope or a confocal         fluorescence microscope.

Direct Detection of Individual T Cells in Fluid Sample by Capture on Solid Support Followed by Elution.

-   -   MHC multimers are immobilized to a support e.g. beads,         immunotubes, wells of a microtiterplate, CD, microchip or         similar and as described elsewhere herein, then a suspension of         T cells are added allowing specific T cells to bind MHC multimer         molecules. Following washing bound T cells are recovered/eluted         (e.g. using acid or competition with a competitor molecules) and         counted.         Direct Detection of Populations of T Cells     -   Cell suspensions are added labeled MHC multimer, samples are         washed and then total signal from label are measured. The MHC         multimers may be labeled themselves or detected through a         labeled marker molecule.     -   Cell suspensions are added labeled MHC multimer, samples are         washed and then signal from label are amplified and then total         signal from label and/or amplifier are measured.         Direct Detection of Immobilized T Cells.

T cells may be immobilized and then detected directly. Immobilization can be on solid support, in solid tissue or in fixator (e.g. paraffin, a sugar matrix or another medium fixing the T cells).

Direct Detection of T Cells Immobilized on Solid Support.

In a number of applications, it may be advantageous immobilise the T cell onto a solid or semi-solid support. Such support may be any which is suited for immobilisation, separation etc. Non-limiting examples include particles, beads, biodegradable particles, sheets, gels, filters, membranes (e.g. nylon membranes), fibres, capillaries, needles, microtitre strips, tubes, plates or wells, combs, pipette tips, micro arrays, chips, slides, or indeed any solid surface material. The solid or semi-solid support may be labelled, if this is desired. The support may also have scattering properties or sizes, which enable discrimination among supports of the same nature, e.g. particles of different sizes or scattering properties, colour or intensities.

Conveniently the support may be made of glass, silica, latex, plastic or any polymeric material. The support may also be made from a biodegradable material.

Generally speaking, the nature of the support is not critical and a variety of materials may be used. The surface of support may be hydrophobic or hydrophilic.

Preferred are materials presenting a high surface area for binding of the T cells. Such supports may be for example be porous or particulate e.g. particles, beads, fibres, webs, sinters or sieves.

Particulate materials like particles and beads are generally preferred due to their greater binding capacity. Particularly polymeric beads and particles may be of interest.

Conveniently, a particulate support (e.g. beads or particles) may be substantially spherical. The size of the particulate support is not critical, but it may for example have a diameter of at least 1 μm and preferably at least 2 μm, and have a maximum diameter of preferably not more than 10 μm and more preferably not more than 6 μm. For example, particulate supports having diameters of 2.8 μm and 4.5 μm will work well.

An example of a particulate support is monodisperse particles, i.e. such which are substantially uniform in size (e.g. size having a diameter standard deviation of less than 5%). Such have the advantage that they provide very uniform reproducibility of reaction. Monodisperse particles, e.g. made of a polymeric material, produced by the technique described in U.S. Pat. No. 4,336,173 (ref. 25) are especially suitable.

Non-magnetic polymer beads may also be applicable. Such are available from a wide range of manufactures, e.g. Dynal Particles AS, Qiagen, Amersham Biosciences, Serotec, Seradyne, Merck, Nippon Paint, Chemagen, Promega, Prolabo, Polysciences, Agowa, and Bangs Laboratories.

Another example of a suitable support is magnetic beads or particles. The term “magnetic” as used everywhere herein is intended to mean that the support is capable of having a magnetic moment imparted to it when placed in a magnetic field, and thus is displaceable under the action of that magnetic field. In other words, a support comprising magnetic beads or particles may readily be removed by magnetic aggregation, which provides a quick, simple and efficient way of separating out the beads or particles from a solution. Magnetic beads and particles may suitably be paramagnetic or superparamagnetic. Superparamagnetic beads and particles are e.g. described in EP 0 106 873 (Sintef, ref. 26). Magnetic beads and particles are available from several manufacturers, e.g. Dynal Biotech ASA (Oslo, Norway, previously Dynal AS, e.g. Dynabeads®).

The support may suitably have a functionalised surface. Different types of functionalisation include making the surface of the support positively or negatively charged, or hydrophilic or hydrophobic. This applies in particular to beads and particles. Various methods therefore are e.g. described in U.S. Pat. No. 4,336,173 (ref. 25), U.S. Pat. No. 4,459,378 (ref. 27) and U.S. Pat. No. 4,654,267 (ref. 28).

Immobilized T cells may be detected in several ways including:

Direct Detection of T Cells Directly Immobilized on Solid Support.

-   -   T cells may be directly immobilized on solid support e.g. by         non-specifically adhesion. Then MHC multimers are added to the         immobilized T cells thereby allowing specific T cells to bind         the MHC multimers. Bound MHC multimer may be measured through         label directly attached to the multimer or through labeled         marker molecules. Individual T cells may be detected if the         method for analysis is able to distinguish individual labeled         cells, e.g. cells are immobilized in a monolayer on a cell         culture well or a glass slide. Following staining with labeled         multimer a digital picture is taken and labeled cells identified         and counted.     -   Alternatively a population of T cells is detected by measurement         of total signal from all labeled T cells, e.g. cells are plated         to wells of a microtiter plate, stained with labeled MHC         multimer and total signal from each well are measured.

Direct Detection of T Cells Immobilized on Solid Support Through Linker Molecule

-   -   T cell can also be immobilized to solid support through a linker         molecule. The linker molecule can be an antibody specific for         the T cell, the linker can be MHC multimer or the linker can be         any molecule able to bind the T cells. In any case the linker         may be attached directly to the solid support, the linker may be         attached to the solid support through another linker or the         linker is embedded in a matrix, e.g. a sugar matrix.         -   Then MHC multimers are added to the immobilized T cells             thereby allowing specific T cells to bind the MHC multimers.             Bound MHC multimer may be measured through label directly             attached to the multimer or through labeled marker             molecules. Individual T cells may be detected if the method             for analysis is able to distinguish individual labeled             cells, e.g. a digital picture is taken and labeled cells             identified and counted. Alternatively a population of T             cells is detected by measurement of total signal from all             labeled T cells.

Phenotyping T Cell Sample Using MHC Multimer Beads.

-   -   Different MHC multimers are immobilized to different beads with         different characteristics (e.g. different size, different         fluorescence's or different fluorescence intensities) where each         kind of bead has a specific type of MHC multimer molecule         immobilized. The immobilization may be direct or through a         linker molecule as described above. The amount of bound T cells         to a specific populations of beads can be analyzed, thereby,         phenotyping the sample. The TCR on the T cell is defined by the         bead to which it binds.

Direct Detection of T Cells Immobilized to Solid Support in a Defined Pattern.

-   -   Different MHC multimers are immobilized to a support to form a         spatial array in a defined pattern, where the position specifies         the identity of the MHC multimer immobilized at this position.         The immobilization may be direct or through a linker molecule as         described above. Then a suspension of labeled T cells are added         or passed over the array of MHC multimers and specific T cells         will bind the immobilized MHC multimer molecules. The label will         thus be located at specific regions of the array, which will         allow identification of the MHC multimers that bind the cells,         and thus, allows the identification of T cells with recognition         specificity for the immobilized MHC multimers. Alternatively,         the cells can be labelled after they have been bound to the MHC         multimers. The label can be specific for the type of cell that         is expected to bind the MHC multimer (e.g. anti-CD4 for the         labelling of T-helper cells in general, where some of the         T-helper cells can be specific for a Class II MHC complex), or         the label can stain cells in general (e.g. a label that binds         DNA).     -   In this way T cells bound to the defined areas of the support         are analyzed, thereby, phenotyping the sample. Each individual T         cell is defined by the TCR it expose and depending on these TCRs         each entity will bind to different types of MHC multimer         molecules immobilized at defined positions on the solid support.         Direct Detection of Immobilized T Cells Followed by Sorting

T cells immobilized to solid support in either of the ways described above can following washing be eluted from the solid support and treated further. This is a method to sort out specific T cells from a population of different T cells. Specific T-cells can e.g. be isolated through the use of bead-based MHC multimers. Bead-based MHC multimers are beads whereto monomer MHC-peptide complexes or MHC multimers are immobilized. After the cells have been isolated they can be manipulated in many different ways. The isolated cells can be activated (to differentiate or proliferate), they can undergo induced apoptosis, or undesired cells of the isolated cell population can be removed. Then, the manipulated cell population can be re-introduced into the patient, or can be introduced into another patient.

A typical cell sorting experiment, based on bead-based MHC multimers, would follow some of the steps of the general procedure outlined in general terms in the following:

Acquire the sample, e.g. a cell sample from the bone marrow of a cancer patient.

Block the sample with a protein solution, e.g. BSA or skim milk.

Block the beads coated with MHC complexes, with BSA or skim milk.

Mix MHC-coated beads and the cell sample, and incubate.

Wash the beads with washing buffer, to remove unbound cells and non-specifically bound cells.

Isolate the immobilized cells, by either cleavage of the linker that connects MHC complex and bead; or alternatively, release the cells by a change in pH, salt-concentration addition of competitive binder or the like. Preferably, the cells are released under conditions that do not disrupt the integrity of the cells.

Manipulate the isolated cells (induce apoptosis, proliferation or differentiation)

Direct Detection of T Cells in Solid Tissue.

Direct Detection of T Cells in Solid Tissue In Vitro.

-   -   For in vitro methods of the present invention solid tissue         includes tissue, tissue biopsies, frozen tissue or tissue         biopsies, paraffin embedded tissue or tissue biopsies and         sections of either of the above mentioned. In a preferred method         of this invention sections of fixed or frozen tissues are         incubated with MHC multimer, allowing MHC multimer to bind to         specific T cells in the tissue section. The MHC multimer may be         labeled directly or through a labeled marker molecule. As an         example, the MHC multimer can be labeled with a tag that can be         recognized by e.g. a secondary antibody, optionally labeled with         HRP or another label. The bound MHC multimer is then detected by         its fluorescence or absorbance (for fluorophore or chromophore),         or by addition of an enzyme-labeled antibody directed against         this tag, or another component of the MHC multimer (e.g. one of         the protein chains, a label on the multimerization domain). The         enzyme can be Horse Raddish Peroxidase (HRP) or Alkaline         Phosphatase (AP), both of which convert a colorless substrate         into a colored reaction product in situ. This colored deposit         identifies the binding site of the MHC multimer, and can be         visualized under a light microscope. The MHC multimer can also         be directly labeled with e.g. HRP or AP, and used in IHC without         an additional antibody.     -   The tissue sections may derive from blocks of tissue or tissue         biopsies embedded in paraffin, and tissue sections from this         paraffin-tissue block fixed in formalin before staining. This         procedure may influence the structure of the TCR in the fixed T         cells and thereby influence the ability to recognize specific         MHC complexes. In this case, the native structure of TCR needs         to be at least partly preserved in the fixed tissue. Fixation of         tissue therefore should be gentle. Alternatively, the staining         is performed on frozen tissue sections, and the fixation is done         after MHC multimer staining.

Direct Detection of T Cells in Solid Tissue In Vivo

-   -   For in vivo detection of T cells labeled MHC multimers are         injected in to the body of the individual to be investigated.         The MHC multimers may be labeled with e.g. a paramagnetic         isotope. Using a magnetic resonance imaging (MRI) scanner or         electron spin resonance (ESR) scanner MHC multimer binding T         cells can then be measured and localized. In general, any         conventional method for diagnostic imaging visualization can be         utilized. Usually gamma and positron emitting radioisotopes are         used for camera and paramagnetic isotopes for MRI.

The methods described above for direct detection of TCR embedded in lipid bilayers collectively called T cells using MHC multimers also applies to detection of TCR in solution and detection of TCR attached to or in a solid medium. Though detection of individual TCRs may not be possible when TCR is in solution.

Indirect Detection of TCR

Indirect detection of TCR is primarily useful for detection of TCRs embedded in lipid bilayer, preferably natural occurring T cells, T cell hybridomas or transfected T cells. In indirect detection, the number or activity of T cells are measured, by detection of events that are the result of TCR-MHC-peptide complex interaction. Interaction between MHC multimer and T cell may stimulate the T cell resulting in activation of T cells, in cell division and proliferation of T cell populations or alternatively result in inactivation of T cells. All these mechanism can be measured using various detection methods.

Indirect Detection of T Cells by Measurement of Activation.

MHC multimers, e.g. antigen presenting cells, can stimulate T cells resulting in activation of the stimulated T cells. Activation of T cell can be detected by measurement of secretion of specific soluble factor from the stimulated T cell, e.g. secretion of cytokines like INFγ and IL2.

Stimulation of T cells can also be detected by measurement of changes in expression of specific surface receptors, or by measurement of T cell effector functions.

Measurement of activation of T cells involves the following steps:

-   a) To a sample of T cells, preferably a suspension of cells, is     added MHC multimer to induce either secretion of soluble factor, up-     or down-regulation of surface receptor or other changes in the T     cell.     -   Alternatively, a sample of T cells containing antigen presenting         cells is added antigenic peptide or protein/protein fragments         that can be processed into antigenic peptides by the antigen         presenting cell and that are able to bind MHC I or MHC II         molecules expressed by the antigen presenting cells thereby         generating a cell based MHC multimer in the sample. Several         different peptides and proteins be added to the sample. The         peptide-loaded antigen presenting cells can then stimulate         specific T cells, and thereby induce the secretion of soluble         factor, up- or down-regulation of surface receptors, or mediate         other changes in the T cell, e.g. enhancing effector functions.     -   Optionally a second soluble factor, e.g. cytokine and/or growth         factor(s) may be added to facilitate continued activation and         expansion of T cell population. -   b) Detect the presence of soluble factor, the presence/absence of     surface receptor or detect effector function -   c) Correlate the measured result with presence of T cells. The     measured signal/response indicate the presence of specific T cells     that have been stimulated with particular MHC multimer.     -   The signal/response of a T lymphocyte population is a measure of         the overall response. The frequency of specific T cells able to         respond to a given MHC multimer can be determined by including a         limiting-dilution culture in the assay also called a Limiting         dilution assay.     -   The limiting-dilution culture method involves the following         steps:         -   a) Sample of T cells in suspension are plated into culture             wells at increasing dilutions         -   b) MHC multimers are added to stimulate specific T cells.             Alternatively antigen presenting cells are provided in the             sample and then antigenic peptide I added to the sample as             described above.             -   Optionally growth factors, cytokines or other factors                 helping T cells to proliferate are added.         -   c) Cells are allowed to grow and proliferate (½-several             days). Each well that initially contained a specific T cell             will make a response to the MHC multimer and divide.         -   d) Wells are tested for a specific response e.g. secretion             of soluble factors, cell proliferation, cytotoxicity or             other effector function.         -   The assay is replicated with different numbers of T cells in             the sample, and each well that originally contained a             specific T cell will make a response to the MHC multimer.             The frequency of specific T cells in the sample equals the             reciprocal of the number of cells added to each well when             37% of the wells are negative, because due to Poisson             distribution each well then on average contained one             specific T cell at the beginning of the culture.

In the following various methods to measure secretion of specific soluble factor, expression of surface receptors, effector functions or proliferation is described.

Indirect Detection of T Cells by Measurement of Secretion of Soluble Factors.

Indirect Detection of T Cells by Measurement of Extracellular Secreted Soluble Factors.

Secreted soluble factors can be measured directly in fluid suspension, captured by immobilization on solid support and then detected or an effect of the secreted soluble factor can be detected.

Indirect Detection of T Cells by Measurement of Extracellular Secreted Soluble Factor Directly in Fluid Sample.

-   -   A sample of T cells are added MHC multimer or antigenic peptide         as described above to induce secretion of soluble factors from         antigen specific T cells. The secreted soluble factors can be         measured directly in the supernatant using e.g. mass         spectrometry.

Indirect Detection of T Cells by Capture of Extracellular Secreted Soluble Factor on Solid Support.

-   -   A sample of T cells are added MHC multimer or antigenic peptide         as described above to induce secretion of soluble factors from         antigen specific T cells. Secreted soluble factors in the         supernatant are then immobilized on a solid support either         directly or through a linker as described for immobilization of         T cells elsewhere herein. Then immobilized soluble factors can         be detected using labeled marker molecules.     -   Soluble factors secreted from individual T cells can be detected         by capturing of the secreted soluble factors locally by marker         molecules, e.g antibodies specific for the soluble factor.         Soluble factor recognising marker molecules are then immobilised         on a solid support together with T cells and soluble factors         secreted by individual T cells are thereby captured in the         proximity of each T cell. Bound soluble factor can be measured         using labelled marker molecule specific for the captured soluble         factor. The number of T cells that has given rise to labelled         spots on solid support can then be enumerated and these spots         indicate the presence of specific T cells that may be stimulated         with particular MHC multimer.     -   Soluble factors secreted from a population of T cells are         detected by capture and detection of soluble factor secreted         from the entire population of specific T cells. In this case         soluble factor do not have to be captured locally close to each         T cell but the secreted soluble factors my be captured and         detected in the same well as where the T cells are or         transferred to another solid support with marker molecules for         capture and detection e.g. beads or wells of ELISA plate.

Indirect Detection of T Cells Immobilized to Solid Support in a Defined Pattern.

-   -   Different MHC multimers of MHC-peptide complexes are immobilized         to a support to form a spatial array in a defined pattern, where         the position specifies the identity of the MHC         multimer/MHC-peptide complex immobilized at this position.         Marker molecules able to bind T cell secreted soluble factors         are co-spotted together with MHC multimer/MHC-peptide complex.         Such marker molecules can e.g. be antibodies specific for         cytokines like INFγ or IL-2. The immobilization may be direct or         through a linker molecule as described above. Then a suspension         of labeled T cells are added or passed over the array of MHC         multimers/MHC-peptide complexes and specific T cells will bind         to the immobilized MHC multimers/MHC-peptide complexes and upon         binding be stimulated to secrete soluble factors e.g. cytokines         like INFγ ord IL-2. Soluble factors secreted by individual T         cells are then captured in the proximity of each T cell and         bound soluble factor can be measured using labelled marker         molecule specific for the soluble factor. The number and         position of different specific T cells that has given rise to         labelled spots on solid support can then be identified and         enumerated. In this way T cells bound to defined areas of the         support are analyzed, thereby, phenotyping the sample. Each         individual T cell is defined by the TCR it expose and depending         on these TCRs each entity will bind to different types of MHC         multimers/MHC-peptide complexes immobilized at defined positions         on the solid support.

Indirect Detection of T Cells by Measurement of Effect of Extracellular Secreted Soluble Factor.

-   -   Secreted soluble factors can be measured and quantified         indirectly by measurement of the effect of the soluble factor on         other cell systems. Briefly,     -   a sample of T cells are added MHC multimer or antigenic peptide         as described above to induce secretion of soluble factors from         antigen specific T cells. The supernatant containing secreted         soluble factor are transferred to another cell system and the         effect measured. The soluble factor may induce proliferation,         secretion of other soluble factors, expression/downregulation of         receptors, or the soluble factor may have cytotoxic effects on         these other cells. All effects can be measured as described         elsewhere herein.         Indirect Detection of T Cells by Measurement of Intracellular         Secreted Soluble Factors

Soluble factor production by stimulated T cells can be also be measured intracellular by e.g. flow cytometry. This can be done using block of secretion of soluble factor (e.g. by monensin), permeabilization of cell (by e.g. saponine) followed by immunofluorescent staining. The method involves the following steps: 1) Stimulation of T cells by binding specific MHC multimers, e.g. antigen presenting cells loaded with antigenic peptide. An reagent able to block extracellular secretion of cytokine is added, e.g. monensin that interrupt intracellular transport processes leading to accumulation of produced soluble factor, e.g. cytokine in the Golgi complex. During stimulation other soluble factors may be added to the T cell sample during stimulation to enhance activation and/or expansion. This other soluble factor can be cytokine and or growth factors. 2) addition of one or more labelled marker able to detect special surface receptors (e.g. CD8, CD4, CD3, CD27, CD28, CD2). 3) Fixation of cell membrane using mild fixator followed by permeabilization of cell membrane by. e.g. saponine. 4) Addition of labelled marker specific for the produced soluble factor to be determined, e.g. INFγ, IL-2, IL-4, IL-10.

5) Measurement of labelled cells using a flow cytometer.

An alternative to this procedure is to trap secreted soluble factors on the surface of the secreting T cell as described by Manz, R. et al., Proc. Natl. Acad. Sci. USA 92:1921 (1995).

Indirect Detection of T Cells by Measurement of Expression of Receptors

Activation of T cells can be detected by measurement of expression and/or down regulation of specific surface receptors. The method includes the following steps. A sample of T cells are added MHC multimer or antigenic peptide as described above to induce expression or downregulation of specific surface receptors on antigen specific T cells. These receptors include but are not limited to CD28, CD27, CCR7, CD45RO, CD45RA, IL2-receptor, CD62L, CCR5. Their expression level can be detected by addition of labelled marker specific for the desired receptor and then measure the amount of label using flow cytometry, microscopy, immobilization of activated T cell on solid support or any other method like those described for direct detection of TCR in lipid bilayer.

Indirect Detection of T Cells by Measurement of Effector Function

Activation of T cells can be detected indirectly by measurement of effector functions. A sample of T cells are added MHC multimer or antigenic peptide as described above to induce the T cell to be able to do effector function. The effector function is then measured. E.g. activation of antigen specific CD8 positive T cells can be measured in a cytotoxicity assay.

Indirect Detection of T Cells by Measurement of Proliferation

T cells can be stimulated to proliferate upon binding specific MHC multimers. Proliferation of T cells can be measured several ways including but not limited to:

Detection of mRNA

-   -   Proliferation of T cells can be detected by measurement of mRNA         inside cell. Cell division and proliferation requires production         of new protein in each cell which as an initial step requires         production of mRNA encoding the proteins to be synthesized.     -   A sample of T cells are added MHC multimer or antigenic peptide         as described above to induce proliferation of antigen specific T         cells. Detection of levels of mRNA inside the proliferating T         cells can be done by quantitative PCR and indirectly measure         activation of a T cell population as a result of interaction         with MHC multimer. An example is measurement of cytokine mRNA by         in sity hybridization.

Detection of Incorporation of Thymidine

-   -   The proliferative capacity of T cells in response to stimulation         by MHC multimer can be determined by a radioactive assay based         on incorporation of [³H]thymidine ([³H]TdR) into newly generated         DNA followed by measurement of radioactive signal.

Detection of Incorporation of BrdU

-   -   T cell proliferation can also be detected by of incorporation of         bromo-2′-deoxyuridine (BrdU) followed by measurement of         incorporated BrdU using a labeled anti-BrdU antibody in an ELISA         based analysis.

Viability of cells may be measured by measurement ATP in a cell culture.

Indirect Detection of T Cells by Measurement of Inactivation

Not all MHC multimers will lead to activation of the T cells they bind. Under certain circumstances some MHC multimers may rather inactivate the T cells they bind to.

Indirect Detection of T Cells by Measurement of Effect of Blockade of TCR

Inactivation of T cells by MHC multimers may be measured be measuring the effect of blocking TCR on antigen specific T cells. MHC multimers, e.g. MHC-peptide complexes coupled to IgG scaffold can block the TCR of an antigen specific T cell by binding the TCR, thereby prevent the blocked T cell receptor interacting with e.g. antigen presenting cells. Blockade of TCRs of a T cell can be detected in any of the above described methods for detection of TCR by addition of an unlabeled blocking MHC multimer together with the labelled MHC multimer and then measuring the effect of the blockade on the readout.

Indirect Detection of T Cells by Measurement of Induction of Apoptosis

Inactivation of T cells by MHC multimers may be measured be measuring apoptosis of the antigen specific T cell. Binding of some MHC multimers to specific T cells may lead to induction of apoptosis. Inactivation of T cells by binding MHC multimer may therefore be detected by measuring apoptosis in the T cell population. Methods to measure apoptosis in T cells include but are not limited to measurement of the following:

-   -   DNA fragmentation     -   Alterations in membrane asymmetry (phosphatidylserine         translocation)     -   Activation of apoptotic caspases     -   Release of cytochrome C and AIF from mitochondria into the         cytoplasm         Positive Control Experiments for the Use of MHC Multimers in         Flow Cytometry and Related Techniques

When performing flow cytometry experiments, or when using similar technologies, it is important to include appropriate positive and negative controls. In addition to establishing proper conditions for the experiments, positive and negative control reagents can also be used to evaluate the quality (e.g. specificity and affinity) and stability (e.g. shelf life) of produced MHC multimers.

The quality and stability of a given MHC multimer can be tested in a number of different ways, including:

-   -   Measurement of specific MHC multimer binding to beads, other         types of solid support, or micelles and liposomes, to which         TCR's have been immobilized. Other kinds of molecules that         recognize specifically the MHC-peptide complex can be         immobilized and used as well. Depending on the nature of the         solid support or membrane structure to which the TCR is         immobilized, the TCR can be full-length (i.e. comprise the         intracellular- and intra-membrane domains), or can be truncated         (e.g. only comprise the extracellular domains). Likewise, the         TCR can be recombinant, and can be chemically or enzymatically         modified.     -   Measurement of MHC multimer binding to beads, other types of         solid support, or micelles and liposomes, to which aptamers,         antibodies or other kinds of molecules that recognize correctly         folded MHC-peptide complexes have been immobilized.     -   Measurement of specific MHC multimer binding to specific cell         lines (e.g. T-cell lines) displaying MHC multimer-binding         molecules, e.g. displaying TCRs with appropriate specificity and         affinity for the MHC multimer in question.     -   Measurement of specific MHC multimer binding to cells in blood         samples, preparations of purified lymphocytes (HPBMCs), or other         bodily fluids that contain cells carrying receptor molecules         specific for the MHC multimer in question.     -   Measurement of specific MHC multimer binding to soluble TCRs,         aptamers, antibodies, or other soluble MHC-peptide         complex-binding molecules, by density-gradient centrifugation         (e.g. in CsCl) or by size exclusion chromatography, PAGE or         other type of chromatographic method.

Measurement of specific MHC binding to TCRs, aptamers, antibodies, streptavidin, or other MHC-peptide complex-binding molecules immobilized on a solid surface (e.g. a microtiter plate). The degree of MHC multimer binding can be visualized with a secondary component that binds the MHC multimer, e.g. a biotinylated fluorophore in cases where the MHC multimer contains streptavidin proteins, not fully loaded with biotin. Alternatively, the secondary component is unlabelled, and a labelled second component-specific compound is employed (e.g. EnVision System, Dako) for visualization. This solid surface can be beads, immunotubes, microtiterplates act. The principle for purification are basically the same I.e. T cells are added to the solid with immobilized MHC′mer, non-binding T cells are washed away and MHC-peptide specific T cells can be retrieved by elution with mild acid or a competitive binding reagent.

-   -   Measurement of specific MHC multimer binding to TCRs, aptamers,         antibodies, streptavidin, or other MHC-peptide complex-binding         molecules immobilized on a solid surface (e.g. a microtiter         plate) visualized with a secondary component specific to MHC         multimer (e.g. TCRs, aptamers, antibodies, streptavidin, or         other MHC-peptide binding complex-binding molecules).         Alternatively the secondary receptor is unlabelled, and a         labelled second receptor-specific compound is employed (e.g.         EnVision System, Dako) before visualization.

In the above mentioned approaches, positive control reagents include MHC multimers comprising correctly folded MHC, complexed with an appropriate peptide that allows the MHC multimer to interact specifically and efficiently with its cognate TCR. Negative control reagents include empty MHC multimers, or correctly folded MHC multimers complexed with so-called nonsense peptides that support a correct conformation of the MHC-peptide complex, but that do not efficiently bind TCRs through the peptide-binding site of the MHC complex.

Negative Control Reagents and Negative Control Experiments for the Use of MHC Multimers in Flow Cytometry and Related Techniques

Experiments with MHC multimers require a negative control in order to determine background staining with MHC multimer. Background staining can be due to unwanted binding of any of the individual components of the MHC multimer, e.g., MHC complex or individual components of the MHC complex, multimerization domain or label molecules. The unwanted binding can be to any surface or intracellular protein or other cellular structure of any cell in the test sample, e.g. undesired binding to B cells, NK cells or T cells. Unwanted binding to certain cells or certain components on cells can normally be corrected for during the analysis, by staining with antibodies that bind to unique surface markers of these specific cells, and thus identifies these as false positives, or alternatively, that bind to other components of the target cells, and thus identifies these cells as true positives. A negative control reagent can be used in any experiment involving MHC multimers, e.g. flow cytometry analysis, other cytometric methods, immunohistochemistry (IHC) and ELISA. Negative control reagents include the following:

-   -   MHC complexes or MHC multimers comprising MHC complexes carrying         nonsense peptides. A nonsense peptide is here to be understood         as a peptide that binds the MHC protein efficiently, but that         does not support binding of the resultant MHC-peptide complex to         the desired TCR. An example nonsense peptide is a peptide with         an amino acid sequence different from the linear sequence of any         peptide derived from any known protein. When choosing an         appropriate nonsense peptide the following points are taken into         consideration. The peptide should ideally have appropriate amino         acids at relevant positions that can anchor the peptide to the         peptide-binding groove of the MHC. The remaining amino acids         should ideally be chosen in such a way that possible binding to         TCR (through interactions with the peptide or peptide-binding         site of MHC) are minimized. The peptide should ideally be         soluble in water to make proper folding with MHC alpha chain and         β2m possible in aqueous buffer. The length of the peptide should         ideally match the type and allele of MHC complex. The final         peptide sequence should ideally be taken through a blast search         or similar analysis, to ensure that it is not identical with any         peptide sequence found in any known naturally occurring         proteins.     -   MHC complexes or MHC multimers comprising MHC complexes carrying         a chemically modified peptide in the peptide-binding groove. The         modification should ideally allow proper conformation of the         MHC-peptide structure, yet should not allow efficient         interaction of the peptide or peptide-binding site of MHC with         the TCR.     -   MHC complexes or MHC multimers comprising MHC complexes carrying         a naturally occurring peptide different from the peptide used         for analysis of specific T cells in the sample. When choosing         the appropriate natural peptide the following should be taken         into consideration. The peptide in complex with the MHC protein         should ideally not be likely to bind a TCR of any T cell in the         sample with such an affinity that it can be detected with the         applied analysis method. The peptide should ideally be soluble         in water to make proper folding with MHC alpha chain and β2m         possible in aqueous buffer. The length of the peptide should         match the type and allele of MHC complex.     -   Empty MHC complexes or MHC multimers comprising empty MHC         complexes, meaning any correctly folded MHC complex without a         peptide in the peptide-binding groove.     -   MHC heavy chain or MHC multimers comprising MHC heavy chain,         where MHC heavy chain should be understood as full-length MHC I         or MHC II heavy chain or any truncated version of MHC I or MHC         II heavy chain. The MHC heavy chains can be either folded or         unfolded. Of special interest is MHC I alpha chains containing         the α3 domain that binds CD8 molecules on cytotoxic T cells.         Another embodiment of special interest is MHC II β chains         containing the β2 domain that binds CD4 on the surface of helper         T cells.     -   Beta2microglobulin or subunits of beta2microglobulin, or MHC         multimers comprising Beta2microglobulin or subunits of         beta2microglobulin, folded or unfolded.     -   MHC-like complexes or MHC multimers comprising MHC-like         complexes, folded or unfolded. An example could be CD1 molecules         that are able to bind peptides in a peptide-binding groove that         can be recognized by T cells (Russano et al. (2007).         CD1-restricted recognition of exogenous and self-lipid antigens         by duodenal gammadelta+ T lymphocytes. J. Immunol.         178(6):3620-6)     -   Multimerization domains without MHC or MHC-like molecules, e.g.         dextran, streptavidin, IgG, coiled-coil-domain liposomes.     -   Labels, e.g. FITC, PE, APC, pacific blue, cascade yellow, or any         other label listed elsewhere herein.

Negative controls 1-4 can provide information about potentially undesired binding of the MHC multimer, through interaction of a surface of the MHC-peptide complex different from the peptide-binding groove and its surroundings. Negative control 5 and 6 can provide information about binding through interactions through the MHC I or MHC II proteins (in the absence of peptide). Negative control 7 can provide information about binding through surfaces of the MHC complex that is not unique to the MHC complex. Negative controls 8 and 9 provide information about potential undesired interactions between non-MHC-peptide complex components of the MHC multimer and cell constituents.

Minimization of Undesired Binding of the MHC Multimer

Identification of MHC-peptide specific T cells can give rise to background signals due to unwanted binding to cells that do not carry TCRs. This undesired binding can result from binding to cells or other material, by various components of the MHC multimer, e.g. the dextran in a MHC dextramer construct, the labelling molecule (e.g. FITC), or surface regions of the MHC-peptide complex that do not include the peptide and the peptide-binding cleft. MHC-peptide complexes bind to specific T cells through interaction with at least two receptors in the cell membrane of the T-cell. These two receptors are the T-cell receptor (TCR) and CD8 for MHC I-peptide complexes and TCR and CD4 receptor protein for MHC II-peptide complexes. Therefore, a particularly interesting example of undesired binding of a MHC multimer is its binding to the CD8 or CD4 molecules of T cells that do not carry a TCR specific for the actual MHC-peptide complex. The interaction of CD8 or CD4 molecules with the MHC is not very strong; however, because of the avidity gained from the binding of several MHC complexes of a MHC multimer, the interaction between the MHC multimer and several CD8 or CD4 receptors potentially can result in undesired but efficient binding of the MHC multimer to these T cells. In an analytical experiment this would give rise to an unwanted background signal; in a cell sorting experiment undesired cells might become isolated.

Other particular interesting examples of undesired binding is binding to lymphoid cells different from T cells, e.g. NK-cells, B-cells, monocytes, dendritic cells, and granulocytes like eosinophils, neutrophils and basophiles.

Apart from the MHC complex, other components in the MHC multimer can give rise to unspecific binding. Of special interest are the multimerization domain, multimerization domain molecules, and labelling molecules.

One way to overcome the problem with unwanted binding is to include negative controls in the experiment and subtract this signal from signals derived from the analyzed sample, as described elsewhere in the invention.

Alternatively, unwanted binding could be minimized or eliminated during the experiment. Methods to minimize or eliminate background signals include:

-   -   Mutations in areas of the MHC complex responsible for binding to         unwanted cells can be introduced. Mutations here mean         substitution, insertion, or deletion of natural or non-natural         amino acids. Sub-domains in the MHC complex can be responsible         for unwanted binding of the MHC multimer to cells without a TCR         specific for the MHC-peptide complex contained in the MHC         multimer. One example of special interest is a small region in         the α3-domain of the α-chain of MHC I molecules that is         responsible for binding to CD8 on all cytotoxic T cells.         Mutations in this area can alter or completely abolish the         interaction between CD8 on cytotoxic T cells and MHC multimer         (Neveu et al. (2006) Int Immunol. 18, 1139-45). Similarly a sub         domain in the β2 domain of the β-chain of MHC II molecules is         responsible for binding CD4 molecules on all CD4 positive T         cells. Mutations in this sub domain can alter or completely         abolish the interaction between MHC 11 and CD4.     -   Another embodiment is to mutate other areas of MHC I/MHC II         complexes that are involved in interactions with T cell surface         receptors different from TCR, CD8 and CD4, or that bind surface         receptors on B cells, NK cells, Eosiniophils, Neutrophils,         Basophiles, Dendritic cells or monocytes.     -   Chemical alterations in areas of the MHC complex responsible for         binding to unwanted cells can be employed in order to minimize         unwanted binding of MHC multimer to irrelevant cells. Chemical         alteration here means any chemical modification of one or more         amino acids. Regions in MHC complexes that are of special         interest are as mentioned above the α3 domain of the α-chain in         MHC I molecules and β2 domains in the β-chain of MHC II         molecules. Other regions in MHC I/MHC II molecules that can be         chemically modified to decrease the extent of undesired binding         are regions involved in interaction with T cell surface         receptors different from TCR, CD8 and CD4, or that bind surface         receptors on B cells, NK cells, Eosiniophils, Neutrophils,         Basophiles, Dendritic cells or monocytes.     -   Another method to minimize undesired binding involves the         addition of one or more components of a MHC multimer, predicted         to be responsible for the unwanted binding. The added component         is not labeled, or carries a label different from the label of         the MHC multimer used for analysis. Of special interest is         addition of MHC multimers that contain nonsense peptides, i.e.         peptides that interact efficiently with the MHC protein, but         that expectably do not support specific binding of the MHC         multimer to the TCR in question. Another example of interest is         addition of soluble MHC complexes not coupled to a         multimerization domain, and with or without peptide bound in the         peptide binding cleft. In another embodiment, individual         components of the MHC complex can be added to the sample, e.g. I         α-chain or subunits of MHC I α-chain either folded or unfolded,         beta2microglobulin or subunits thereof either folded or         unfolded, α/β-chain of MHC II or subunits thereof either folded         or unfolded. Any of the above mentioned individual components         can also be attached to a multimerization domain identical or         different from the one used in the MHC multimer employed in the         analysis.     -   Of special interest is also addition of multimerization domain         similar or identical to the multimerization domain used in the         MHC multimer or individual components of the multimerization         domain.     -   Reagents able to identify specific cell types either by         selection or exclusion can be included in the analysis to help         identify the population of T cells of interest, and in this way         deselect the signal arising from binding of the MHC multimer to         undesired cells.     -   Of special interest is the use of appropriate gating reagents in         flow cytometry experiments. Thus, fluorescent antibodies         directed against specific surface markers can be used for         identification of specific subpopulations of cells, and in this         way help to deselect signals resulting from MHC-multimers         binding to undesired cells.     -   Gating reagents of special interest that helps identify the         subset of T cells of interest when using MHC I multimers are         reagents binding to CD3 and CD8 identifying all cytotoxic T         cells. These reagents are preferably antibodies but can be any         labeled molecule capable of binding CD3 or CD8. Gating reagents         directed against CD3 and CD8 are preferably used together. As         they stain overlapping cell populations they are preferably         labeled with distinct fluorochromes. However, they can also be         used individually in separate samples. In experiments with MHC         II multimers reagents binding to CD3 and CD4 identifying T         helper cells can be used. These reagents are preferably         antibodies but can be any labeled molecule capable of binding         CD3 or CD4. Gating reagents directed against CD3 and CD4 are         preferable used together. As they stain overlapping cell         populations they are preferably labeled with distinct         fluorochromes. However, they can also be used individually in         separate samples.

Other gating reagents of special interest in experiments with any MHC multimer, are reagents binding to the cell surface markers CD2, CD27, CD28, CD45RA, CD45RO, CD62L and CCR7. These surface markers are unique to T cells in various differentiation states. Co staining with either of these reagents or combinations thereof together with MHC multimers helps to select MHC multimer binding T cells expressing a correct TCR. These reagents can also be combined with reagents directed against CD3, CD4 and/or CD8.

Another flow cytometric method of special interest to remove signals from MHC multimer stained cells not expressing the specific TCR, is to introduce an exclusion gate. Antibodies or other reagents specific for surface markers unique to the unwanted cells are labeled with a fluorochrome and added to the test sample together with the MHC multimer. The number of antibodies or surface marker specific reagents are not limited to one but can be two, three, four, five, six, seven, eight, nine, ten or more individual reagents recognizing different surface markers, all of which are unique to the unwanted cells. During or after collection of data all events representing cells labeled with these antibodies are dumped in the same gate and removed from the dataset. This is possible because all the antibodies/reagents that bind to the wrong cells are labeled with the same fluorochrome.

Reagents of special interest that exclude irrelevant cells include reagents against CD45 expressed on red blood cells, CD19 expressed on B cells, CD56 expressed on NK cells, CD4 expressed on T helper cells and CD8 expressed on cytotoxic T cells, CD14 expressed on monocytes and CD15 expressed on granulocytes and monocytes.

Vaccine Treatment

For the purpose of making cancer vaccines or other types of vaccines it can be desirable to employ MHC multimers that comprise a polymer such as dextran, or that are cell-based (e.g. specialized dendritic cells such as described by Banchereau and Palucka, Nature Reviews, Immunology, 2005, vol. 5, p. 296-306).

-   -   Preventive vaccination leading to prophylaxis/sterile immunity         by inducing memory in the immune system may be obtained by         immunizing/vaccinating an individual or animal with MHC alone,         or with MHC in combination with other molecules as mentioned         elsewhere in the patent.         -   Vaccine antigens can be administered alone         -   Vaccine can be administered in combination with adjuvant(s).             -   Adjuvant can be mixed with vaccine component or                 administered alone, simultaneously or in any order.             -   Adjuvant can be administered by the same route as the                 other vaccine components         -   Vaccine administered more than once may change composition             from 1^(st) administration to the 2^(nd), 3^(rd), etc.         -   Vaccine administered more than once can be administered by             alternating routes         -   Vaccine components can be administered alone or in             combinations by the same route or by alternating/mixed             routes         -   Vaccine can be administered by the following routes             -   Cutaneously             -   Subcutaneously (SC)             -   Intramuscular (IM)             -   Intravenous (IV)             -   Per-oral (PO)             -   Inter peritoneally             -   Pulmonally             -   Vaginally             -   Rectally     -   Therapeutic vaccination i.e. vaccination “teaching” the immune         system to fight an existing infection or disease, may be         obtained by immunizing/vaccinating an individual or animal with         MHC alone, or with MHC in combination with other molecules as         mentioned elsewhere in the patent.         -   Vaccine antigens can be administered alone         -   Vaccine can be administered in combination with adjuvant(s).             -   Adjuvant can be mixed with vaccine component or                 administered alone, simultaneously or in any order.             -   Adjuvant can be administered by the same route as the                 other vaccine components         -   Vaccine administered more than once may change composition             from 1^(st) administration to the 2^(nd), 3^(rd), etc.         -   Vaccine administered more than once can be administered by             alternating routes         -   Vaccine components can be administered alone or in             combinations by the same route or by alternating/mixed             routes         -   Vaccine can be administered by the following routes             -   Cutaneously             -   Subcutaneously (SC)             -   Intramuscular (IM)             -   Intravenous (IV)             -   Per-oral (PO)             -   Inter peritoneally             -   Pulmonally             -   Vaginally             -   Rectally                 Therapeutic Treatment     -   Therapeutic treatment includes the use of MHC molecules alone or         in any molecular combination mentioned elsewhere in the patent         application for the purpose of treating a disease in any state.         Treatment may be in the form of         -   Per-orally intake             -   Pills             -   Capsules         -   Injections             -   Systemic             -   Local         -   Jet-infusion (micro-drops, micro-spheres, micro-beads)             through skin         -   Drinking solution, suspension or gel         -   Inhalation         -   Nose-drops         -   Eye-drops         -   Ear-drops         -   Skin application as ointment, gel or creme         -   Vaginal application as ointment, gel, crème or washing         -   Gastro-Intestinal flushing         -   Rectal washings or by use of suppositories     -   Treatment can be performed as         -   Single intake, injection, application, washing         -   Multiple intake, injection, application, washing             -   On single day basis             -   Over prolonged time as days, month, years     -   Treatment dose and regimen can be modified during the course         Personalized Medicine Takes Advantage of the Large Diversity of         Peptide Epitopes that May be Generated from a Given Antigen.

The immune system is very complex. Each individual has a very large repertoire of specific T cells (on the order of 10⁶-10⁹ different T cell specificities), which again is only a small subset of the total T cell repertoire of a population of individuals. It is estimated that the Caucasian population represents a T cell diversity of 10¹⁰-10¹². MHC allele diversity combined with large variation among individuals' proteolytic metabolism further enhances the variation among different individuals' immune responses. As a result, each individual has its own characteristic immune response profile.

This is important when designing a MHC multimer-based immune monitoring reagent or immunotherapeutic agent. If an agent is sought that should be as generally applicable as possible, one should try to identify peptide epitopes and MHC alleles that are common for the majority of individuals of a population. As described elsewhere in this application, such peptide epitopes can be identified through computerized search algorithms developed for that same purpose, and may be further strengthened by experimental testing of a large set of individuals.

This approach will be advantageous in many cases, but because of the variability among immune responses of different individuals, is likely to be inefficient or inactive in certain individuals, because of these individuals' non-average profile. In these latter cases one may have to turn to personalized medicine. In the case of immune monitoring and immunotherapy, this may involve testing a large number of different epitopes from a given antigen, in order to find peptide epitopes that may provide MHC multimers with efficiency for a given individual.

Thus, personalized medicine takes advantage of the wealth of peptide epitopes that may be generated from a given antigen. A large number of the e.g. 8-, 9-, 10-, and 11-mer epitopes that may be generated from a given antigen to be included in a class 1 MHC multimer reagent, for use in immune monitoring or immunotherapy, are therefore of relevance in personalized medicine. Only in the case where one wants to generate a therapeutic agent or diagnostic reagent that is applicable to the majority of individuals of a population can the large majority of epitope sequences be said to be irrelevant, and only those identified by computerized search algorithms and experimental testing be said to be of value. For the odd individual with the odd immune response these disregarded peptide epitopes may be the epitopes that provide an efficient diagnostic reagent or cures that individual from a deadly disease.

Antigenic Peptides

The present invention relates to one or more MHC multimers and/or one or more MHC complexes comprising one or more antigenic peptides such as the antigenic peptides listed in table A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, X and Y.

The one or more antigenic peptides can in one embodiment comprise a fragment of one or more cancer antigens.

The one or more cancer antigens can be selected from Table A.

TABLE A Protein designation and accession numbers for the four selected cancer antigens Bcl-2, BclX(L), Survivin and Mcl-1. The amino acid sequence of each protein is displayed. Protein and accession number Cancer antigen AAH27258.1 MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAP B-cell CLL/lymphoma 2, GIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPV Bcl-2 [Homo sapiens] VHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELF RDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRH LHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACI TLGAYLGHK NP_612815.1 MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEME Bcl-X(L) TPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALRE (BCL2-like 1 isoform 1) AGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWG [Homo sapiens] RIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQE NGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLF SRK AAC51660.1 MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHC apoptosis inhibitor PTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQ survivin [Homo sapiens] FEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQL AAMD AAF64255.1 MFGLKRNAVIGLNLYCGGAGLGAGSGGATRPGGRLLATEKEASARR Mcl-1 [Homo sapiens] EIGGGEAGAVIGGSAGASPPSTLTPDSRRVARPPPIGAEVPDVTAT PARLLFFAPTRRAAPLEEMEAPAADAIMSPEEELDGYEPEPLGKRP AVLPLLELVGESGNNTSTDGSLPSTPPPAEEEEDDLYRQSLEIISR YLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQG MLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAK HLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVE DLEGGIRNVLLAFAGVAGVGAGLAYLIR SEQ ID NOS: 44889-44892

The one or more antigenic peptides can in one embodiment comprise one or more fragments from one or more cancer antigens capable of interacting with one or more MHC class 1 molecules.

The one or more antigenic peptides can in another embodiment comprise one or more fragments from one or more cancer antigens capable of interacting with one or more MHC class 2 molecules.

The one or more antigenic peptides can in one embodiment comprise one or more fragments from BclX(L).

The one or more antigenic peptides can in one embodiment comprise one or more fragments from Bcl-2.

The one or more antigenic peptides can in one embodiment comprise one or more fragments from Survivin.

The one or more antigenic peptides can in one embodiment comprise one or more fragments from Mcl-1.

Preferred fragments of BclX(L) capable of interacting with one or more MHC class 1 molecules are listed in table B.

TABLE B Prediction of cancer antigen BclX(L) specific MHC class1, 8-, 9-, 10-, 11-mer peptide binders for 42 MHC class 1 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/ NetMHC/ database. The MHC class 1 molecules for which no binders were found are not listed. pos peptide logscore affinity (nM) Bind Level Protein Name Allele 8-mers 57 HLADSPAV 0.691 28 SB Sequence A0201 213 FLTGMTVA 0.687 29 SB Sequence A0201 166 AAWMATYL 0.477 285 WB Sequence A0201 160 VLVSRIAA 0.463 333 WB Sequence A0201 119 YQSFEQVV 0.436 448 WB Sequence A0201 147 GALCVESV 0.431 472 WB Sequence A0201 223 VLLGSLFS 0.427 494 WB Sequence A0201 213 FLTGMTVA 0.777 11 SB Sequence A0202 57 HLADSPAV 0.771 11 SB Sequence A0202 119 YQSFEQVV 0.590 84 WB Sequence A0202 218 TVAGVVLL 0.565 110 WB Sequence A0202 11 FLSYKLSQ 0.545 137 WB Sequence A0202 82 MAAVKQAL 0.512 195 WB Sequence A0202 73 SLDAREVI 0.475 294 WB Sequence A0202 192 ELYGNNAA 0.444 410 WB Sequence A0202 217 MTVAGVVL 0.440 425 WB Sequence A0202 160 VLVSRIAA 0.434 454 WB Sequence A0202 1 SQSNRELV 0.434 457 WB Sequence A0202 213 FLTGMTVA 0.852 4 SB Sequence A0203 57 HLADSPAV 0.831 6 SB Sequence A0203 160 VLVSRIAA 0.642 48 SB Sequence A0203 158 MQVLVSRI 0.602 74 WB Sequence A0203 11 FLSYKLSQ 0.582 92 WB Sequence A0203 133 GVNWGRIV 0.581 92 WB Sequence A0203 216 GMTVAGVV 0.579 94 WB Sequence A0203 119 YQSFEQVV 0.578 96 WB Sequence A0203 164 RIAAWMAT 0.573 101 WB Sequence A0203 78 EVIPMAAV 0.486 261 WB Sequence A0203 1 SQSNRELV 0.481 274 WB Sequence A0203 217 MTVAGVVL 0.467 318 WB Sequence A0203 147 GALCVESV 0.464 328 WB Sequence A0203 221 GVVLLGSL 0.443 412 WB Sequence A0203 218 TVAGVVLL 0.440 429 WB Sequence A0203 57 HLADSPAV 0.555 122 WB Sequence A0204 153 SVDKEMQV 0.431 469 WB Sequence A0204 57 HLADSPAV 0.780 10 SB Sequence A0206 158 MQVLVSRI 0.733 18 SB Sequence A0206 213 FLTGMTVA 0.682 31 SB Sequence A0206 1 SQSNRELV 0.677 32 SB Sequence A0206 119 YQSFEQVV 0.677 33 SB Sequence A0206 138 RIVAFFSF 0.653 42 SB Sequence A0206 164 RIAAWMAT 0.575 99 WB Sequence A0206 147 GALCVESV 0.568 106 WB Sequence A0206 166 AAWMATYL 0.567 108 WB Sequence A0206 217 MTVAGVVL 0.563 112 WB Sequence A0206 160 VLVSRIAA 0.517 185 WB Sequence A0206 42 SEMETPSA 0.514 191 WB Sequence A0206 78 EVIPMAAV 0.496 233 WB Sequence A0206 153 SVDKEMQV 0.493 240 WB Sequence A0206 57 HLADSPAV 0.955 1 SB Sequence A0211 153 SVDKEMQV 0.898 3 SB Sequence A0211 213 FLTGMTVA 0.893 3 SB Sequence A0211 73 SLDAREVI 0.877 3 SB Sequence A0211 192 ELYGNNAA 0.834 6 SB Sequence A0211 218 TVAGVVLL 0.797 8 SB Sequence A0211 172 YLNDHLEP 0.751 14 SB Sequence A0211 78 EVIPMAAV 0.739 16 SB Sequence A0211 216 GMTVAGVV 0.718 21 SB Sequence A0211 160 VLVSRIAA 0.684 30 SB Sequence A0211 223 VLLGSLFS 0.683 30 SB Sequence A0211 133 GVNWGRIV 0.668 36 SB Sequence A0211 212 WFLTGMTV 0.668 36 SB Sequence A0211 144 SFGGALCV 0.591 83 WB Sequence A0211 72 SSLDAREV 0.590 84 WB Sequence A0211 106 DLTSQLHI 0.564 111 WB Sequence A0211 119 YQSFEQVV 0.545 136 WB Sequence A0211 81 PMAAVKQA 0.532 158 WB Sequence A0211 11 FLSYKLSQ 0.511 198 WB Sequence A0211 166 AAWMATYL 0.456 360 WB Sequence A0211 1 SQSNRELV 0.439 431 WB Sequence A0211 147 GALCVESV 0.439 434 WB Sequence A0211 57 HLADSPAV 0.915 2 SB Sequence A0212 192 ELYGNNAA 0.813 7 SB Sequence A0212 213 FLTGMTVA 0.801 8 SB Sequence A0212 153 SVDKEMQV 0.732 18 SB Sequence A0212 73 SLDAREVI 0.714 22 SB Sequence A0212 160 VLVSRIAA 0.662 38 SB Sequence A0212 172 YLNDHLEP 0.662 38 SB Sequence A0212 119 YQSFEQVV 0.586 88 WB Sequence A0212 78 EVIPMAAV 0.585 88 WB Sequence A0212 223 VLLGSLFS 0.582 92 WB Sequence A0212 11 FLSYKLSQ 0.573 101 WB Sequence A0212 212 WFLTGMTV 0.541 142 WB Sequence A0212 216 GMTVAGVV 0.466 321 WB Sequence A0212 57 HLADSPAV 0.892 3 SB Sequence A0216 153 SVDKEMQV 0.817 7 SB Sequence A0216 213 FLTGMTVA 0.761 13 SB Sequence A0216 192 ELYGNNAA 0.715 21 SB Sequence A0216 78 EVIPMAAV 0.666 37 SB Sequence A0216 218 TVAGVVLL 0.657 41 SB Sequence A0216 73 SLDAREVI 0.640 49 SB Sequence A0216 144 SFGGALCV 0.630 54 WB Sequence A0216 216 GMTVAGVV 0.613 65 WB Sequence A0216 166 AAWMATYL 0.603 73 WB Sequence A0216 160 VLVSRIAA 0.583 91 WB Sequence A0216 212 WFLTGMTV 0.565 110 WB Sequence A0216 11 FLSYKLSQ 0.488 255 WB Sequence A0216 106 DLTSQLHI 0.487 258 WB Sequence A0216 133 GVNWGRIV 0.470 308 WB Sequence A0216 81 PMAAVKQA 0.469 311 WB Sequence A0216 118 AYQSFEQV 0.461 342 WB Sequence A0216 223 VLLGSLFS 0.442 417 WB Sequence A0216 147 GALCVESV 0.438 436 WB Sequence A0216 57 HLADSPAV 0.924 2 SB Sequence A0219 213 FLTGMTVA 0.668 36 SB Sequence A0219 153 SVDKEMQV 0.597 78 WB Sequence A0219 73 SLDAREVI 0.576 98 WB Sequence A0219 218 TVAGVVLL 0.517 185 WB Sequence A0219 192 ELYGNNAA 0.486 259 WB Sequence A0219 212 WFLTGMTV 0.458 352 WB Sequence A0219 166 AAWMATYL 0.455 362 WB Sequence A0219 106 DLTSQLHI 0.448 390 WB Sequence A0219 223 VLLGSLFS 0.431 471 WB Sequence A0219 12 LSYKLSQK 0.761 13 SB Sequence A0301 8 VVDFLSYK 0.551 128 WB Sequence A0301 224 LLGSLFSR 0.487 257 WB Sequence A0301 8 VVDFLSYK 0.751 14 SB Sequence A1101 12 LSYKLSQK 0.721 20 SB Sequence A1101 79 VIPMAAVK 0.509 203 WB Sequence A1101 124 QVVNELFR 0.472 302 WB Sequence A1101 7 LVVDFLSY 0.457 355 WB Sequence A1101 197 NAAAESRK 0.455 363 WB Sequence A1101 135 NWGRIVAF 0.600 75 WB Sequence A2301 138 RIVAFFSF 0.466 321 WB Sequence A2301 222 VVLLGSLF 0.461 339 WB Sequence A2301 135 NWGRIVAF 0.617 62 WB Sequence A2402 118 AYQSFEQV 0.569 105 WB Sequence A2403 78 EVIPMAAV 0.598 77 WB Sequence A2601 7 LVVDFLSY 0.541 144 WB Sequence A2601 78 EVIPMAAV 0.862 4 SB Sequence A2602 7 LVVDFLSY 0.797 9 SB Sequence A2602 112 HITPGTAY 0.755 14 SB Sequence A2602 97 ELRYRRAF 0.589 85 WB Sequence A2602 138 RIVAFFSF 0.529 164 WB Sequence A2602 112 HITPGTAY 0.597 78 WB Sequence A2902 7 LVVDFLSY 0.480 276 WB Sequence A2902 204 KGQERFNR 0.743 16 SB Sequence A3101 224 LLGSLFSR 0.697 26 SB Sequence A3101 157 EMQVLVSR 0.583 90 WB Sequence A3101 70 HSSSLDAR 0.577 97 WB Sequence A3101 83 AAVKQALR 0.539 146 WB Sequence A3101 95 EFELRYRR 0.509 201 WB Sequence A3101 124 QVVNELFR 0.453 369 WB Sequence A3101 12 LSYKLSQK 0.447 397 WB Sequence A3101 95 EFELRYRR 0.823 6 SB Sequence A3301 157 EMQVLVSR 0.738 16 SB Sequence A3301 94 DEFELRYR 0.650 43 SB Sequence A3301 201 ESRKGQER 0.606 71 WB Sequence A3301 224 LLGSLFSR 0.538 148 WB Sequence A3301 70 HSSSLDAR 0.463 332 WB Sequence A3301 124 QVVNELFR 0.803 8 SB Sequence A6801 70 HSSSLDAR 0.775 11 SB Sequence A6801 197 NAAAESRK 0.681 31 SB Sequence A6801 12 LSYKLSQK 0.647 45 SB Sequence A6801 157 EMQVLVSR 0.599 76 WB Sequence A6801 196 NNAAAESR 0.585 88 WB Sequence A6801 83 AAVKQALR 0.535 153 WB Sequence A6801 201 ESRKGQER 0.532 158 WB Sequence A6801 165 IAAWMATY 0.532 158 WB Sequence A6801 95 EFELRYRR 0.511 198 WB Sequence A6801 117 TAYQSFEQ 0.507 208 WB Sequence A6801 8 VVDFLSYK 0.481 273 WB Sequence A6801 94 DEFELRYR 0.457 357 WB Sequence A6801 26 FSDVEENR 0.442 418 WB Sequence A6801 224 LLGSLFSR 0.430 476 WB Sequence A6801 78 EVIPMAAV 0.888 3 SB Sequence A6802 218 TVAGVVLL 0.790 9 SB Sequence A6802 215 TGMTVAGV 0.742 16 SB Sequence A6802 217 MTVAGVVL 0.697 26 SB Sequence A6802 82 MAAVKQAL 0.633 52 WB Sequence A6802 57 HLADSPAV 0.549 131 WB Sequence A6802 207 ERFNRWFL 0.481 273 WB Sequence A6802 60 DSPAVNGA 0.473 300 WB Sequence A6802 192 ELYGNNAA 0.447 395 WB Sequence A6802 91 EAGDEFEL 0.436 444 WB Sequence A6802 78 EVIPMAAV 0.812 7 SB Sequence A6901 57 HLADSPAV 0.740 16 SB Sequence A6901 192 ELYGNNAA 0.570 104 WB Sequence A6901 217 MTVAGVVL 0.544 138 WB Sequence A6901 218 TVAGVVLL 0.507 206 WB Sequence A6901 91 EAGDEFEL 0.489 252 WB Sequence A6901 153 SVDKEMQV 0.437 441 WB Sequence A6901 212 WFLTGMTV 0.436 445 WB Sequence A6901 61 SPAVNGAT 0.657 41 SB Sequence B0702 82 MAAVKQAL 0.468 316 WB Sequence B0702 166 AAWMATYL 0.430 477 WB Sequence B0702 97 ELRYRRAF 0.589 85 WB Sequence B0801 7 LVVDFLSY 0.511 198 WB Sequence B1501 138 RIVAFFSF 0.493 240 WB Sequence B1501 112 HITPGTAY 0.492 243 WB Sequence B1501 165 IAAWMATY 0.473 300 WB Sequence B1501 97 ELRYRRAF 0.439 430 WB Sequence B1501 222 VVLLGSLF 0.433 461 WB Sequence B1501 206 QERFNRWF 0.528 165 WB Sequence B1801 5 RELVVDFL 0.517 185 WB Sequence B1801 122 FEQVVNEL 0.508 205 WB Sequence B1801 210 NRWFLTGM 0.510 200 WB Sequence B2705 165 IAAWMATY 0.806 8 SB Sequence B3501 7 LVVDFLSY 0.629 55 WB Sequence B3501 82 MAAVKQAL 0.591 83 WB Sequence B3501 112 HITPGTAY 0.543 140 WB Sequence B3501 75 DAREVIPM 0.516 187 WB Sequence B3501 142 FFSFGGAL 0.499 226 WB Sequence B3501 61 SPAVNGAT 0.478 283 WB Sequence B3501 166 AAWMATYL 0.476 289 WB Sequence B3501 217 MTVAGVVL 0.470 307 WB Sequence B3501 5 RELVVDFL 0.624 58 WB Sequence B4001 122 FEQVVNEL 0.618 62 WB Sequence B4001 5 RELVVDFL 0.442 420 WB Sequence B4002 156 KEMQVLVS 0.430 478 WB Sequence B4403 77 REVIPMAA 0.434 456 WB Sequence B4501 161 LVSRIAAW 0.626 57 WB Sequence B5801 165 IAAWMATY 0.593 81 WB Sequence B5801 16 LSQKGYSW 0.586 88 WB Sequence B5801 19 KGYSWSQF 0.543 141 WB Sequence B5801 138 RIVAFFSF 0.467 320 WB Sequence B5801 49 AINGNPSW 0.447 394 WB Sequence B5801 9.mers 104 FSDLTSQLH 0.482 270 WB Sequence A0101 143 FSFGGALCV 0.518 183 WB Sequence A0201 217 MTVAGVVLL 0.478 282 WB Sequence A0201 172 YLNDHLEPW 0.739 16 SB Sequence A0202 217 MTVAGVVLL 0.604 72 WB Sequence A0202 165 IAAWMATYL 0.568 107 WB Sequence A0202 213 FLTGMTVAG 0.564 111 WB Sequence A0202 11 FLSYKLSQK 0.520 179 WB Sequence A0202 161 LVSRIAAWM 0.450 382 WB Sequence A0202 8 VVDFLSYKL 0.449 387 WB Sequence A0202 192 ELYGNNAAA 0.447 394 WB Sequence A0202 81 PMAAVKQAL 0.437 441 WB Sequence A0202 216 GMTVAGVVL 0.436 448 WB Sequence A0202 214 LTGMTVAGV 0.691 28 SB Sequence A0203 217 MTVAGVVLL 0.609 69 WB Sequence A0203 165 IAAWMATYL 0.530 161 WB Sequence A0203 84 AVKQALREA 0.518 183 WB Sequence A0203 110 QLHITPGTA 0.507 206 WB Sequence A0203 172 YLNDHLEPW 0.493 240 WB Sequence A0203 117 TAYQSFEQV 0.473 300 WB Sequence A0203 11 FLSYKLSQK 0.447 396 WB Sequence A0203 214 LTGMTVAGV 0.504 213 WB Sequence A0204 217 MTVAGVVLL 0.475 291 WB Sequence A0204 109 SQLHITPGT 0.712 22 SB Sequence A0206 217 MTVAGVVLL 0.675 33 SB Sequence A0206 117 TAYQSFEQV 0.650 43 SB Sequence A0206 1 SQSNRELVV 0.648 45 SB Sequence A0206 143 FSFGGALCV 0.584 90 WB Sequence A0206 77 REVIPMAAV 0.572 103 WB Sequence A0206 165 IAAWMATYL 0.551 128 WB Sequence A0206 158 MQVLVSRIA 0.544 138 WB Sequence A0206 214 LTGMTVAGV 0.492 244 WB Sequence A0206 172 YLNDHLEPW 0.464 331 WB Sequence A0206 42 SEMETPSAI 0.440 426 WB Sequence A0206 192 ELYGNNAAA 0.863 4 SB Sequence A0211 143 FSFGGALCV 0.797 8 SB Sequence A0211 81 PMAAVKQAL 0.794 9 SB Sequence A0211 172 YLNDHLEPW 0.715 21 SB Sequence A0211 153 SVDKEMQVL 0.703 24 SB Sequence A0211 8 VVDFLSYKL 0.696 26 SB Sequence A0211 217 MTVAGVVLL 0.634 52 WB Sequence A0211 112 HITPGTAYQ 0.618 62 WB Sequence A0211 117 TAYQSFEQV 0.617 63 WB Sequence A0211 223 VLLGSLFSR 0.581 93 WB Sequence A0211 213 FLTGMTVAG 0.581 93 WB Sequence A0211 133 GVNWGRIVA 0.575 99 WB Sequence A0211 216 GMTVAGVVL 0.553 126 WB Sequence A0211 185 GGWDTFVEL 0.550 130 WB Sequence A0211 103 AFSDLTSQL 0.472 302 WB Sequence A0211 176 HLEPWIQEN 0.427 493 WB Sequence A0211 192 ELYGNNAAA 0.845 5 SB Sequence A0212 81 PMAAVKQAL 0.789 9 SB Sequence A0212 143 FSFGGALCV 0.702 25 SB Sequence A0212 172 YLNDHLEPW 0.673 34 SB Sequence A0212 223 VLLGSLFSR 0.573 101 WB Sequence A0212 8 VVDFLSYKL 0.561 115 WB Sequence A0212 153 SVDKEMQVL 0.535 153 WB Sequence A0212 213 FLTGMTVAG 0.521 178 WB Sequence A0212 118 AYQSFEQVV 0.476 290 WB Sequence A0212 192 ELYGNNAAA 0.741 16 SB Sequence A0216 81 PMAAVKQAL 0.710 22 SB Sequence A0216 143 FSFGGALCV 0.652 42 SB Sequence A0216 117 TAYQSFEQV 0.593 81 WB Sequence A0216 112 HITPGTAYQ 0.512 196 WB Sequence A0216 216 GMTVAGVVL 0.430 479 WB Sequence A0216 81 PMAAVKQAL 0.675 33 SB Sequence A0219 143 FSFGGALCV 0.652 43 SB Sequence A0219 192 ELYGNNAAA 0.541 142 WB Sequence A0219 117 TAYQSFEQV 0.497 232 WB Sequence A0219 172 YLNDHLEPW 0.459 348 WB Sequence A0219 223 VLLGSLFSR 0.456 361 WB Sequence A0219 214 LTGMTVAGV 0.450 384 WB Sequence A0219 --- 224 LLGSLFSRK 0.762 13 SB Sequence A0301 11 FLSYKLSQK 0.710 23 SB Sequence A0301 164 RIAAWMATY 0.698 26 SB Sequence A0301 223 VLLGSLFSR 0.615 64 WB Sequence A0301 7 LVVDFLSYK 0.497 231 WB Sequence A0301 7 LVVDFLSYK 0.767 12 SB Sequence A1101 224 LLGSLFSRK 0.612 66 WB Sequence A1101 223 VLLGSLFSR 0.595 79 WB Sequence A1101 164 RIAAWMATY 0.575 99 WB Sequence A1101 148 ALCVESVDK 0.529 163 WB Sequence A1101 78 EVIPMAAVK 0.509 201 WB Sequence A1101 11 FLSYKLSQK 0.430 477 WB Sequence A1101 99 RYRRAFSDL 0.690 28 SB Sequence A2301 135 NWGRIVAFF 0.644 47 SB Sequence A2301 137 GRIVAFFSF 0.459 346 WB Sequence A2301 135 NWGRIVAFF 0.739 16 SB Sequence A2402 99 RYRRAFSDL 0.550 129 WB Sequence A2402 99 RYRRAFSDL 0.748 15 SB Sequence A2403 121 SFEQVVNEL 0.557 120 WB Sequence A2403 118 AYQSFEQVV 0.487 256 WB Sequence A2403 6 ELVVDFLSY 0.532 158 WB Sequence A2601 164 RIAAWMATY 0.495 235 WB Sequence A2601 164 RIAAWMATY 0.923 2 SB Sequence A2602 6 ELVVDFLSY 0.873 3 SB Sequence A2602 161 LVSRIAAWM 0.677 32 SB Sequence A2602 153 SVDKEMQVL 0.639 49 SB Sequence A2602 78 EVIPMAAVK 0.496 234 WB Sequence A2602 217 MTVAGVVLL 0.481 273 WB Sequence A2602 111 LHITPGTAY 0.553 125 WB Sequence A2902 6 ELVVDFLSY 0.539 146 WB Sequence A2902 164 RIAAWMATY 0.463 334 WB Sequence A3002 82 MAAVKQALR 0.766 12 SB Sequence A3101 223 VLLGSLFSR 0.686 30 SB Sequence A3101 7 LVVDFLSYK 0.573 101 WB Sequence A3101 156 KEMQVLVSR 0.474 296 WB Sequence A3101 94 DEFELRYRR 0.721 20 SB Sequence A3301 82 MAAVKQALR 0.665 37 SB Sequence A3301 97 ELRYRRAFS 0.614 65 WB Sequence A3301 223 VLLGSLFSR 0.581 92 WB Sequence A3301 91 EAGDEFELR 0.532 157 WB Sequence A3301 25 QFSDVEENR 0.531 159 WB Sequence A3301 78 EVIPMAAVK 0.848 5 SB Sequence A6801 82 MAAVKQALR 0.813 7 SB Sequence A6801 7 LVVDFLSYK 0.786 10 SB Sequence A6801 91 EAGDEFELR 0.710 23 SB Sequence A6801 123 EQVVNELFR 0.635 51 WB Sequence A6801 11 FLSYKLSQK 0.558 119 WB Sequence A6801 94 DEFELRYRR 0.544 139 WB Sequence A6801 25 QFSDVEENR 0.540 145 WB Sequence A6801 196 NNAAAESRK 0.474 295 WB Sequence A6801 223 VLLGSLFSR 0.430 477 WB Sequence A6801 217 MTVAGVVLL 0.796 9 SB Sequence A6802 117 TAYQSFEQV 0.729 18 SB Sequence A6802 215 TGMTVAGVV 0.654 42 SB Sequence A6802 0 MSQSNRELV 0.587 86 WB Sequence A6802 21 YSWSQFSDV 0.549 131 WB Sequence A6802 143 FSFGGALCV 0.526 169 WB Sequence A6802 152 ESVDKEMQV 0.525 171 WB Sequence A6802 169 MATYLNDHL 0.520 180 WB Sequence A6802 192 ELYGNNAAA 0.509 202 WB Sequence A6802 140 VAFFSFGGA 0.500 222 WB Sequence A6802 214 LTGMTVAGV 0.464 330 WB Sequence A6802 165 IAAWMATYL 0.451 378 WB Sequence A6802 217 MTVAGVVLL 0.705 24 SB Sequence A6901 117 TAYQSFEQV 0.623 58 WB Sequence A6901 192 ELYGNNAAA 0.604 72 WB Sequence A6901 143 FSFGGALCV 0.589 85 WB Sequence A6901 214 LTGMTVAGV 0.557 120 WB Sequence A6901 21 YSWSQFSDV 0.489 252 WB Sequence A6901 36 APEGTESEM 0.519 181 WB Sequence B0702 61 SPAVNGATG 0.454 369 WB Sequence B0702 114 TPGTAYQSF 0.450 382 WB Sequence B0702 96 FELRYRRAF 0.497 229 WB Sequence B0801 164 RIAAWMATY 0.586 87 WB Sequence B1501 88 ALREAGDEF 0.520 180 WB Sequence B1501 96 FELRYRRAF 0.752 14 SB Sequence B1801 206 QERFNRWFL 0.592 82 WB Sequence B1801 122 FEQVVNELF 0.523 174 WB Sequence B1801 182 QENGGWDTF 0.476 290 WB Sequence B1801 137 GRIVAFFSF 0.554 124 WB Sequence B2705 101 RRAFSDLTS 0.434 459 WB Sequence B2705 114 TPGTAYQSF 0.705 24 SB Sequence B3501 165 IAAWMATYL 0.649 44 SB Sequence B3501 36 APEGTESEM 0.540 144 WB Sequence B3501 6 ELVVDFLSY 0.531 159 WB Sequence B3501 111 LHITPGTAY 0.437 441 WB Sequence B3501 53 NPSWHLADS 0.429 480 WB Sequence B3501 164 RIAAWMATY 0.428 485 WB Sequence B3501 90 REAGDEFEL 0.788 9 SB Sequence B4001 206 QERFNRWFL 0.597 78 WB Sequence B4001 182 QENGGWDTF 0.525 170 WB Sequence B4001 122 FEQVVNELF 0.453 370 WB Sequence B4001 96 FELRYRRAF 0.446 399 WB Sequence B4001 42 SEMETPSAI 0.504 215 WB Sequence B4002 96 FELRYRRAF 0.473 299 WB Sequence B4002 182 QENGGWDTF 0.434 455 WB Sequence B4402 42 SEMETPSAI 0.467 319 WB Sequence B4403 5 RELVVDFLS 0.444 407 WB Sequence B4403 77 REVIPMAAV 0.438 438 WB Sequence B4501 165 IAAWMATYL 0.442 416 WB Sequence B5301 80 IPMAAVKQA 0.716 21 SB Sequence B5401 48 SAINGNPSW 0.641 48 SB Sequence B5801 15 KLSQKGYSW 0.596 79 WB Sequence B5801 165 IAAWMATYL 0.559 118 WB Sequence B5801 172 YLNDHLEPW 0.506 208 WB Sequence B5801 10-mers 104 FSDLTSQLHI 0.427 492 WB Sequence A0101 172 YLNDHLEPWI 0.866 4 SB Sequence A0201 213 FLTGMTVAGV 0.841 5 SB Sequence A0201 164 RIAAWMATYL 0.651 43 SB Sequence A0201 168 WMATYLNDHL 0.573 101 WB Sequence A0201 7 LVVDFLSYKL 0.524 173 WB Sequence A0201 73 SLDAREVIPM 0.491 246 WB Sequence A0201 160 VLVSRIAAWM 0.486 259 WB Sequence A0201 153 SVDKEMQVLV 0.473 298 WB Sequence A0201 216 GMTVAGVVLL 0.444 411 WB Sequence A0201 213 FLTGMTVAGV 0.811 7 SB Sequence A0202 168 WMATYLNDHL 0.772 11 SB Sequence A0202 164 RIAAWMATYL 0.763 13 SB Sequence A0202 7 LVVDFLSYKL 0.651 43 SB Sequence A0202 102 RAFSDLTSQL 0.617 63 WB Sequence A0202 73 SLDAREVIPM 0.616 63 WB Sequence A0202 172 YLNDHLEPWI 0.587 87 WB Sequence A0202 216 GMTVAGVVLL 0.496 233 WB Sequence A0202 145 FGGALCVESV 0.480 276 WB Sequence A0202 160 VLVSRIAAWM 0.430 476 WB Sequence A0202 213 FLTGMTVAGV 0.936 2 SB Sequence A0203 172 YLNDHLEPWI 0.891 3 SB Sequence A0203 164 RIAAWMATYL 0.837 5 SB Sequence A0203 168 WMATYLNDHL 0.647 45 SB Sequence A0203 160 VLVSRIAAWM 0.613 66 WB Sequence A0203 139 IVAFFSFGGA 0.596 79 WB Sequence A0203 7 LVVDFLSYKL 0.581 92 WB Sequence A0203 125 VVNELFRDGV 0.570 105 WB Sequence A0203 216 GMTVAGVVLL 0.476 289 WB Sequence A0203 102 RAFSDLTSQL 0.470 308 WB Sequence A0203 214 LTGMTVAGVV 0.468 315 WB Sequence A0203 116 GTAYQSFEQV 0.463 335 WB Sequence A0203 213 FLTGMTVAGV 0.697 26 SB Sequence A0204 172 YLNDHLEPWI 0.664 37 SB Sequence A0204 73 SLDAREVIPM 0.477 287 WB Sequence A0204 164 RIAAWMATYL 0.476 290 WB Sequence A0204 7 LVVDFLSYKL 0.468 317 WB Sequence A0204 49 AINGNPSWHL 0.452 374 WB Sequence A0204 213 FLTGMTVAGV 0.869 4 SB Sequence A0206 164 RIAAWMATYL 0.809 7 SB Sequence A0206 172 YLNDHLEPWI 0.722 20 SB Sequence A0206 158 MQVLVSRIAA 0.689 28 SB Sequence A0206 7 LVVDFLSYKL 0.684 30 SB Sequence A0206 168 WMATYLNDHL 0.680 31 SB Sequence A0206 109 SQLHITPGTA 0.652 43 SB Sequence A0206 116 GTAYQSFEQV 0.572 102 WB Sequence A0206 153 SVDKEMQVLV 0.558 119 WB Sequence A0206 102 RAFSDLTSQL 0.543 140 WB Sequence A0206 156 KEMQVLVSRI 0.508 204 WB Sequence A0206 181 IQENGGWDTF 0.508 205 WB Sequence A0206 139 IVAFFSFGGA 0.495 235 WB Sequence A0206 125 VVNELFRDGV 0.483 269 WB Sequence A0206 117 TAYQSFEQVV 0.450 383 WB Sequence A0206 213 FLTGMTVAGV 0.966 1 SB Sequence A0211 172 YLNDHLEPWI 0.951 1 SB Sequence A0211 153 SVDKEMQVLV 0.905 2 SB Sequence A0211 73 SLDAREVIPM 0.826 6 SB Sequence A0211 216 GMTVAGVVLL 0.737 17 SB Sequence A0211 7 LVVDFLSYKL 0.730 18 SB Sequence A0211 164 RIAAWMATYL 0.711 22 SB Sequence A0211 125 VVNELFRDGV 0.687 29 SB Sequence A0211 49 AINGNPSWHL 0.686 29 SB Sequence A0211 168 WMATYLNDHL 0.685 30 SB Sequence A0211 117 TAYQSFEQVV 0.633 52 WB Sequence A0211 160 VLVSRIAAWM 0.632 53 WB Sequence A0211 142 FFSFGGALCV 0.567 107 WB Sequence A0211 223 VLLGSLFSRK 0.498 228 WB Sequence A0211 102 RAFSDLTSQL 0.453 372 WB Sequence A0211 116 GTAYQSFEQV 0.429 481 WB Sequence A0211 213 FLTGMTVAGV 0.932 2 SB Sequence A0212 172 YLNDHLEPWI 0.916 2 SB Sequence A0212 153 SVDKEMQVLV 0.742 16 SB Sequence A0212 168 WMATYLNDHL 0.697 26 SB Sequence A0212 125 VVNELFRDGV 0.695 27 SB Sequence A0212 7 LVVDFLSYKL 0.648 45 SB Sequence A0212 160 VLVSRIAAWM 0.604 72 WB Sequence A0212 73 SLDAREVIPM 0.594 80 WB Sequence A0212 49 AINGNPSWHL 0.570 104 WB Sequence A0212 164 RIAAWMATYL 0.550 129 WB Sequence A0212 142 FFSFGGALCV 0.494 238 WB Sequence A0212 223 VLLGSLFSRK 0.487 258 WB Sequence A0212 117 TAYQSFEQVV 0.482 270 WB Sequence A0212 192 ELYGNNAAAE 0.475 293 WB Sequence A0212 216 GMTVAGVVLL 0.440 426 WB Sequence A0212 213 FLTGMTVAGV 0.911 2 SB Sequence A0216 172 YLNDHLEPWI 0.869 4 SB Sequence A0216 153 SVDKEMQVLV 0.772 11 SB Sequence A0216 168 WMATYLNDHL 0.696 26 SB Sequence A0216 164 RIAAWMATYL 0.695 27 SB Sequence A0216 49 AINGNPSWHL 0.680 31 SB Sequence A0216 160 VLVSRIAAWM 0.657 41 SB Sequence A0216 7 LVVDFLSYKL 0.643 47 SB Sequence A0216 73 SLDAREVIPM 0.617 62 WB Sequence A0216 216 GMTVAGVVLL 0.588 85 WB Sequence A0216 117 TAYQSFEQVV 0.530 161 WB Sequence A0216 142 FFSFGGALCV 0.487 256 WB Sequence A0216 116 GTAYQSFEQV 0.444 408 WB Sequence A0216 213 FLTGMTVAGV 0.927 2 SB Sequence A0219 172 YLNDHLEPWI 0.884 3 SB Sequence A0219 168 WMATYLNDHL 0.611 67 WB Sequence A0219 49 AINGNPSWHL 0.543 140 WB Sequence A0219 7 LVVDFLSYKL 0.539 146 WB Sequence A0219 153 SVDKEMQVLV 0.533 156 WB Sequence A0219 164 RIAAWMATYL 0.449 387 WB Sequence A0219 73 SLDAREVIPM 0.445 404 WB Sequence A0219 160 VLVSRIAAWM 0.441 421 WB Sequence A0219 223 VLLGSLFSRK 0.767 12 SB Sequence A0301 6 ELVVDFLSYK 0.504 213 WB Sequence A0301 147 GALCVESVDK 0.488 253 WB Sequence A0301 222 VVLLGSLFSR 0.457 356 WB Sequence A0301 77 REVIPMAAVK 0.453 372 WB Sequence A0301 223 VLLGSLFSRK 0.742 16 SB Sequence A1101 222 VVLLGSLFSR 0.681 31 SB Sequence A1101 147 GALCVESVDK 0.515 190 WB Sequence A1101 24 SQFSDVEENR 0.470 310 WB Sequence A1101 121 SFEQVVNELF 0.581 92 WB Sequence A2301 171 TYLNDHLEPW 0.547 134 WB Sequence A2301 121 SFEQVVNELF 0.528 165 WB Sequence A2402 171 TYLNDHLEPW 0.520 180 WB Sequence A2402 113 ITPGTAYQSF 0.460 343 WB Sequence A2402 171 TYLNDHLEPW 0.739 16 SB Sequence A2403 121 SFEQVVNELF 0.546 136 WB Sequence A2403 113 ITPGTAYQSF 0.508 204 WB Sequence A2403 35 EAPEGTESEM 0.448 390 WB Sequence A2601 164 RIAAWMATYL 0.626 57 WB Sequence A2602 113 ITPGTAYQSF 0.581 92 WB Sequence A2602 160 VLVSRIAAWM 0.553 126 WB Sequence A2602 35 EAPEGTESEM 0.507 207 WB Sequence A2602 152 ESVDKEMQVL 0.490 249 WB Sequence A2602 95 EFELRYRRAF 0.483 268 WB Sequence A2602 110 QLHITPGTAY 0.506 209 WB Sequence A2902 222 VVLLGSLFSR 0.683 30 SB Sequence A3101 129 LFRDGVNWGR 0.667 36 SB Sequence A3101 202 SRKGQERFNR 0.608 69 WB Sequence A3101 81 PMAAVKQALR 0.521 177 WB Sequence A3101 222 VVLLGSLFSR 0.572 103 WB Sequence A3301 129 LFRDGVNWGR 0.553 126 WB Sequence A3301 10 DFLSYKLSQK 0.470 308 WB Sequence A3301 6 ELVVDFLSYK 0.702 25 SB Sequence A6801 24 SQFSDVEENR 0.532 158 WB Sequence A6801 222 VVLLGSLFSR 0.516 188 WB Sequence A6801 194 YGNNAAAESR 0.493 240 WB Sequence A6801 78 EVIPMAAVKQ 0.454 368 WB Sequence A6801 169 MATYLNDHLE 0.448 394 WB Sequence A6801 139 IVAFFSFGGA 0.742 16 SB Sequence A6802 116 GTAYQSFEQV 0.673 34 SB Sequence A6802 7 LVVDFLSYKL 0.659 39 SB Sequence A6802 120 QSFEQVVNEL 0.618 62 WB Sequence A6802 213 FLTGMTVAGV 0.577 96 WB Sequence A6802 117 TAYQSFEQVV 0.561 115 WB Sequence A6802 164 RIAAWMATYL 0.519 182 WB Sequence A6802 65 NGATGHSSSL 0.496 234 WB Sequence A6802 218 TVAGVVLLGS 0.491 246 WB Sequence A6802 145 FGGALCVESV 0.474 294 WB Sequence A6802 125 VVNELFRDGV 0.465 328 WB Sequence A6802 161 LVSRIAAWMA 0.451 380 WB Sequence A6802 215 TGMTVAGVVL 0.450 382 WB Sequence A6802 153 SVDKEMQVLV 0.534 155 WB Sequence A6901 213 FLTGMTVAGV 0.527 166 WB Sequence A6901 117 TAYQSFEQVV 0.466 324 WB Sequence A6901 7 LVVDFLSYKL 0.451 378 WB Sequence A6901 164 RIAAWMATYL 0.443 412 WB Sequence A6901 116 GTAYQSFEQV 0.427 493 WB Sequence A6901 80 IPMAAVKQAL 0.704 24 SB Sequence B0702 17 SQKGYSWSQF 0.572 102 WB Sequence B1501 110 QLHITPGTAY 0.557 121 WB Sequence B1501 133 GVNWGRIVAF 0.548 132 WB Sequence B1501 181 IQENGGWDTF 0.522 175 WB Sequence B1501 12 LSYKLSQKGY 0.455 364 WB Sequence B1501 5 RELVVDFLSY 0.759 13 SB Sequence B1801 163 SRIAAWMATY 0.588 86 WB Sequence B2705 101 RRAFSDLTSQ 0.461 340 WB Sequence B2705 80 IPMAAVKQAL 0.609 69 WB Sequence B3501 178 EPWIQENGGW 0.604 72 WB Sequence B3501 91 EAGDEFELRY 0.566 109 WB Sequence B3501 35 EAPEGTESEM 0.563 112 WB Sequence B3501 87 QALREAGDEF 0.508 206 WB Sequence B3501 61 SPAVNGATGH 0.490 249 WB Sequence B3501 46 TPSAINGNPS 0.483 269 WB Sequence B3501 133 GVNWGRIVAF 0.455 362 WB Sequence B3501 140 VAFFSFGGAL 0.454 367 WB Sequence B3501 190 FVELYGNNAA 0.439 430 WB Sequence B3501 200 AESRKGQERF 0.453 370 WB Sequence B4501 178 EPWIQENGGW 0.603 73 WB Sequence B5301 2 QSNRELVVDF 0.474 295 WB Sequence B5801 159 QVLVSRIAAW 0.467 320 WB Sequence B5801 47 PSAINGNPSW 0.437 444 WB Sequence B5801 11-mers 213 FLTGMTVAGVV 0.627 56 WB Sequence A0201 73 SLDAREVIPMA 0.561 115 WB Sequence A0201 160 VLVSRIAAWMA 0.547 135 WB Sequence A0201 57 HLADSPAVNGA 0.539 147 WB Sequence A0201 172 YLNDHLEPWIQ 0.480 278 WB Sequence A0201 88 ALREAGDEFEL 0.470 309 WB Sequence A0201 119 YQSFEQVVNEL 0.426 497 WB Sequence A0201 57 HLADSPAVNGA 0.763 12 SB Sequence A0202 213 FLTGMTVAGVV 0.754 14 SB Sequence A0202 119 YQSFEQVVNEL 0.734 17 SB Sequence A0202 88 ALREAGDEFEL 0.679 32 SB Sequence A0202 172 YLNDHLEPWIQ 0.611 67 WB Sequence A0202 139 IVAFFSFGGAL 0.558 119 WB Sequence A0202 218 TVAGVVLLGSL 0.537 149 WB Sequence A0202 160 VLVSRIAAWMA 0.525 170 WB Sequence A0202 15 KLSQKGYSWSQ 0.450 382 WB Sequence A0202 6 ELVVDFLSYKL 0.449 387 WB Sequence A0202 73 SLDAREVIPMA 0.446 401 WB Sequence A0202 213 FLTGMTVAGVV 0.864 4 SB Sequence A0203 57 HLADSPAVNGA 0.844 5 SB Sequence A0203 138 RIVAFFSFGGA 0.752 14 SB Sequence A0203 160 VLVSRIAAWMA 0.649 44 SB Sequence A0203 218 TVAGVVLLGSL 0.619 61 WB Sequence A0203 88 ALREAGDEFEL 0.604 72 WB Sequence A0203 119 YQSFEQVVNEL 0.567 108 WB Sequence A0203 172 YLNDHLEPWIQ 0.565 110 WB Sequence A0203 49 AINGNPSWHLA 0.562 114 WB Sequence A0203 209 FNRWFLTGMTV 0.494 239 WB Sequence A0203 139 IVAFFSFGGAL 0.487 257 WB Sequence A0203 73 SLDAREVIPMA 0.480 276 WB Sequence A0203 82 MAAVKQALREA 0.430 477 WB Sequence A0203 124 QVVNELFRDGV 0.426 496 WB Sequence A0203 213 FLTGMTVAGVV 0.584 90 WB Sequence A0204 88 ALREAGDEFEL 0.526 168 WB Sequence A0204 160 VLVSRIAAWMA 0.517 185 WB Sequence A0204 172 YLNDHLEPWIQ 0.517 186 WB Sequence A0204 73 SLDAREVIPMA 0.485 263 WB Sequence A0204 213 FLTGMTVAGVV 0.746 15 SB Sequence A0206 138 RIVAFFSFGGA 0.725 19 SB Sequence A0206 181 IQENGGWDTFV 0.704 24 SB Sequence A0206 119 YQSFEQVVNEL 0.671 35 SB Sequence A0206 48 SAINGNPSWHL 0.664 38 SB Sequence A0206 124 QVVNELFRDGV 0.619 62 WB Sequence A0206 160 VLVSRIAAWMA 0.584 90 WB Sequence A0206 86 KQALREAGDEF 0.547 134 WB Sequence A0206 57 HLADSPAVNGA 0.509 201 WB Sequence A0206 218 TVAGVVLLGSL 0.456 358 WB Sequence A0206 88 ALREAGDEFEL 0.442 420 WB Sequence A0206 109 SQLHITPGTAY 0.441 422 WB Sequence A0206 213 FLTGMTVAGVV 0.943 1 SB Sequence A0211 73 SLDAREVIPMA 0.876 3 SB Sequence A0211 172 YLNDHLEPWIQ 0.852 4 SB Sequence A0211 88 ALREAGDEFEL 0.799 8 SB Sequence A0211 57 HLADSPAVNGA 0.787 10 SB Sequence A0211 160 VLVSRIAAWMA 0.759 13 SB Sequence A0211 15 KLSQKGYSWSQ 0.743 16 SB Sequence A0211 6 ELVVDFLSYKL 0.682 31 SB Sequence A0211 218 TVAGVVLLGSL 0.628 55 WB Sequence A0211 49 AINGNPSWHLA 0.612 66 WB Sequence A0211 212 WFLTGMTVAGV 0.577 97 WB Sequence A0211 141 AFFSFGGALCV 0.571 103 WB Sequence A0211 144 SFGGALCVESV 0.569 105 WB Sequence A0211 79 VIPMAAVKQAL 0.568 107 WB Sequence A0211 124 QVVNELFRDGV 0.535 152 WB Sequence A0211 130 FRDGVNWGRIV 0.516 187 WB Sequence A0211 48 SAINGNPSWHL 0.515 189 WB Sequence A0211 192 ELYGNNAAAES 0.504 214 WB Sequence A0211 150 CVESVDKEMQV 0.489 252 WB Sequence A0211 116 GTAYQSFEQVV 0.452 376 WB Sequence A0211 139 IVAFFSFGGAL 0.444 411 WB Sequence A0211 213 FLTGMTVAGVV 0.824 6 SB Sequence A0212 172 YLNDHLEPWIQ 0.812 7 SB Sequence A0212 88 ALREAGDEFEL 0.779 10 SB Sequence A0212 73 SLDAREVIPMA 0.745 15 SB Sequence A0212 57 HLADSPAVNGA 0.714 22 SB Sequence A0212 160 VLVSRIAAWMA 0.681 31 SB Sequence A0212 79 VIPMAAVKQAL 0.604 72 WB Sequence A0212 15 KLSQKGYSWSQ 0.568 107 WB Sequence A0212 212 WFLTGMTVAGV 0.504 213 WB Sequence A0212 6 ELVVDFLSYKL 0.451 380 WB Sequence A0212 130 FRDGVNWGRIV 0.431 473 WB Sequence A0212 213 FLTGMTVAGVV 0.862 4 SB Sequence A0216 88 ALREAGDEFEL 0.821 6 SB Sequence A0216 73 SLDAREVIPMA 0.744 16 SB Sequence A0216 160 VLVSRIAAWMA 0.649 44 SB Sequence A0216 150 CVESVDKEMQV 0.641 48 SB Sequence A0216 57 HLADSPAVNGA 0.595 79 WB Sequence A0216 144 SFGGALCVESV 0.591 83 WB Sequence A0216 172 YLNDHLEPWIQ 0.581 92 WB Sequence A0216 15 KLSQKGYSWSQ 0.561 115 WB Sequence A0216 6 ELVVDFLSYKL 0.544 138 WB Sequence A0216 218 TVAGVVLLGSL 0.534 154 WB Sequence A0216 141 AFFSFGGALCV 0.526 168 WB Sequence A0216 181 IQENGGWDTFV 0.497 231 WB Sequence A0216 124 QVVNELFRDGV 0.490 249 WB Sequence A0216 79 VIPMAAVKQAL 0.487 257 WB Sequence A0216 192 ELYGNNAAAES 0.478 283 WB Sequence A0216 48 SAINGNPSWHL 0.468 315 WB Sequence A0216 212 WFLTGMTVAGV 0.437 441 WB Sequence A0216 49 AINGNPSWHLA 0.436 447 WB Sequence A0216 213 FLTGMTVAGVV 0.781 10 SB Sequence A0219 57 HLADSPAVNGA 0.730 18 SB Sequence A0219 172 YLNDHLEPWIQ 0.695 27 SB Sequence A0219 73 SLDAREVIPMA 0.609 68 WB Sequence A0219 88 ALREAGDEFEL 0.549 131 WB Sequence A0219 212 WFLTGMTVAGV 0.524 172 WB Sequence A0219 160 VLVSRIAAWMA 0.499 225 WB Sequence A0219 222 VVLLGSLFSRK 0.688 29 SB Sequence A0301 222 VVLLGSLFSRK 0.786 10 SB Sequence A1101 221 GVVLLGSLFSR 0.596 78 WB Sequence A1101 67 ATGHSSSLDAR 0.505 212 WB Sequence A1101 5 RELVVDFLSYK 0.428 489 WB Sequence A1101 135 NWGRIVAFFSF 0.695 26 SB Sequence A2301 171 TYLNDHLEPWI 0.576 98 WB Sequence A2301 167 AWMATYLNDHL 0.534 154 WB Sequence A2301 13 SYKLSQKGYSW 0.531 159 WB Sequence A2301 135 NWGRIVAFFSF 0.746 15 SB Sequence A2402 171 TYLNDHLEPWI 0.746 15 SB Sequence A2402 167 AWMATYLNDHL 0.520 180 WB Sequence A2402 171 TYLNDHLEPWI 0.660 39 SB Sequence A2403 167 AWMATYLNDHL 0.523 174 WB Sequence A2403 13 SYKLSQKGYSW 0.523 174 WB Sequence A2403 112 HITPGTAYQSF 0.431 473 WB Sequence A2403 159 QVLVSRIAAWM 0.640 49 SB Sequence A2602 112 HITPGTAYQSF 0.573 101 WB Sequence A2602 180 WIQENGGWDTF 0.518 183 WB Sequence A2602 11 FLSYKLSQKGY 0.516 188 WB Sequence A2602 132 DGVNWGRIVAF 0.462 336 WB Sequence A2602 218 TVAGVVLLGSL 0.443 415 WB Sequence A2602 109 SQLHITPGTAY 0.516 188 WB Sequence A2902 222 VVLLGSLFSRK 0.435 453 WB Sequence A3001 99 RYRRAFSDLTS 0.428 486 WB Sequence A3001 221 GVVLLGSLFSR 0.598 77 WB Sequence A3101 121 SFEQVVNELFR 0.552 127 WB Sequence A3101 201 ESRKGQERFNR 0.511 198 WB Sequence A3101 67 ATGHSSSLDAR 0.475 292 WB Sequence A3101 5 RELVVDFLSYK 0.442 417 WB Sequence A3101 193 LYGNNAAAESR 0.435 449 WB Sequence A3101 201 ESRKGQERFNR 0.690 28 SB Sequence A3301 128 ELFRDGVNWGR 0.634 52 WB Sequence A3301 91 EAGDEFELRYR 0.538 148 WB Sequence A3301 121 SFEQVVNELFR 0.472 303 WB Sequence A3301 221 GVVLLGSLFSR 0.447 396 WB Sequence A3301 95 EFELRYRRAFS 0.435 449 WB Sequence A3301 128 ELFRDGVNWGR 0.739 16 SB Sequence A6801 23 WSQFSDVEENR 0.667 36 SB Sequence A6801 201 ESRKGQERFNR 0.666 36 SB Sequence A6801 91 EAGDEFELRYR 0.643 47 SB Sequence A6801 221 GVVLLGSLFSR 0.638 49 SB Sequence A6801 80 IPMAAVKQALR 0.566 109 WB Sequence A6801 121 SFEQVVNELFR 0.536 151 WB Sequence A6801 218 TVAGVVLLGSL 0.796 9 SB Sequence A6802 124 QVVNELFRDGV 0.712 22 SB Sequence A6802 139 IVAFFSFGGAL 0.684 30 SB Sequence A6802 152 ESVDKEMQVLV 0.613 65 WB Sequence A6802 215 TGMTVAGVVLL 0.561 116 WB Sequence A6802 6 ELVVDFLSYKL 0.551 129 WB Sequence A6802 138 RIVAFFSFGGA 0.548 132 WB Sequence A6802 188 DTFVELYGNNA 0.530 161 WB Sequence A6802 78 EVIPMAAVKQA 0.516 188 WB Sequence A6802 116 GTAYQSFEQVV 0.514 191 WB Sequence A6802 75 DAREVIPMAAV 0.509 203 WB Sequence A6802 57 HLADSPAVNGA 0.508 206 WB Sequence A6802 217 MTVAGVVLLGS 0.480 277 WB Sequence A6802 45 ETPSAINGNPS 0.479 279 WB Sequence A6802 213 FLTGMTVAGVV 0.470 308 WB Sequence A6802 70 HSSSLDAREVI 0.447 397 WB Sequence A6802 48 SAINGNPSWHL 0.541 143 WB Sequence A6901 75 DAREVIPMAAV 0.527 166 WB Sequence A6901 152 ESVDKEMQVLV 0.511 199 WB Sequence A6901 57 HLADSPAVNGA 0.485 263 WB Sequence A6901 54 PSWHLADSPAV 0.469 312 WB Sequence A6901 212 WFLTGMTVAGV 0.453 369 WB Sequence A6901 78 EVIPMAAVKQA 0.442 417 WB Sequence A6901 6 ELVVDFLSYKL 0.442 417 WB Sequence A6901 218 TVAGVVLLGSL 0.430 475 WB Sequence A6901 188 DTFVELYGNNA 0.427 494 WB Sequence A6901 139 IVAFFSFGGAL 0.518 183 WB Sequence B0702 53 NPSWHLADSPA 0.499 224 WB Sequence B0702 61 SPAVNGATGHS 0.457 355 WB Sequence B0702 109 SQLHITPGTAY 0.605 72 WB Sequence B1501 86 KQALREAGDEF 0.567 108 WB Sequence B1501 1 SQSNRELVVDF 0.540 144 WB Sequence B1501 119 YQSFEQVVNEL 0.515 189 WB Sequence B1501 158 MQVLVSRIAAW 0.512 196 WB Sequence B1501 162 VSRIAAWMATY 0.477 285 WB Sequence B1501 11 FLSYKLSQKGY 0.474 294 WB Sequence B1501 180 WIQENGGWDTF 0.473 299 WB Sequence B1501 120 QSFEQVVNELF 0.450 386 WB Sequence B1501 112 HITPGTAYQSF 0.447 394 WB Sequence B1501 133 GVNWGRIVAFF 0.433 463 WB Sequence B1501 94 DEFELRYRRAF 0.829 6 SB Sequence B1801 90 REAGDEFELRY 0.560 116 WB Sequence B1801 109 SQLHITPGTAY 0.539 146 WB Sequence B1801 151 VESVDKEMQVL 0.476 288 WB Sequence B1801 177 LEPWIQENGGW 0.466 321 WB Sequence B1801 209 FNRWFLTGMTV 0.444 409 WB Sequence B1801 101 RRAFSDLTSQL 0.563 113 WB Sequence B2705 163 SRIAAWMATYL 0.470 310 WB Sequence B2705 53 NPSWHLADSPA 0.623 59 WB Sequence B3501 46 TPSAINGNPSW 0.485 263 WB Sequence B3501 180 WIQENGGWDTF 0.474 297 WB Sequence B3501 132 DGVNWGRIVAF 0.442 419 WB Sequence B3501 119 YQSFEQVVNEL 0.610 68 WB Sequence B3901 151 VESVDKEMQVL 0.492 243 WB Sequence B4001 40 TESEMETPSAI 0.446 402 WB Sequence B4002 30 EENRTEAPEGT 0.498 228 WB Sequence B4501 46 TPSAINGNPSW 0.772 11 SB Sequence B5301 53 NPSWHLADSPA 0.430 474 WB Sequence B5401 170 ATYLNDHLEPW 0.540 145 WB Sequence B5701 170 ATYLNDHLEPW 0.537 150 WB Sequence B5801 120 QSFEQVVNELF 0.495 235 WB Sequence B5801 SEQ ID NOS.: 45801-46593

Preferred fragments of Bcl-2 capable of interacting with one or more MHC class 1 molecules are listed in table C below.

TABLE C Prediction of cancer antigen Bcl-2 specific MHC class1, 8-, 9-, 10-, 11-mer peptide binders for 42 MHC class 1 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/ NetMHC/ database. The MHC class 1 molecules for which no binders were found are not listed. pos peptide logscore affinity (nM) Bind Level Protein Name Allele 8-mer 84 ALSPVPPV 0.783 10 SB Sequence A0201 218 TLLSLALV 0.723 20 SB Sequence A0201 173 ALWMTEYL 0.682 31 SB Sequence A0201 154 GVMCVESV 0.630 54 WB Sequence A0201 207 PLFDFSWL 0.488 253 WB Sequence A0201 215 SLKTLLSL 0.449 387 WB Sequence A0201 84 ALSPVPPV 0.710 23 SB Sequence A0202 213 WLSLKTLL 0.709 23 SB Sequence A0202 215 SLKTLLSL 0.661 39 SB Sequence A0202 207 PLFDFSWL 0.653 42 SB Sequence A0202 173 ALWMTEYL 0.631 54 WB Sequence A0202 154 GVMCVESV 0.630 55 WB Sequence A0202 218 TLLSLALV 0.610 68 WB Sequence A0202 113 EMSSQLHL 0.570 105 WB Sequence A0202 224 LVGACITL 0.534 154 WB Sequence A0202 129 FATVVEEL 0.512 195 WB Sequence A0202 167 PLVDNIAL 0.508 204 WB Sequence A0202 179 YLNRHLHT 0.435 453 WB Sequence A0202 209 FDFSWLSL 0.432 464 WB Sequence A0202 84 ALSPVPPV 0.909 2 SB Sequence A0203 215 SLKTLLSL 0.853 4 SB Sequence A0203 154 GVMCVESV 0.754 14 SB Sequence A0203 179 YLNRHLHT 0.682 31 SB Sequence A0203 218 TLLSLALV 0.673 34 SB Sequence A0203 213 WLSLKTLL 0.665 37 SB Sequence A0203 140 GVNWGRIV 0.581 92 WB Sequence A0203 123 FTARGRFA 0.523 174 WB Sequence A0203 173 ALWMTEYL 0.497 229 WB Sequence A0203 207 PLFDFSWL 0.478 284 WB Sequence A0203 84 ALSPVPPV 0.763 13 SB Sequence A0204 173 ALWMTEYL 0.541 144 WB Sequence A0204 218 TLLSLALV 0.526 168 WB Sequence A0204 154 GVMCVESV 0.478 283 WB Sequence A0204 224 LVGACITL 0.451 381 WB Sequence A0204 84 ALSPVPPV 0.764 12 SB Sequence A0206 154 GVMCVESV 0.743 16 SB Sequence A0206 116 SQLHLTPF 0.737 17 SB Sequence A0206 218 TLLSLALV 0.714 21 SB Sequence A0206 145 RIVAFFEF 0.623 58 WB Sequence A0206 217 KTLLSLAL 0.574 100 WB Sequence A0206 173 ALWMTEYL 0.538 148 WB Sequence A0206 224 LVGACITL 0.463 334 WB Sequence A0206 123 FTARGRFA 0.462 335 WB Sequence A0206 213 WLSLKTLL 0.451 378 WB Sequence A0206 129 FATVVEEL 0.450 383 WB Sequence A0206 97 RQAGDDFS 0.436 445 WB Sequence A0206 84 ALSPVPPV 0.956 1 SB Sequence A0211 218 TLLSLALV 0.954 1 SB Sequence A0211 173 ALWMTEYL 0.935 2 SB Sequence A0211 207 PLFDFSWL 0.934 2 SB Sequence A0211 167 PLVDNIAL 0.888 3 SB Sequence A0211 215 SLKTLLSL 0.819 7 SB Sequence A0211 213 WLSLKTLL 0.780 10 SB Sequence A0211 179 YLNRHLHT 0.716 21 SB Sequence A0211 113 EMSSQLHL 0.686 29 SB Sequence A0211 140 GVNWGRIV 0.668 36 SB Sequence A0211 154 GVMCVESV 0.578 95 WB Sequence A0211 148 AFFEFGGV 0.534 154 WB Sequence A0211 87 PVPPVVHL 0.512 197 WB Sequence A0211 228 CITLGAYL 0.500 223 WB Sequence A0211 224 LVGACITL 0.500 223 WB Sequence A0211 223 ALVGACIT 0.479 281 WB Sequence A0211 27 YEWDAGDV 0.472 303 WB Sequence A0211 151 EFGGVMCV 0.452 377 WB Sequence A0211 221 SLALVGAC 0.445 405 WB Sequence A0211 84 ALSPVPPV 0.874 3 SB Sequence A0212 173 ALWMTEYL 0.860 4 SB Sequence A0212 218 TLLSLALV 0.857 4 SB Sequence A0212 207 PLFDFSWL 0.836 5 SB Sequence A0212 167 PLVDNIAL 0.787 9 SB Sequence A0212 215 SLKTLLSL 0.756 13 SB Sequence A0212 179 YLNRHLHT 0.720 20 SB Sequence A0212 113 EMSSQLHL 0.594 80 WB Sequence A0212 213 WLSLKTLL 0.564 112 WB Sequence A0212 27 YEWDAGDV 0.477 288 WB Sequence A0212 154 GVMCVESV 0.460 344 WB Sequence A0212 84 ALSPVPPV 0.926 2 SB Sequence A0216 173 ALWMTEYL 0.916 2 SB Sequence A0216 218 TLLSLALV 0.902 2 SB Sequence A0216 207 PLFDFSWL 0.889 3 SB Sequence A0216 167 PLVDNIAL 0.767 12 SB Sequence A0216 215 SLKTLLSL 0.723 20 SB Sequence A0216 213 WLSLKTLL 0.718 21 SB Sequence A0216 113 EMSSQLHL 0.665 37 SB Sequence A0216 154 GVMCVESV 0.646 46 SB Sequence A0216 179 YLNRHLHT 0.631 53 WB Sequence A0216 223 ALVGACIT 0.591 83 WB Sequence A0216 224 LVGACITL 0.531 159 WB Sequence A0216 87 PVPPVVHL 0.526 168 WB Sequence A0216 151 EFGGVMCV 0.524 173 WB Sequence A0216 228 CITLGAYL 0.522 176 WB Sequence A0216 140 GVNWGRIV 0.470 308 WB Sequence A0216 84 ALSPVPPV 0.898 3 SB Sequence A0219 173 ALWMTEYL 0.871 4 SB Sequence A0219 218 TLLSLALV 0.847 5 SB Sequence A0219 207 PLFDFSWL 0.785 10 SB Sequence A0219 167 PLVDNIAL 0.713 22 SB Sequence A0219 113 EMSSQLHL 0.613 65 WB Sequence A0219 213 WLSLKTLL 0.599 76 WB Sequence A0219 154 GVMCVESV 0.468 317 WB Sequence A0219 215 SLKTLLSL 0.466 322 WB Sequence A0219 27 YEWDAGDV 0.437 440 WB Sequence A0219 179 YLNRHLHT 0.436 447 WB Sequence A0219 14 VMKYIHYK 0.629 55 WB Sequence A0301 13 IVMKYIHY 0.514 193 WB Sequence A0301 119 HLTPFTAR 0.467 319 WB Sequence A0301 199 ELYGPSMR 0.456 360 WB Sequence A0301 14 VMKYIHYK 0.645 46 SB Sequence A1101 131 TVVEELFR 0.616 63 WB Sequence A1101 13 IVMKYIHY 0.577 97 WB Sequence A1101 142 NWGRIVAF 0.600 75 WB Sequence A2301 145 RIVAFFEF 0.518 184 WB Sequence A2301 204 SMRPLFDF 0.469 312 WB Sequence A2301 122 PFTARGRF 0.441 424 WB Sequence A2301 142 NWGRIVAF 0.617 62 WB Sequence A2402 212 SWLSLKTL 0.459 349 WB Sequence A2402 204 SMRPLFDF 0.547 135 WB Sequence A2403 145 RIVAFFEF 0.437 441 WB Sequence A2403 13 IVMKYIHY 0.638 50 WB Sequence A2602 113 EMSSQLHL 0.445 406 WB Sequence A2602 145 RIVAFFEF 0.436 445 WB Sequence A2602 12 EIVMKYIH 0.430 478 WB Sequence A2602 130 ATVVEELF 0.428 489 WB Sequence A2602 13 IVMKYIHY 0.603 73 WB Sequence A2902 227 ACITLGAY 0.449 387 WB Sequence A2902 14 VMKYIHYK 0.593 81 WB Sequence A3001 60 ASRDPVAR 0.498 229 WB Sequence A3001 126 RGRFATVV 0.480 276 WB Sequence A3001 113 EMSSQLHL 0.446 401 WB Sequence A3002 204 SMRPLFDF 0.444 410 WB Sequence A3002 14 VMKYIHYK 0.842 5 SB Sequence A3101 119 HLTPFTAR 0.709 23 SB Sequence A3101 60 ASRDPVAR 0.692 28 SB Sequence A3101 102 DFSRRYRR 0.622 59 WB Sequence A3101 175 WMTEYLNR 0.564 112 WB Sequence A3101 131 TVVEELFR 0.458 351 WB Sequence A3101 102 DFSRRYRR 0.883 3 SB Sequence A3301 119 HLTPFTAR 0.746 15 SB Sequence A3301 210 DFSWLSLK 0.672 34 SB Sequence A3301 101 DDFSRRYR 0.622 60 WB Sequence A3301 199 ELYGPSMR 0.615 64 WB Sequence A3301 131 TVVEELFR 0.546 136 WB Sequence A3301 14 VMKYIHYK 0.510 199 WB Sequence A3301 131 TVVEELFR 0.843 5 SB Sequence A6801 199 ELYGPSMR 0.792 9 SB Sequence A6801 119 HLTPFTAR 0.733 18 SB Sequence A6801 210 DFSWLSLK 0.637 50 WB Sequence A6801 121 TPFTARGR 0.625 58 WB Sequence A6801 55 TPHPAASR 0.581 93 WB Sequence A6801 101 DDFSRRYR 0.526 168 WB Sequence A6801 14 VMKYIHYK 0.524 171 WB Sequence A6801 98 QAGDDFSR 0.522 176 WB Sequence A6801 175 WMTEYLNR 0.505 211 WB Sequence A6801 156 MCVESVNR 0.502 219 WB Sequence A6801 102 DFSRRYRR 0.491 247 WB Sequence A6801 90 PVVHLTLR 0.456 358 WB Sequence A6801 154 GVMCVESV 0.630 54 WB Sequence A6802 165 MSPLVDNI 0.606 70 WB Sequence A6802 123 FTARGRFA 0.594 80 WB Sequence A6802 129 FATVVEEL 0.501 220 WB Sequence A6802 72 QTPAAPGA 0.474 297 WB Sequence A6802 218 TLLSLALV 0.607 70 WB Sequence A6901 123 FTARGRFA 0.486 261 WB Sequence A6901 113 EMSSQLHL 0.470 309 WB Sequence A6901 84 ALSPVPPV 0.444 409 WB Sequence A6901 202 GPSMRPLF 0.599 76 WB Sequence B0702 73 TPAAPGAA 0.598 77 WB Sequence B0702 69 SPLQTPAA 0.539 146 WB Sequence B0702 89 PPVVHLTL 0.503 216 WB Sequence B0702 206 RPLFDFSW 0.445 403 WB Sequence B0702 116 SQLHLTPF 0.583 91 WB Sequence B1501 204 SMRPLFDF 0.523 173 WB Sequence B1501 13 IVMKYIHY 0.492 243 WB Sequence B1501 145 RIVAFFEF 0.447 397 WB Sequence B1501 198 VELYGPSM 0.595 80 WB Sequence B1801 177 TEYLNRHL 0.498 228 WB Sequence B1801 172 IALWMTEY 0.475 292 WB Sequence B1801 116 SQLHLTPF 0.464 328 WB Sequence B1801 150 FEFGGVMC 0.452 375 WB Sequence B1801 172 IALWMTEY 0.767 12 SB Sequence B3501 149 FFEFGGVM 0.548 132 WB Sequence B3501 69 SPLQTPAA 0.503 215 WB Sequence B3501 111 FAEMSSQL 0.488 253 WB Sequence B3501 86 SPVPPVVH 0.443 413 WB Sequence B3501 73 TPAAPGAA 0.435 452 WB Sequence B3501 129 FATVVEEL 0.430 475 WB Sequence B3501 177 TEYLNRHL 0.547 133 WB Sequence B4001 11 REIVMKYI 0.513 194 WB Sequence B4001 150 FEFGGVMC 0.466 324 WB Sequence B4001 11 REIVMKYI 0.497 231 WB Sequence B4002 112 AEMSSQLH 0.471 305 WB Sequence B4501 134 EELFRDGV 0.465 326 WB Sequence B4501 11 REIVMKYI 0.435 450 WB Sequence B4501 222 LALVGACI 0.470 308 WB Sequence B5101 89 PPVVHLTL 0.448 391 WB Sequence B5101 206 RPLFDFSW 0.768 12 SB Sequence B5301 202 GPSMRPLF 0.430 474 WB Sequence B5301 73 TPAAPGAA 0.677 32 SB Sequence B5401 69 SPLQTPAA 0.605 71 WB Sequence B5401 37 APPGAAPA 0.557 120 WB Sequence B5401 166 SPLVDNIA 0.470 309 WB Sequence B5401 88 VPPVVHLT 0.450 382 WB Sequence B5401 22 LSQRGYEW 0.648 45 SB Sequence B5801 145 RIVAFFEF 0.512 196 WB Sequence B5801 168 LVDNIALW 0.475 292 WB Sequence B5801 172 IALWMTEY 0.460 345 WB Sequence B5801 9-mer 171 NIALWMTEY 0.497 230 WB Sequence A0101 84 ALSPVPPVV 0.676 33 SB Sequence A0201 223 ALVGACITL 0.631 54 WB Sequence A0201 217 KTLLSLALV 0.613 65 WB Sequence A0201 219 LLSLALVGA 0.542 141 WB Sequence A0201 172 IALWMTEYL 0.487 258 WB Sequence A0201 219 LLSLALVGA 0.824 6 SB Sequence A0202 14 VMKYIHYKL 0.705 24 SB Sequence A0202 223 ALVGACITL 0.654 42 SB Sequence A0202 215 SLKTLLSLA 0.635 52 WB Sequence A0202 160 SVNREMSPL 0.619 61 WB Sequence A0202 80 AAGPALSPV 0.617 62 WB Sequence A0202 84 ALSPVPPVV 0.593 81 WB Sequence A0202 164 EMSPLVDNI 0.582 91 WB Sequence A0202 221 SLALVGACI 0.579 94 WB Sequence A0202 67 RTSPLQTPA 0.554 124 WB Sequence A0202 204 SMRPLFDFS 0.495 234 WB Sequence A0202 179 YLNRHLHTW 0.479 280 WB Sequence A0202 172 IALWMTEYL 0.459 346 WB Sequence A0202 217 KTLLSLALV 0.443 414 WB Sequence A0202 113 EMSSQLHLT 0.432 464 WB Sequence A0202 215 SLKTLLSLA 0.875 3 SB Sequence A0203 84 ALSPVPPVV 0.842 5 SB Sequence A0203 219 LLSLALVGA 0.839 5 SB Sequence A0203 80 AAGPALSPV 0.770 11 SB Sequence A0203 160 SVNREMSPL 0.699 26 SB Sequence A0203 124 TARGRFATV 0.666 37 SB Sequence A0203 14 VMKYIHYKL 0.642 48 SB Sequence A0203 223 ALVGACITL 0.629 55 WB Sequence A0203 221 SLALVGACI 0.605 71 WB Sequence A0203 217 KTLLSLALV 0.584 90 WB Sequence A0203 67 RTSPLQTPA 0.539 146 WB Sequence A0203 147 VAFFEFGGV 0.520 180 WB Sequence A0203 164 EMSPLVDNI 0.516 187 WB Sequence A0203 117 QLHLTPFTA 0.490 249 WB Sequence A0203 204 SMRPLFDFS 0.441 425 WB Sequence A0203 179 YLNRHLHTW 0.432 468 WB Sequence A0203 84 ALSPVPPVV 0.766 12 SB Sequence A0204 223 ALVGACITL 0.571 103 WB Sequence A0204 80 AAGPALSPV 0.454 366 WB Sequence A0204 217 KTLLSLALV 0.742 16 SB Sequence A0206 80 AAGPALSPV 0.729 18 SB Sequence A0206 116 SQLHLTPFT 0.684 30 SB Sequence A0206 71 LQTPAAPGA 0.676 33 SB Sequence A0206 150 FEFGGVMCV 0.650 44 SB Sequence A0206 223 ALVGACITL 0.635 52 WB Sequence A0206 219 LLSLALVGA 0.624 58 WB Sequence A0206 84 ALSPVPPVV 0.621 60 WB Sequence A0206 123 FTARGRFAT 0.598 77 WB Sequence A0206 188 IQDNGGWDA 0.594 80 WB Sequence A0206 172 IALWMTEYL 0.589 85 WB Sequence A0206 36 AAPPGAAPA 0.569 106 WB Sequence A0206 124 TARGRFATV 0.543 140 WB Sequence A0206 147 VAFFEFGGV 0.511 198 WB Sequence A0206 67 RTSPLQTPA 0.462 336 WB Sequence A0206 84 ALSPVPPVV 0.951 1 SB Sequence A0211 223 ALVGACITL 0.929 2 SB Sequence A0211 207 PLFDFSWLS 0.902 2 SB Sequence A0211 150 FEFGGVMCV 0.812 7 SB Sequence A0211 179 YLNRHLHTW 0.742 16 SB Sequence A0211 221 SLALVGACI 0.715 21 SB Sequence A0211 219 LLSLALVGA 0.627 56 WB Sequence A0211 164 EMSPLVDNI 0.626 57 WB Sequence A0211 117 QLHLTPFTA 0.626 57 WB Sequence A0211 215 SLKTLLSLA 0.620 61 WB Sequence A0211 168 LVDNIALWM 0.592 82 WB Sequence A0211 217 KTLLSLALV 0.581 93 WB Sequence A0211 140 GVNWGRIVA 0.575 99 WB Sequence A0211 14 VMKYIHYKL 0.561 115 WB Sequence A0211 80 AAGPALSPV 0.551 128 WB Sequence A0211 113 EMSSQLHLT 0.531 159 WB Sequence A0211 6 TGYDNREIV 0.513 194 WB Sequence A0211 119 HLTPFTARG 0.505 211 WB Sequence A0211 199 ELYGPSMRP 0.504 213 WB Sequence A0211 192 GGWDAFVEL 0.503 216 WB Sequence A0211 172 IALWMTEYL 0.462 337 WB Sequence A0211 173 ALWMTEYLN 0.459 347 WB Sequence A0211 36 AAPPGAAPA 0.432 467 WB Sequence A0211 84 ALSPVPPVV 0.914 2 SB Sequence A0212 223 ALVGACITL 0.760 13 SB Sequence A0212 179 YLNRHLHTW 0.739 16 SB Sequence A0212 150 FEFGGVMCV 0.735 17 SB Sequence A0212 207 PLFDFSWLS 0.676 33 SB Sequence A0212 14 VMKYIHYKL 0.596 79 WB Sequence A0212 219 LLSLALVGA 0.587 87 WB Sequence A0212 221 SLALVGACI 0.529 162 WB Sequence A0212 164 EMSPLVDNI 0.520 180 WB Sequence A0212 117 QLHLTPFTA 0.476 290 WB Sequence A0212 123 FTARGRFAT 0.464 328 WB Sequence A0212 84 ALSPVPPVV 0.915 2 SB Sequence A0216 223 ALVGACITL 0.909 2 SB Sequence A0216 80 AAGPALSPV 0.699 25 SB Sequence A0216 150 FEFGGVMCV 0.640 49 SB Sequence A0216 221 SLALVGACI 0.630 54 WB Sequence A0216 14 VMKYIHYKL 0.570 104 WB Sequence A0216 207 PLFDFSWLS 0.530 162 WB Sequence A0216 117 QLHLTPFTA 0.490 250 WB Sequence A0216 215 SLKTLLSLA 0.489 251 WB Sequence A0216 179 YLNRHLHTW 0.461 340 WB Sequence A0216 124 TARGRFATV 0.448 393 WB Sequence A0216 84 ALSPVPPVV 0.899 2 SB Sequence A0219 150 FEFGGVMCV 0.686 29 SB Sequence A0219 223 ALVGACITL 0.683 30 SB Sequence A0219 80 AAGPALSPV 0.557 120 WB Sequence A0219 219 LLSLALVGA 0.542 142 WB Sequence A0219 83 PALSPVPPV 0.498 229 WB Sequence A0219 164 EMSPLVDNI 0.460 345 WB Sequence A0219 113 EMSSQLHLT 0.437 443 WB Sequence A0219 179 YLNRHLHTW 0.428 485 WB Sequence A0219 13 IVMKYIHYK 0.758 13 SB Sequence A0301 230 TLGAYLGHK 0.655 41 SB Sequence A0301 209 FDFSWLSLK 0.457 357 WB Sequence A0301 13 IVMKYIHYK 0.834 6 SB Sequence A1101 230 TLGAYLGHK 0.708 23 SB Sequence A1101 130 ATVVEELFR 0.574 100 WB Sequence A1101 142 NWGRIVAFF 0.644 47 SB Sequence A2301 203 PSMRPLFDF 0.530 161 WB Sequence A2301 144 GRIVAFFEF 0.530 162 WB Sequence A2301 13 IVMKYIHYK 0.499 226 WB Sequence A2301 106 RYRRDFAEM 0.467 321 WB Sequence A2301 128 RFATVVEEL 0.454 366 WB Sequence A2301 142 NWGRIVAFF 0.739 16 SB Sequence A2402 128 RFATVVEEL 0.568 107 WB Sequence A2402 212 SWLSLKTLL 0.536 151 WB Sequence A2402 106 RYRRDFAEM 0.669 35 SB Sequence A2403 128 RFATVVEEL 0.626 57 WB Sequence A2403 200 LYGPSMRPL 0.553 125 WB Sequence A2403 12 EIVMKYIHY 0.628 55 WB Sequence A2601 171 NIALWMTEY 0.622 60 WB Sequence A2601 12 EIVMKYIHY 0.935 2 SB Sequence A2602 171 NIALWMTEY 0.866 4 SB Sequence A2602 160 SVNREMSPL 0.849 5 SB Sequence A2602 179 YLNRHLHTW 0.538 148 WB Sequence A2602 197 FVELYGPSM 0.520 180 WB Sequence A2602 168 LVDNIALWM 0.432 464 WB Sequence A2602 171 NIALWMTEY 0.586 88 WB Sequence A2902 12 EIVMKYIHY 0.516 188 WB Sequence A2902 13 IVMKYIHYK 0.758 13 SB Sequence A3001 0 MAHAGRTGY 0.487 258 WB Sequence A3001 230 TLGAYLGHK 0.475 293 WB Sequence A3001 171 NIALWMTEY 0.427 491 WB Sequence A3002 13 IVMKYIHYK 0.797 8 SB Sequence A3101 17 YIHYKLSQR 0.715 21 SB Sequence A3101 155 VMCVESVNR 0.631 54 WB Sequence A3101 97 RQAGDDFSR 0.588 85 WB Sequence A3101 14 VMKYIHYKL 0.497 230 WB Sequence A3101 130 ATVVEELFR 0.471 307 WB Sequence A3101 101 DDFSRRYRR 0.698 26 SB Sequence A3301 17 YIHYKLSQR 0.649 44 SB Sequence A3301 54 HTPHPAASR 0.476 290 WB Sequence A3301 13 IVMKYIHYK 0.427 493 WB Sequence A3301 13 IVMKYIHYK 0.790 9 SB Sequence A6801 17 YIHYKLSQR 0.747 15 SB Sequence A6801 54 HTPHPAASR 0.729 18 SB Sequence A6801 120 LTPFTARGR 0.703 24 SB Sequence A6801 130 ATVVEELFR 0.655 41 SB Sequence A6801 101 DDFSRRYRR 0.571 103 WB Sequence A6801 209 FDFSWLSLK 0.540 145 WB Sequence A6801 98 QAGDDFSRR 0.529 163 WB Sequence A6801 171 NIALWMTEY 0.477 288 WB Sequence A6801 230 TLGAYLGHK 0.449 388 WB Sequence A6801 0 MAHAGRTGY 0.447 398 WB Sequence A6801 123 FTARGRFAT 0.692 27 SB Sequence A6802 147 VAFFEFGGV 0.641 48 SB Sequence A6802 57 HPAASRDPV 0.627 56 WB Sequence A6802 72 QTPAAPGAA 0.604 72 WB Sequence A6802 160 SVNREMSPL 0.570 104 WB Sequence A6802 124 TARGRFATV 0.531 160 WB Sequence A6802 6 TGYDNREIV 0.513 193 WB Sequence A6802 164 EMSPLVDNI 0.512 196 WB Sequence A6802 67 RTSPLQTPA 0.488 254 WB Sequence A6802 225 VGACITLGA 0.472 303 WB Sequence A6802 165 MSPLVDNIA 0.466 322 WB Sequence A6802 150 FEFGGVMCV 0.449 388 WB Sequence A6802 83 PALSPVPPV 0.726 19 SB Sequence A6901 33 DVGAAPPGA 0.535 152 WB Sequence A6901 57 HPAASRDPV 0.495 235 WB Sequence A6901 164 EMSPLVDNI 0.485 262 WB Sequence A6901 123 FTARGRFAT 0.483 267 WB Sequence A6901 217 KTLLSLALV 0.460 344 WB Sequence A6901 73 TPAAPGAAA 0.460 344 WB Sequence A6901 172 IALWMTEYL 0.426 497 WB Sequence A6901 57 HPAASRDPV 0.770 12 SB Sequence B0702 63 DPVARTSPL 0.750 14 SB Sequence B0702 166 SPLVDNIAL 0.674 33 SB Sequence B0702 73 TPAAPGAAA 0.652 43 SB Sequence B0702 206 RPLFDFSWL 0.627 56 WB Sequence B0702 86 SPVPPVVHL 0.606 71 WB Sequence B0702 76 APGAAAGPA 0.573 101 WB Sequence B0702 88 VPPVVHLTL 0.542 142 WB Sequence B0702 121 TPFTARGRF 0.505 210 WB Sequence B0702 124 TARGRFATV 0.449 389 WB Sequence B0702 0 MAHAGRTGY 0.532 158 WB Sequence B1501 115 SSQLHLTPF 0.427 490 WB Sequence B1501 150 FEFGGVMCV 0.633 53 WB Sequence B1801 9 DNREIVMKY 0.541 143 WB Sequence B1801 172 IALWMTEYL 0.505 211 WB Sequence B1801 144 GRIVAFFEF 0.456 360 WB Sequence B2705 105 RRYRRDFAE 0.456 361 WB Sequence B2705 166 SPLVDNIAL 0.680 31 SB Sequence B3501 0 MAHAGRTGY 0.658 40 SB Sequence B3501 197 FVELYGPSM 0.628 55 WB Sequence B3501 121 TPFTARGRF 0.610 67 WB Sequence B3501 172 IALWMTEYL 0.584 90 WB Sequence B3501 63 DPVARTSPL 0.584 90 WB Sequence B3501 129 FATVVEELF 0.562 113 WB Sequence B3501 73 TPAAPGAAA 0.551 128 WB Sequence B3501 171 NIALWMTEY 0.523 174 WB Sequence B3501 111 FAEMSSQLH 0.460 343 WB Sequence B3501 112 AEMSSQLHL 0.740 16 SB Sequence B4001 150 FEFGGVMCV 0.588 86 WB Sequence B4001 112 AEMSSQLHL 0.554 124 WB Sequence B4002 150 FEFGGVMCV 0.466 323 WB Sequence B4002 112 AEMSSQLHL 0.454 368 WB Sequence B4402 112 AEMSSQLHL 0.533 157 WB Sequence B4403 112 AEMSSQLHL 0.587 87 WB Sequence B4501 88 VPPVVHLTL 0.548 132 WB Sequence B5101 206 RPLFDFSWL 0.470 307 WB Sequence B5301 166 SPLVDNIAL 0.459 348 WB Sequence B5301 172 IALWMTEYL 0.450 382 WB Sequence B5301 73 TPAAPGAAA 0.715 21 SB Sequence B5401 57 HPAASRDPV 0.684 30 SB Sequence B5401 76 APGAAAGPA 0.625 57 WB Sequence B5401 51 QPGHTPHPA 0.515 189 WB Sequence B5401 179 YLNRHLHTW 0.682 31 SB Sequence B5801 21 KLSQRGYEW 0.649 44 SB Sequence B5801 129 FATVVEELF 0.547 134 WB Sequence B5801 40 GAAPAPGIF 0.483 268 WB Sequence B5801 10-mer 179 YLNRHLHTWI 0.735 17 SB Sequence A0201 13 IVMKYIHYKL 0.638 50 WB Sequence A0201 218 TLLSLALVGA 0.571 103 WB Sequence A0201 207 PLFDFSWLSL 0.536 151 WB Sequence A0201 213 WLSLKTLLSL 0.530 161 WB Sequence A0201 123 FTARGRFATV 0.522 175 WB Sequence A0201 171 NIALWMTEYL 0.521 178 WB Sequence A0201 175 WMTEYLNRHL 0.486 260 WB Sequence A0201 218 TLLSLALVGA 0.731 18 SB Sequence A0202 171 NIALWMTEYL 0.727 19 SB Sequence A0202 213 WLSLKTLLSL 0.700 25 SB Sequence A0202 215 SLKTLLSLAL 0.646 46 SB Sequence A0202 175 WMTEYLNRHL 0.642 47 SB Sequence A0202 207 PLFDFSWLSL 0.637 50 WB Sequence A0202 79 AAAGPALSPV 0.588 86 WB Sequence A0202 13 IVMKYIHYKL 0.569 106 WB Sequence A0202 123 FTARGRFATV 0.568 106 WB Sequence A0202 199 ELYGPSMRPL 0.541 143 WB Sequence A0202 179 YLNRHLHTWI 0.540 145 WB Sequence A0202 224 LVGACITLGA 0.483 267 WB Sequence A0202 146 IVAFFEFGGV 0.439 431 WB Sequence A0202 179 YLNRHLHTWI 0.933 2 SB Sequence A0203 123 FTARGRFATV 0.821 6 SB Sequence A0203 213 WLSLKTLLSL 0.782 10 SB Sequence A0203 215 SLKTLLSLAL 0.773 11 SB Sequence A0203 171 NIALWMTEYL 0.682 31 SB Sequence A0203 160 SVNREMSPLV 0.680 31 SB Sequence A0203 146 IVAFFEFGGV 0.667 36 SB Sequence A0203 79 AAAGPALSPV 0.606 71 WB Sequence A0203 175 WMTEYLNRHL 0.569 106 WB Sequence A0203 218 TLLSLALVGA 0.545 137 WB Sequence A0203 13 IVMKYIHYKL 0.532 157 WB Sequence A0203 224 LVGACITLGA 0.532 158 WB Sequence A0203 199 ELYGPSMRPL 0.519 182 WB Sequence A0203 50 SQPGHTPHPA 0.447 398 WB Sequence A0203 219 LLSLALVGAC 0.444 410 WB Sequence A0203 124 TARGRFATVV 0.428 489 WB Sequence A0203 179 YLNRHLHTWI 0.655 41 SB Sequence A0204 123 FTARGRFATV 0.613 66 WB Sequence A0204 13 IVMKYIHYKL 0.509 203 WB Sequence A0204 79 AAAGPALSPV 0.474 296 WB Sequence A0204 160 SVNREMSPLV 0.450 384 WB Sequence A0204 123 FTARGRFATV 0.867 4 SB Sequence A0206 116 SQLHLTPFTA 0.776 11 SB Sequence A0206 188 IQDNGGWDAF 0.673 34 SB Sequence A0206 213 WLSLKTLLSL 0.667 36 SB Sequence A0206 50 SQPGHTPHPA 0.621 60 WB Sequence A0206 179 YLNRHLHTWI 0.619 61 WB Sequence A0206 79 AAAGPALSPV 0.602 74 WB Sequence A0206 175 WMTEYLNRHL 0.600 75 WB Sequence A0206 160 SVNREMSPLV 0.567 108 WB Sequence A0206 171 NIALWMTEYL 0.562 114 WB Sequence A0206 218 TLLSLALVGA 0.560 116 WB Sequence A0206 146 IVAFFEFGGV 0.553 125 WB Sequence A0206 71 LQTPAAPGAA 0.546 135 WB Sequence A0206 13 IVMKYIHYKL 0.525 171 WB Sequence A0206 27 YEWDAGDVGA 0.511 199 WB Sequence A0206 207 PLFDFSWLSL 0.486 260 WB Sequence A0206 67 RTSPLQTPAA 0.477 286 WB Sequence A0206 224 LVGACITLGA 0.471 304 WB Sequence A0206 207 PLFDFSWLSL 0.935 2 SB Sequence A0211 179 YLNRHLHTWI 0.925 2 SB Sequence A0211 199 ELYGPSMRPL 0.888 3 SB Sequence A0211 213 WLSLKTLLSL 0.835 5 SB Sequence A0211 218 TLLSLALVGA 0.829 6 SB Sequence A0211 123 FTARGRFATV 0.823 6 SB Sequence A0211 167 PLVDNIALWM 0.802 8 SB Sequence A0211 215 SLKTLLSLAL 0.799 8 SB Sequence A0211 175 WMTEYLNRHL 0.796 9 SB Sequence A0211 160 SVNREMSPLV 0.788 9 SB Sequence A0211 87 PVPPVVHLTL 0.705 24 SB Sequence A0211 79 AAAGPALSPV 0.635 51 WB Sequence A0211 13 IVMKYIHYKL 0.601 74 WB Sequence A0211 146 IVAFFEFGGV 0.568 107 WB Sequence A0211 132 VVEELFRDGV 0.549 131 WB Sequence A0211 171 NIALWMTEYL 0.547 133 WB Sequence A0211 164 EMSPLVDNIA 0.488 254 WB Sequence A0211 168 LVDNIALWMT 0.484 266 WB Sequence A0211 149 FFEFGGVMCV 0.475 292 WB Sequence A0211 221 SLALVGACIT 0.462 336 WB Sequence A0211 187 WIQDNGGWDA 0.453 370 WB Sequence A0211 179 YLNRHLHTWI 0.878 3 SB Sequence A0212 207 PLFDFSWLSL 0.859 4 SB Sequence A0212 123 FTARGRFATV 0.849 5 SB Sequence A0212 215 SLKTLLSLAL 0.730 18 SB Sequence A0212 199 ELYGPSMRPL 0.726 19 SB Sequence A0212 175 WMTEYLNRHL 0.716 21 SB Sequence A0212 213 WLSLKTLLSL 0.697 26 SB Sequence A0212 218 TLLSLALVGA 0.692 27 SB Sequence A0212 132 VVEELFRDGV 0.601 74 WB Sequence A0212 167 PLVDNIALWM 0.560 116 WB Sequence A0212 13 IVMKYIHYKL 0.533 156 WB Sequence A0212 160 SVNREMSPLV 0.509 202 WB Sequence A0212 187 WIQDNGGWDA 0.479 280 WB Sequence A0212 146 IVAFFEFGGV 0.476 288 WB Sequence A0212 87 PVPPVVHLTL 0.475 294 WB Sequence A0212 27 YEWDAGDVGA 0.467 321 WB Sequence A0212 179 YLNRHLHTWI 0.854 4 SB Sequence A0216 207 PLFDFSWLSL 0.849 5 SB Sequence A0216 123 FTARGRFATV 0.812 7 SB Sequence A0216 199 ELYGPSMRPL 0.767 12 SB Sequence A0216 213 WLSLKTLLSL 0.745 15 SB Sequence A0216 167 PLVDNIALWM 0.702 25 SB Sequence A0216 160 SVNREMSPLV 0.685 30 SB Sequence A0216 13 IVMKYIHYKL 0.676 33 SB Sequence A0216 175 WMTEYLNRHL 0.675 33 SB Sequence A0216 79 AAAGPALSPV 0.661 39 SB Sequence A0216 87 PVPPVVHLTL 0.638 50 WB Sequence A0216 215 SLKTLLSLAL 0.634 52 WB Sequence A0216 218 TLLSLALVGA 0.574 100 WB Sequence A0216 171 NIALWMTEYL 0.557 120 WB Sequence A0216 221 SLALVGACIT 0.472 301 WB Sequence A0216 146 IVAFFEFGGV 0.429 483 WB Sequence A0216 207 PLFDFSWLSL 0.805 8 SB Sequence A0219 179 YLNRHLHTWI 0.789 9 SB Sequence A0219 213 WLSLKTLLSL 0.766 12 SB Sequence A0219 123 FTARGRFATV 0.703 24 SB Sequence A0219 199 ELYGPSMRPL 0.585 88 WB Sequence A0219 167 PLVDNIALWM 0.574 100 WB Sequence A0219 79 AAAGPALSPV 0.563 112 WB Sequence A0219 218 TLLSLALVGA 0.551 129 WB Sequence A0219 175 WMTEYLNRHL 0.521 178 WB Sequence A0219 83 PALSPVPPVV 0.486 259 WB Sequence A0219 13 IVMKYIHYKL 0.461 341 WB Sequence A0219 171 NIALWMTEYL 0.446 401 WB Sequence A0219 229 ITLGAYLGHK 0.760 13 SB Sequence A0301 208 LFDFSWLSLK 0.497 232 WB Sequence A0301 12 EIVMKYIHYK 0.475 292 WB Sequence A0301 154 GVMCVESVNR 0.444 411 WB Sequence A0301 173 ALWMTEYLNR 0.429 480 WB Sequence A0301 229 ITLGAYLGHK 0.752 14 SB Sequence A1101 154 GVMCVESVNR 0.637 50 WB Sequence A1101 12 EIVMKYIHYK 0.540 145 WB Sequence A1101 173 ALWMTEYLNR 0.455 363 WB Sequence A1101 208 LFDFSWLSLK 0.435 453 WB Sequence A1101 178 EYLNRHLHTW 0.686 29 SB Sequence A2301 200 LYGPSMRPLF 0.686 29 SB Sequence A2301 128 RFATVVEELF 0.620 60 WB Sequence A2301 7 GYDNREIVMK 0.595 80 WB Sequence A2301 102 DFSRRYRRDF 0.499 226 WB Sequence A2301 13 IVMKYIHYKL 0.451 381 WB Sequence A2301 94 LTLRQAGDDF 0.437 441 WB Sequence A2301 128 RFATVVEELF 0.764 12 SB Sequence A2402 200 LYGPSMRPLF 0.733 17 SB Sequence A2402 178 EYLNRHLHTW 0.715 21 SB Sequence A2402 178 EYLNRHLHTW 0.718 21 SB Sequence A2403 128 RFATVVEELF 0.657 41 SB Sequence A2403 200 LYGPSMRPLF 0.636 51 WB Sequence A2403 170 DNIALWMTEY 0.478 283 WB Sequence A2601 159 ESVNREMSPL 0.621 60 WB Sequence A2602 199 ELYGPSMRPL 0.595 79 WB Sequence A2602 171 NIALWMTEYL 0.549 131 WB Sequence A2602 170 DNIALWMTEY 0.487 258 WB Sequence A2602 229 ITLGAYLGHK 0.718 21 SB Sequence A3001 16 KYIHYKLSQR 0.837 5 SB Sequence A3101 136 LFRDGVNWGR 0.667 36 SB Sequence A3101 154 GVMCVESVNR 0.576 98 WB Sequence A3101 119 HLTPFTARGR 0.573 101 WB Sequence A3101 173 ALWMTEYLNR 0.509 203 WB Sequence A3101 99 AGDDFSRRYR 0.507 207 WB Sequence A3101 129 FATVVEELFR 0.493 241 WB Sequence A3101 117 QLHLTPFTAR 0.431 471 WB Sequence A3101 136 LFRDGVNWGR 0.553 126 WB Sequence A3301 16 KYIHYKLSQR 0.520 180 WB Sequence A3301 129 FATVVEELFR 0.516 188 WB Sequence A3301 173 ALWMTEYLNR 0.441 423 WB Sequence A3301 129 FATVVEELFR 0.829 6 SB Sequence A6801 12 EIVMKYIHYK 0.780 10 SB Sequence A6801 119 HLTPFTARGR 0.721 20 SB Sequence A6801 197 FVELYGPSMR 0.688 29 SB Sequence A6801 154 GVMCVESVNR 0.646 46 SB Sequence A6801 229 ITLGAYLGHK 0.568 106 WB Sequence A6801 176 MTEYLNRHLH 0.485 262 WB Sequence A6801 117 QLHLTPFTAR 0.466 322 WB Sequence A6801 2 HAGRTGYDNR 0.446 399 WB Sequence A6801 123 FTARGRFATV 0.861 4 SB Sequence A6802 146 IVAFFEFGGV 0.809 7 SB Sequence A6802 171 NIALWMTEYL 0.728 18 SB Sequence A6802 13 IVMKYIHYKL 0.680 31 SB Sequence A6802 79 AAAGPALSPV 0.644 47 SB Sequence A6802 72 QTPAAPGAAA 0.617 63 WB Sequence A6802 165 MSPLVDNIAL 0.591 83 WB Sequence A6802 199 ELYGPSMRPL 0.582 92 WB Sequence A6802 159 ESVNREMSPL 0.550 129 WB Sequence A6802 205 MRPLFDFSWL 0.522 175 WB Sequence A6802 160 SVNREMSPLV 0.471 306 WB Sequence A6802 124 TARGRFATVV 0.441 421 WB Sequence A6802 123 FTARGRFATV 0.792 9 SB Sequence A6901 199 ELYGPSMRPL 0.714 22 SB Sequence A6901 83 PALSPVPPVV 0.580 94 WB Sequence A6901 171 NIALWMTEYL 0.558 119 WB Sequence A6901 160 SVNREMSPLV 0.537 149 WB Sequence A6901 79 AAAGPALSPV 0.502 219 WB Sequence A6901 33 DVGAAPPGAA 0.489 251 WB Sequence A6901 146 IVAFFEFGGV 0.464 330 WB Sequence A6901 13 IVMKYIHYKL 0.441 422 WB Sequence A6901 76 APGAAAGPAL 0.708 23 SB Sequence B0702 82 GPALSPVPPV 0.604 72 WB Sequence B0702 57 HPAASRDPVA 0.536 152 WB Sequence B0702 202 GPSMRPLFDF 0.468 317 WB Sequence B0702 124 TARGRFATVV 0.465 327 WB Sequence B0702 42 APAPGIFSSQ 0.451 378 WB Sequence B0702 140 GVNWGRIVAF 0.548 132 WB Sequence B1501 114 MSSQLHLTPF 0.504 214 WB Sequence B1501 188 IQDNGGWDAF 0.490 249 WB Sequence B1501 11 REIVMKYIHY 0.603 73 WB Sequence B1801 105 RRYRRDFAEM 0.622 59 WB Sequence B2705 127 GRFATVVEEL 0.493 241 WB Sequence B2705 114 MSSQLHLTPF 0.582 91 WB Sequence B3501 147 VAFFEFGGVM 0.561 115 WB Sequence B3501 76 APGAAAGPAL 0.526 168 WB Sequence B3501 222 LALVGACITL 0.473 297 WB Sequence B3501 156 MCVESVNREM 0.473 299 WB Sequence B3501 98 QAGDDFSRRY 0.461 340 WB Sequence B3501 73 TPAAPGAAAG 0.459 346 WB Sequence B3501 140 GVNWGRIVAF 0.455 362 WB Sequence B3501 166 SPLVDNIALW 0.453 371 WB Sequence B3501 11 REIVMKYIHY 0.502 218 WB Sequence B4002 112 AEMSSQLHLT 0.472 303 WB Sequence B4002 11 REIVMKYIHY 0.476 289 WB Sequence B4402 11 REIVMKYIHY 0.481 273 WB Sequence B4403 134 EELFRDGVNW 0.473 300 WB Sequence B4403 112 AEMSSQLHLT 0.523 175 WB Sequence B4501 11 REIVMKYIHY 0.438 437 WB Sequence B4501 134 EELFRDGVNW 0.367 946 Sequence B4501 222 LALVGACITL 0.480 277 WB Sequence B5101 38 PPGAAPAPGI 0.427 490 WB Sequence B5101 166 SPLVDNIALW 0.744 15 SB Sequence B5301 57 HPAASRDPVA 0.665 37 SB Sequence B5401 121 TPFTARGRFA 0.661 39 SB Sequence B5401 51 QPGHTPHPAA 0.476 289 WB Sequence B5401 82 GPALSPVPPV 0.461 340 WB Sequence B5401 86 SPVPPVVHLT 0.434 456 WB Sequence B5401 185 HTWIQDNGGW 0.427 491 WB Sequence B5701 114 MSSQLHLTPF 0.611 67 WB Sequence B5801 185 HTWIQDNGGW 0.580 94 WB Sequence B5801 204 SMRPLFDFSW 0.474 294 WB Sequence B5801 11-mer 223 ALVGACITLGA 0.632 53 WB Sequence A0201 84 ALSPVPPVVHL 0.586 88 WB Sequence A0201 215 SLKTLLSLALV 0.543 141 WB Sequence A0201 188 IQDNGGWDAFV 0.504 215 WB Sequence A0201 219 LLSLALVGACI 0.481 275 WB Sequence A0201 221 SLALVGACITL 0.473 299 WB Sequence A0201 145 RIVAFFEFGGV 0.453 373 WB Sequence A0201 21 KLSQRGYEWDA 0.449 388 WB Sequence A0201 204 SMRPLFDFSWL 0.772 11 SB Sequence A0202 215 SLKTLLSLALV 0.763 12 SB Sequence A0202 221 SLALVGACITL 0.710 23 SB Sequence A0202 84 ALSPVPPVVHL 0.708 23 SB Sequence A0202 219 LLSLALVGACI 0.692 28 SB Sequence A0202 164 EMSPLVDNIAL 0.657 41 SB Sequence A0202 223 ALVGACITLGA 0.630 54 WB Sequence A0202 213 WLSLKTLLSLA 0.616 63 WB Sequence A0202 123 FTARGRFATVV 0.602 74 WB Sequence A0202 78 GAAAGPALSPV 0.597 78 WB Sequence A0202 145 RIVAFFEFGGV 0.569 105 WB Sequence A0202 179 YLNRHLHTWIQ 0.529 163 WB Sequence A0202 21 KLSQRGYEWDA 0.499 226 WB Sequence A0202 131 TVVEELFRDGV 0.478 284 WB Sequence A0202 225 VGACITLGAYL 0.469 312 WB Sequence A0202 215 SLKTLLSLALV 0.899 2 SB Sequence A0203 204 SMRPLFDFSWL 0.853 4 SB Sequence A0203 145 RIVAFFEFGGV 0.813 7 SB Sequence A0203 78 GAAAGPALSPV 0.774 11 SB Sequence A0203 213 WLSLKTLLSLA 0.765 12 SB Sequence A0203 84 ALSPVPPVVHL 0.765 12 SB Sequence A0203 223 ALVGACITLGA 0.751 14 SB Sequence A0203 219 LLSLALVGACI 0.707 23 SB Sequence A0203 123 FTARGRFATVV 0.672 34 SB Sequence A0203 221 SLALVGACITL 0.617 63 WB Sequence A0203 179 YLNRHLHTWIQ 0.565 110 WB Sequence A0203 131 TVVEELFRDGV 0.507 206 WB Sequence A0203 21 KLSQRGYEWDA 0.476 291 WB Sequence A0203 84 ALSPVPPVVHL 0.633 53 WB Sequence A0204 221 SLALVGACITL 0.593 82 WB Sequence A0204 123 FTARGRFATVV 0.587 87 WB Sequence A0204 78 GAAAGPALSPV 0.495 235 WB Sequence A0204 21 KLSQRGYEWDA 0.488 255 WB Sequence A0204 179 YLNRHLHTWIQ 0.461 340 WB Sequence A0204 145 RIVAFFEFGGV 0.868 4 SB Sequence A0206 188 IQDNGGWDAFV 0.822 6 SB Sequence A0206 123 FTARGRFATVV 0.729 18 SB Sequence A0206 131 TVVEELFRDGV 0.725 19 SB Sequence A0206 223 ALVGACITLGA 0.670 35 SB Sequence A0206 50 SQPGHTPHPAA 0.659 40 SB Sequence A0206 71 LQTPAAPGAAA 0.657 40 SB Sequence A0206 78 GAAAGPALSPV 0.598 77 WB Sequence A0206 217 KTLLSLALVGA 0.537 149 WB Sequence A0206 84 ALSPVPPVVHL 0.533 157 WB Sequence A0206 204 SMRPLFDFSWL 0.494 239 WB Sequence A0206 215 SLKTLLSLALV 0.477 286 WB Sequence A0206 213 WLSLKTLLSLA 0.475 293 WB Sequence A0206 27 YEWDAGDVGAA 0.474 295 WB Sequence A0206 21 KLSQRGYEWDA 0.453 373 WB Sequence A0206 84 ALSPVPPVVHL 0.906 2 SB Sequence A0211 215 SLKTLLSLALV 0.896 3 SB Sequence A0211 221 SLALVGACITL 0.892 3 SB Sequence A0211 179 YLNRHLHTWIQ 0.853 4 SB Sequence A0211 164 EMSPLVDNIAL 0.832 6 SB Sequence A0211 204 SMRPLFDFSWL 0.813 7 SB Sequence A0211 223 ALVGACITLGA 0.803 8 SB Sequence A0211 123 FTARGRFATVV 0.782 10 SB Sequence A0211 188 IQDNGGWDAFV 0.746 15 SB Sequence A0211 148 AFFEFGGVMCV 0.730 18 SB Sequence A0211 207 PLFDFSWLSLK 0.720 20 SB Sequence A0211 131 TVVEELFRDGV 0.717 21 SB Sequence A0211 167 PLVDNIALWMT 0.706 24 SB Sequence A0211 21 KLSQRGYEWDA 0.702 25 SB Sequence A0211 213 WLSLKTLLSLA 0.655 41 SB Sequence A0211 145 RIVAFFEFGGV 0.634 52 WB Sequence A0211 199 ELYGPSMRPLF 0.626 56 WB Sequence A0211 219 LLSLALVGACI 0.581 92 WB Sequence A0211 78 GAAAGPALSPV 0.533 156 WB Sequence A0211 137 FRDGVNWGRIV 0.516 187 WB Sequence A0211 218 TLLSLALVGAC 0.500 223 WB Sequence A0211 119 HLTPFTARGRF 0.462 335 WB Sequence A0211 175 WMTEYLNRHLH 0.458 352 WB Sequence A0211 84 ALSPVPPVVHL 0.817 7 SB Sequence A0212 179 YLNRHLHTWIQ 0.794 9 SB Sequence A0212 123 FTARGRFATVV 0.784 10 SB Sequence A0212 204 SMRPLFDFSWL 0.781 10 SB Sequence A0212 215 SLKTLLSLALV 0.719 20 SB Sequence A0212 221 SLALVGACITL 0.719 20 SB Sequence A0212 164 EMSPLVDNIAL 0.714 22 SB Sequence A0212 21 KLSQRGYEWDA 0.616 63 WB Sequence A0212 223 ALVGACITLGA 0.604 72 WB Sequence A0212 131 TVVEELFRDGV 0.602 74 WB Sequence A0212 188 IQDNGGWDAFV 0.569 106 WB Sequence A0212 148 AFFEFGGVMCV 0.548 133 WB Sequence A0212 145 RIVAFFEFGGV 0.511 198 WB Sequence A0212 219 LLSLALVGACI 0.504 213 WB Sequence A0212 167 PLVDNIALWMT 0.483 269 WB Sequence A0212 207 PLFDFSWLSLK 0.472 301 WB Sequence A0212 137 FRDGVNWGRIV 0.431 473 WB Sequence A0212 84 ALSPVPPVVHL 0.878 3 SB Sequence A0216 221 SLALVGACITL 0.855 4 SB Sequence A0216 215 SLKTLLSLALV 0.806 8 SB Sequence A0216 204 SMRPLFDFSWL 0.753 14 SB Sequence A0216 123 FTARGRFATVV 0.739 16 SB Sequence A0216 223 ALVGACITLGA 0.697 26 SB Sequence A0216 188 IQDNGGWDAFV 0.637 50 WB Sequence A0216 164 EMSPLVDNIAL 0.625 57 WB Sequence A0216 179 YLNRHLHTWIQ 0.613 65 WB Sequence A0216 131 TVVEELFRDGV 0.586 88 WB Sequence A0216 78 GAAAGPALSPV 0.571 103 WB Sequence A0216 148 AFFEFGGVMCV 0.563 112 WB Sequence A0216 167 PLVDNIALWMT 0.535 153 WB Sequence A0216 145 RIVAFFEFGGV 0.503 216 WB Sequence A0216 151 EFGGVMCVESV 0.502 217 WB Sequence A0216 213 WLSLKTLLSLA 0.493 241 WB Sequence A0216 21 KLSQRGYEWDA 0.490 248 WB Sequence A0216 219 LLSLALVGACI 0.478 285 WB Sequence A0216 207 PLFDFSWLSLK 0.436 445 WB Sequence A0216 84 ALSPVPPVVHL 0.786 10 SB Sequence A0219 188 IQDNGGWDAFV 0.605 71 WB Sequence A0219 123 FTARGRFATVV 0.594 81 WB Sequence A0219 164 EMSPLVDNIAL 0.584 89 WB Sequence A0219 179 YLNRHLHTWIQ 0.574 100 WB Sequence A0219 221 SLALVGACITL 0.561 115 WB Sequence A0219 219 LLSLALVGACI 0.551 128 WB Sequence A0219 167 PLVDNIALWMT 0.537 149 WB Sequence A0219 78 GAAAGPALSPV 0.496 233 WB Sequence A0219 215 SLKTLLSLALV 0.490 248 WB Sequence A0219 204 SMRPLFDFSWL 0.486 259 WB Sequence A0219 223 ALVGACITLGA 0.467 320 WB Sequence A0219 207 PLFDFSWLSLK 0.604 72 WB Sequence A0301 228 CITLGAYLGHK 0.462 339 WB Sequence A0301 207 PLFDFSWLSLK 0.626 57 WB Sequence A1101 116 SQLHLTPFTAR 0.586 88 WB Sequence A1101 228 CITLGAYLGHK 0.580 94 WB Sequence A1101 172 IALWMTEYLNR 0.524 172 WB Sequence A1101 6 TGYDNREIVMK 0.437 439 WB Sequence A1101 142 NWGRIVAFFEF 0.733 18 SB Sequence A2301 178 EYLNRHLHTWI 0.592 82 WB Sequence A2301 19 HYKLSQRGYEW 0.563 112 WB Sequence A2301 174 LWMTEYLNRHL 0.457 355 WB Sequence A2301 212 SWLSLKTLLSL 0.439 431 WB Sequence A2301 178 EYLNRHLHTWI 0.794 9 SB Sequence A2402 142 NWGRIVAFFEF 0.744 15 SB Sequence A2402 212 SWLSLKTLLSL 0.514 192 WB Sequence A2402 174 LWMTEYLNRHL 0.497 230 WB Sequence A2402 178 EYLNRHLHTWI 0.599 76 WB Sequence A2403 19 HYKLSQRGYEW 0.573 101 WB Sequence A2403 142 NWGRIVAFFEF 0.486 260 WB Sequence A2403 17 YIHYKLSQRGY 0.524 172 WB Sequence A2601 113 EMSSQLHLTPF 0.866 4 SB Sequence A2602 17 YIHYKLSQRGY 0.817 7 SB Sequence A2602 12 EIVMKYIHYKL 0.760 13 SB Sequence A2602 187 WIQDNGGWDAF 0.631 54 WB Sequence A2602 199 ELYGPSMRPLF 0.568 106 WB Sequence A2602 224 LVGACITLGAY 0.545 137 WB Sequence A2602 139 DGVNWGRIVAF 0.462 336 WB Sequence A2602 207 PLFDFSWLSLK 0.456 359 WB Sequence A3001 11 REIVMKYIHYK 0.439 434 WB Sequence A3001 113 EMSSQLHLTPF 0.533 156 WB Sequence A3002 128 RFATVVEELFR 0.765 12 SB Sequence A3101 116 SQLHLTPFTAR 0.741 16 SB Sequence A3101 196 AFVELYGPSMR 0.640 48 SB Sequence A3101 172 IALWMTEYLNR 0.614 64 WB Sequence A3101 11 REIVMKYIHYK 0.571 104 WB Sequence A3101 15 MKYIHYKLSQR 0.500 224 WB Sequence A3101 98 QAGDDFSRRYR 0.483 269 WB Sequence A3101 135 ELFRDGVNWGR 0.634 52 WB Sequence A3301 128 RFATVVEELFR 0.492 244 WB Sequence A3301 172 IALWMTEYLNR 0.481 273 WB Sequence A3301 196 AFVELYGPSMR 0.467 318 WB Sequence A3301 135 ELFRDGVNWGR 0.739 16 SB Sequence A6801 228 CITLGAYLGHK 0.618 62 WB Sequence A6801 172 IALWMTEYLNR 0.593 81 WB Sequence A6801 57 HPAASRDPVAR 0.579 95 WB Sequence A6801 15 MKYIHYKLSQR 0.540 145 WB Sequence A6801 98 QAGDDFSRRYR 0.525 170 WB Sequence A6801 6 TGYDNREIVMK 0.515 190 WB Sequence A6801 128 RFATVVEELFR 0.507 207 WB Sequence A6801 95 TLRQAGDDFSR 0.490 249 WB Sequence A6801 207 PLFDFSWLSLK 0.470 308 WB Sequence A6801 123 FTARGRFATVV 0.809 7 SB Sequence A6802 131 TVVEELFRDGV 0.784 10 SB Sequence A6802 145 RIVAFFEFGGV 0.727 19 SB Sequence A6802 12 EIVMKYIHYKL 0.592 83 WB Sequence A6802 78 GAAAGPALSPV 0.560 116 WB Sequence A6802 164 EMSPLVDNIAL 0.520 179 WB Sequence A6802 159 ESVNREMSPLV 0.488 254 WB Sequence A6802 225 VGACITLGAYL 0.459 349 WB Sequence A6802 55 TPHPAASRDPV 0.435 453 WB Sequence A6802 123 FTARGRFATVV 0.710 23 SB Sequence A6901 164 EMSPLVDNIAL 0.541 144 WB Sequence A6901 131 TVVEELFRDGV 0.510 201 WB Sequence A6901 159 ESVNREMSPLV 0.485 263 WB Sequence A6901 206 RPLFDFSWLSL 0.747 15 SB Sequence B0702 86 SPVPPVVHLTL 0.717 21 SB Sequence B0702 55 TPHPAASRDPV 0.567 108 WB Sequence B0702 82 GPALSPVPPVV 0.559 118 WB Sequence B0702 166 SPLVDNIALWM 0.469 312 WB Sequence B0702 126 RGRFATVVEEL 0.463 332 WB Sequence B0702 121 TPFTARGRFAT 0.443 416 WB Sequence B0702 97 RQAGDDFSRRY 0.600 75 WB Sequence B1501 187 WIQDNGGWDAF 0.499 226 WB Sequence B1501 224 LVGACITLGAY 0.491 245 WB Sequence B1501 17 YIHYKLSQRGY 0.476 290 WB Sequence B1501 113 EMSSQLHLTPF 0.433 461 WB Sequence B1501 140 GVNWGRIVAFF 0.433 463 WB Sequence B1501 177 TEYLNRHLHTW 0.585 89 WB Sequence B1801 198 VELYGPSMRPL 0.558 119 WB Sequence B1801 158 VESVNREMSPL 0.514 191 WB Sequence B1801 133 VEELFRDGVNW 0.459 348 WB Sequence B1801 127 GRFATVVEELF 0.512 196 WB Sequence B2705 108 RRDFAEMSSQL 0.481 273 WB Sequence B2705 97 RQAGDDFSRRY 0.445 405 WB Sequence B2705 166 SPLVDNIALWM 0.573 101 WB Sequence B3501 187 WIQDNGGWDAF 0.544 139 WB Sequence B3501 195 DAFVELYGPSM 0.543 140 WB Sequence B3501 113 EMSSQLHLTPF 0.543 140 WB Sequence B3501 121 TPFTARGRFAT 0.503 217 WB Sequence B3501 224 LVGACITLGAY 0.502 218 WB Sequence B3501 146 IVAFFEFGGVM 0.500 222 WB Sequence B3501 86 SPVPPVVHLTL 0.443 416 WB Sequence B3501 139 DGVNWGRIVAF 0.442 419 WB Sequence B3501 61 SRDPVARTSPL 0.500 223 WB Sequence B3901 198 VELYGPSMRPL 0.547 134 WB Sequence B4001 158 VESVNREMSPL 0.471 306 WB Sequence B4001 177 TEYLNRHLHTW 0.520 180 WB Sequence B4402 112 AEMSSQLHLTP 0.529 163 WB Sequence B4501 37 APPGAAPAPGI 0.507 207 WB Sequence B5101 82 GPALSPVPPVV 0.465 326 WB Sequence B5101 86 SPVPPVVHLTL 0.433 461 WB Sequence B5101 166 SPLVDNIALWM 0.453 373 WB Sequence B5301 206 RPLFDFSWLSL 0.436 448 WB Sequence B5301 121 TPFTARGRFAT 0.638 50 WB Sequence B5401 69 SPLQTPAAPGA 0.557 121 WB Sequence B5401 89 PPVVHLTLRQA 0.501 220 WB Sequence B5401 55 TPHPAASRDPV 0.428 489 WB Sequence B5401 165 MSPLVDNIALW 0.462 335 WB Sequence B5701 203 PSMRPLFDFSW 0.635 51 WB Sequence B5801 SEQ ID NOS: 44893-45800

Preferred fragments of BclX(L) capable of interacting with one or more MHC class 2 molecules are listed in table D.

TABLE D Prediction of cancer antigen BclX(L) specific MHC class 2, 15-mer peptide binders for 14 MHC class 2 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHCII/ database. The MHC class 2 molecules for which no binders were found are not listed. Allele pos peptide  core 1−log50k(aff) affinity(nM) Bind Level Identity DRB1_0101 212 RWFLTGMTVAGVVLL  LTGMTVAGV 0.8028 8 SB BclX(L) DRB1_0101 209 RFNRWFLTGMTVAGV  FLTGMTVAG 0.7932 9 SB BclX(L) DRB1_0101 210 FNRWFLTGMTVAGVV  LTGMTVAGV 0.7940 9 SB BclX(L) DRB1_0101 211 NRWFLTGMTVAGVVL  LTGMTVAGV 0.7970 9 SB BclX(L) DRB1_0101 213 WFLTGMTVAGVVLLG  LTGMTVAGV 0.7753 11 SB BclX(L) DRB1_0101 76 DAREVIPMAAVKQAL  VIPMAAVKQ 0.7755 11 SB BclX(L) DRB1_0101 77 AREVIPMAAVKQALR  VIPMAAVKQ 0.7788 11 SB BclX(L) DRB1_0101 78 REVIPMAAVKQALRE  VIPMAAVKQ 0.7772 11 SB BclX(L) DRB1_0101 75 LDAREVIPMAAVKQA  VIPMAAVKQ 0.7730 12 SB BclX(L) DRB1_0101 157 KEMQVLVSRIAAWMA  MQVLVSRIA 0.7458 16 SB BclX(L) DRB1_0101 108 LTSQLHITPGTAYQS  LHITPGTAY 0.7338 18 SB BclX(L) DRB1_0101 109 TSQLHITPGTAYQSF  ITPGTAYQS 0.7313 18 SB BclX(L) DRB1_0101 74 SLDAREVIPMAAVKQ  AREVIPMAA 0.7348 18 SB BclX(L) DRB1_0101 110 SQLHITPGTAYQSFE  ITPGTAYQS 0.7287 19 SB BclX(L) DRB1_0101 214 FLTGMTVAGVVLLGS  LTGMTVAGV 0.7282 19 SB BclX(L) DRB1_0101 156 DKEMQVLVSRIAAWM  MQVLVSRIA 0.7226 20 SB BclX(L) DRB1_0101 111 QLHITPGTAYQSFEQ  ITPGTAYQS 0.7202 21 SB BclX(L) DRB1_0101 112 LHITPGTAYQSFEQV  ITPGTAYQS 0.7189 21 SB BclX(L) DRB1_0101 154 SVDKEMQVLVSRIAA  MQVLVSRIA 0.7165 21 SB BclX(L) DRB1_0101 79 EVIPMAAVKQALREA  IPMAAVKQA 0.7208 21 SB BclX(L) DRB1_0101 153 ESVDKEMQVLVSRIA  VDKEMQVLV 0.7145 22 SB BclX(L) DRB1_0101 155 VDKEMQVLVSRIAAW  MQVLVSRIA 0.7141 22 SB BclX(L) DRB1_0101 215 LTGMTVAGVVLLGSL  LTGMTVAGV 0.7090 23 SB BclX(L) DRB1_0101 208 ERFNRWFLTGMTVAG  FNRWFLTGM 0.7077 24 SB BclX(L) DRB1_0101 46 ETPSAINGNPSWHLA  INGNPSWHL 0.7051 24 SB BclX(L) DRB1_0101 47 TPSAINGNPSWHLAD  INGNPSWHL 0.7051 24 SB BclX(L) DRB1_0101 48 PSAINGNPSWHLADS  INGNPSWHL 0.7076 24 SB BclX(L) DRB1_0101 49 SAINGNPSWHLADSP  INGNPSWHL 0.7072 24 SB BclX(L) DRB1_0101 45 METPSAINGNPSWHL  PSAINGNPS 0.7034 25 SB BclX(L) DRB1_0101 158 EMQVLVSRIAAWMAT  MQVLVSRIA 0.6845 30 SB BclX(L) DRB1_0101 80 VIPMAAVKQALREAG  VIPMAAVKQ 0.6856 30 SB BclX(L) DRB1_0101 159 MQVLVSRIAAWMATY  MQVLVSRIA 0.6834 31 SB BclX(L) DRB1_0101 161 VLVSRIAAWMATYLN  IAAWMATYL 0.6838 31 SB BclX(L) DRB1_0101 217 GMTVAGVVLLGSLFS  MTVAGVVLL 0.6800 32 SB BclX(L) DRB1_0101 218 MTVAGVVLLGSLFSR  VVLLGSLFS 0.6800 32 SB BclX(L) DRB1_0101 51 INGNPSWHLADSPAV  INGNPSWHL 0.6778 33 SB BclX(L) DRB1_0101 192 VELYGNNAAAESRKG  YGNNAAAES 0.6693 36 SB BclX(L) DRB1_0101 219 TVAGVVLLGSLFSRK  VVLLGSLFS 0.6677 36 SB BclX(L) DRB1_0101 160 QVLVSRIAAWMATYL  VSRIAAWMA 0.6652 37 SB BclX(L) DRB1_0101 191 FVELYGNNAAAESRK  YGNNAAAES 0.6658 37 SB BclX(L) DRB1_0101 193 ELYGNNAAAESRKGQ  YGNNAAAES 0.6661 37 SB BclX(L) DRB1_0101 99 LRYRRAFSDLTSQLH  YRRAFSDLT 0.6657 37 SB BclX(L) DRB1_0101 162 LVSRIAAWMATYLND  IAAWMATYL 0.6627 38 SB BclX(L) DRB1_0101 190 TFVELYGNNAAAESR  YGNNAAAES 0.6628 38 SB BclX(L) DRB1_0101 189 DTFVELYGNNAAAES  FVELYGNNA 0.6613 39 SB BclX(L) DRB1_0101 54 NPSWHLADSPAVNGA  WHLADSPAV 0.6617 39 SB BclX(L) DRB1_0101 55 PSWHLADSPAVNGAT  WHLADSPAV 0.6611 39 SB BclX(L) DRB1_0101 216 TGMTVAGVVLLGSLF  MTVAGVVLL 0.6543 42 SB BclX(L) DRB1_0101 163 VSRIAAWMATYLNDH  IAAWMATYL 0.6531 43 SB BclX(L) DRB1_0101 53 GNPSWHLADSPAVNG  WHLADSPAV 0.6532 43 SB BclX(L) DRB1_0101 59 LADSPAVNGATGHSS  LADSPAVNG 0.6361 51 WB BclX(L) DRB1_0101 98 ELRYRRAFSDLTSQL  YRRAFSDLT 0.6357 51 WB BclX(L) DRB1_0101 164 SRIAAWMATYLNDHL  IAAWMATYL 0.6357 52 WB BclX(L) DRB1_0101 97 FELRYRRAFSDLTSQ  YRRAFSDLT 0.6337 53 WB BclX(L) DRB1_0101 96 EFELRYRRAFSDLTS  YRRAFSDLT 0.6321 54 WB BclX(L) DRB1_0101 95 DEFELRYRRAFSDLT  LRYRRAFSD 0.6294 55 WB BclX(L) DRB1_0101 140 IVAFFSFGGALCVES  FSFGGALCV 0.6203 61 WB BclX(L) DRB1_0101 56 SWHLADSPAVNGATG  LADSPAVNG 0.6196 61 WB BclX(L) DRB1_0101 61 DSPAVNGATGHSSSL  VNGATGHSS 0.6197 61 WB BclX(L) DRB1_0101 62 SPAVNGATGHSSSLD  VNGATGHSS 0.6205 61 WB BclX(L) DRB1_0101 141 VAFFSFGGALCVESV  FSFGGALCV 0.6191 62 WB BclX(L) DRB1_0101 60 ADSPAVNGATGHSSS  VNGATGHSS 0.6174 63 WB BclX(L) DRB1_0101 142 AFFSFGGALCVESVD  FSFGGALCV 0.6153 64 WB BclX(L) DRB1_0101 57 WHLADSPAVNGATGH  LADSPAVNG 0.6162 64 WB BclX(L) DRB1_0101 113 HITPGTAYQSFEQVV  ITPGTAYQS 0.6121 66 WB BclX(L) DRB1_0101 114 ITPGTAYQSFEQVVN  ITPGTAYQS 0.6131 66 WB BclX(L) DRB1_0101 50 AINGNPSWHLADSPA  INGNPSWHL 0.6133 66 WB BclX(L) DRB1_0101 63 PAVNGATGHSSSLDA  VNGATGHSS 0.6078 70 WB BclX(L) DRB1_0101 100 RYRRAFSDLTSQLHI  YRRAFSDLT 0.6026 74 WB BclX(L) DRB1_0101 101 YRRAFSDLTSQLHIT  YRRAFSDLT 0.6021 74 WB BclX(L) DRB1_0101 52 NGNPSWHLADSPAVN  WHLADSPAV 0.6004 75 WB BclX(L) DRB1_0101 138 GRIVAFFSFGGALCV  IVAFFSFGG 0.5864 88 WB BclX(L) DRB1_0101 194 LYGNNAAAESRKGQE  YGNNAAAES 0.5808 93 WB BclX(L) DRB1_0101 165 RIAAWMATYLNDHLE  AAWMATYLN 0.5762 98 WB BclX(L) DRB1_0101 195 YGNNAAAESRKGQER  YGNNAAAES 0.5731 101 WB BclX(L) DRB1_0101 139 RIVAFFSFGGALCVE  FSFGGALCV 0.5729 102 WB BclX(L) DRB1_0101 131 FRDGVNWGRIVAFFS  VNWGRIVAF 0.5627 114 WB BclX(L) DRB1_0101 143 FFSFGGALCVESVDK  FSFGGALCV 0.5613 115 WB BclX(L) DRB1_0101 144 FSFGGALCVESVDKE  FSFGGALCV 0.5583 119 WB BclX(L) DRB1_0101 132 RDGVNWGRIVAFFSF  VNWGRIVAF 0.5561 122 WB BclX(L) DRB1_0101 133 DGVNWGRIVAFFSFG  VNWGRIVAF 0.5558 122 WB BclX(L) DRB1_0101 81 IPMAAVKQALREAGD  IPMAAVKQA 0.5527 126 WB BclX(L) DRB1_0101 102 RRAFSDLTSQLHITP  FSDLTSQLH 0.5334 156 WB BclX(L) DRB1_0101 103 RAFSDLTSQLHITPG  FSDLTSQLH 0.5314 159 WB BclX(L) DRB1_0101 58 HLADSPAVNGATGHS  LADSPAVNG 0.5293 163 WB BclX(L) DRB1_0101 134 GVNWGRIVAFFSFGG  VNWGRIVAF 0.5282 165 WB BclX(L) DRB1_0101 166 IAAWMATYLNDHLEP  IAAWMATYL 0.5271 167 WB BclX(L) DRB1_0101 64 AVNGATGHSSSLDAR  VNGATGHSS 0.5266 168 WB BclX(L) DRB1_0101 135 VNWGRIVAFFSFGGA  VNWGRIVAF 0.5248 171 WB BclX(L) DRB1_0101 7 ELVVDFLSYKLSQKG  VVDFLSYKL 0.5243 172 WB BclX(L) DRB1_0101 129 ELFRDGVNWGRIVAF  FRDGVNWGR 0.5154 189 WB BclX(L) DRB1_0101 65 VNGATGHSSSLDARE  VNGATGHSS 0.5156 189 WB BclX(L) DRB1_0101 130 LFRDGVNWGRIVAFF  VNWGRIVAF 0.5023 218 WB BclX(L) DRB1_0101 8 LVVDFLSYKLSQKGY  LSYKLSQKG 0.4921 244 WB BclX(L) DRB1_0101 9 VVDFLSYKLSQKGYS  LSYKLSQKG 0.4892 251 WB BclX(L) DRB1_0101 207 QERFNRWFLTGMTVA  FNRWFLTGM 0.4845 264 WB BclX(L) DRB1_0101 42 ESEMETPSAINGNPS  METPSAING 0.4626 335 WB BclX(L) DRB1_0101 40 GTESEMETPSAINGN  METPSAING 0.4622 337 WB BclX(L) DRB1_0101 107 DLTSQLHITPGTAYQ  LHITPGTAY 0.4593 347 WB BclX(L) DRB1_0101 39 EGTESEMETPSAING  ESEMETPSA 0.4591 348 WB BclX(L) DRB1_0101 43 SEMETPSAINGNPSW  METPSAING 0.4590 348 WB BclX(L) DRB1_0101 106 SDLTSQLHITPGTAY  SQLHITPGT 0.4569 356 WB BclX(L) DRB1_0101 10 VDFLSYKLSQKGYSW  LSYKLSQKG 0.4565 358 WB BclX(L) DRB1_0101 41 TESEMETPSAINGNP  METPSAING 0.4564 358 WB BclX(L) DRB1_0101 167 AAWMATYLNDHLEPW  AAWMATYLN 0.4556 361 WB BclX(L) DRB1_0101 11 DFLSYKLSQKGYSWS  LSYKLSQKG 0.4515 378 WB BclX(L) DRB1_0101 104 AFSDLTSQLHITPGT  FSDLTSQLH 0.4453 404 WB BclX(L) DRB1_0101 105 FSDLTSQLHITPGTA  FSDLTSQLH 0.4451 405 WB BclX(L) DRB1_0101 137 WGRIVAFFSFGGALC  IVAFFSFGG 0.4311 471 WB BclX(L) DRB1_0101 206 GQERFNRWFLTGMTV  FNRWFLTGM 0.4277 489 WB BclX(L) DRB1_0401 99 LRYRRAFSDLTSQLH  YRRAFSDLT 0.5618 115 WB BclX(L) DRB1_0401 97 FELRYRRAFSDLTSQ  YRRAFSDLT 0.5300 162 WB BclX(L) DRB1_0401 96 EFELRYRRAFSDLTS  YRRAFSDLT 0.5284 164 WB BclX(L) DRB1_0401 95 DEFELRYRRAFSDLT  DEFELRYRR 0.5275 166 WB BclX(L) DRB1_0401 98 ELRYRRAFSDLTSQL  YRRAFSDLT 0.5259 169 WB BclX(L) DRB1_0401 185 NGGWDTFVELYGNNA  WDTFVELYG 0.5189 182 WB BclX(L) DRB1_0401 186 GGWDTFVELYGNNAA  FVELYGNNA 0.5180 184 WB BclX(L) DRB1_0401 188 WDTFVELYGNNAAAE  FVELYGNNA 0.5159 188 WB BclX(L) DRB1_0401 187 GWDTFVELYGNNAAA  FVELYGNNA 0.5157 189 WB BclX(L) DRB1_0401 189 DTFVELYGNNAAAES  FVELYGNNA 0.5154 189 WB BclX(L) DRB1_0401 100 RYRRAFSDLTSQLHI  YRRAFSDLT 0.4844 265 WB BclX(L) DRB1_0401 101 YRRAFSDLTSQLHIT  YRRAFSDLT 0.4813 274 WB BclX(L) DRB1_0401 153 ESVDKEMQVLVSRIA  KEMQVLVSR 0.4561 360 WB BclX(L) DRB1_0401 155 VDKEMQVLVSRIAAW  MQVLVSRIA 0.4519 376 WB BclX(L) DRB1_0401 208 ERFNRWFLTGMTVAG  WFLTGMTVA 0.4512 379 WB BclX(L) DRB1_0401 154 SVDKEMQVLVSRIAA  MQVLVSRIA 0.4495 386 WB BclX(L) DRB1_0401 209 RFNRWFLTGMTVAGV  FLTGMTVAG 0.4467 398 WB BclX(L) DRB1_0401 210 FNRWFLTGMTVAGVV  FLTGMTVAG 0.4427 416 WB BclX(L) DRB1_0401 157 KEMQVLVSRIAAWMA  MQVLVSRIA 0.4419 419 WB BclX(L) DRB1_0401 156 DKEMQVLVSRIAAWM  MQVLVSRIA 0.4413 422 WB BclX(L) DRB1_0401 211 NRWFLTGMTVAGVVL  FLTGMTVAG 0.4327 463 WB BclX(L) DRB1_0404 167 AAWMATYLNDHLEPW  WMATYLNDH 0.5484 132 WB BclX(L) DRB1_0404 164 SRIAAWMATYLNDHL  WMATYLNDH 0.5424 141 WB BclX(L) DRB1_0404 165 RIAAWMATYLNDHLE  WMATYLNDH 0.5417 142 WB BclX(L) DRB1_0404 166 IAAWMATYLNDHLEP  WMATYLNDH 0.5330 156 WB BclX(L) DRB1_0404 163 VSRIAAWMATYLNDH  AAWMATYLN 0.5217 177 WB BclX(L) DRB1_0404 219 TVAGVVLLGSLFSRK  VVLLGSLFS 0.5094 202 WB BclX(L) DRB1_0404 209 RFNRWFLTGMTVAGV  FLTGMTVAG 0.4902 249 WB BclX(L) DRB1_0404 210 FNRWFLTGMTVAGVV  FLTGMTVAG 0.4853 262 WB BclX(L) DRB1_0404 211 NRWFLTGMTVAGVVL  FLTGMTVAG 0.4826 270 WB BclX(L) DRB1_0404 208 ERFNRWFLTGMTVAG  WFLTGMTVA 0.4761 290 WB BclX(L) DRB1_0404 168 AWMATYLNDHLEPWI  WMATYLNDH 0.4694 311 WB BclX(L) DRB1_0404 212 RWFLTGMTVAGVVLL  FLTGMTVAG 0.4547 365 WB BclX(L) DRB1_0404 189 DTFVELYGNNAAAES  FVELYGNNA 0.4505 382 WB BclX(L) DRB1_0404 187 GWDTFVELYGNNAAA  FVELYGNNA 0.4498 385 WB BclX(L) DRB1_0404 169 WMATYLNDHLEPWIQ  WMATYLNDH 0.4478 393 WB BclX(L) DRB1_0404 188 WDTFVELYGNNAAAE  FVELYGNNA 0.4462 400 WB BclX(L) DRB1_0404 186 GGWDTFVELYGNNAA  FVELYGNNA 0.4437 411 WB BclX(L) DRB1_0404 185 NGGWDTFVELYGNNA  GWDTFVELY 0.4388 434 WB BclX(L) DRB1_0405 118 TAYQSFEQVVNELFR  YQSFEQVVN 0.5794 95 WB BclX(L) DRB1_0405 117 GTAYQSFEQVVNELF  YQSFEQVVN 0.5772 97 WB BclX(L) DRB1_0405 115 TPGTAYQSFEQVVNE  YQSFEQVVN 0.5541 124 WB BclX(L) DRB1_0405 116 PGTAYQSFEQVVNEL  YQSFEQVVN 0.5538 125 WB BclX(L) DRB1_0405 114 ITPGTAYQSFEQVVN  AYQSFEQVV 0.5505 129 WB BclX(L) DRB1_0405 163 VSRIAAWMATYLNDH  AAWMATYLN 0.5510 129 WB BclX(L) DRB1_0405 162 LVSRIAAWMATYLND  AAWMATYLN 0.5473 134 WB BclX(L) DRB1_0405 161 VLVSRIAAWMATYLN  IAAWMATYL 0.5442 139 WB BclX(L) DRB1_0405 164 SRIAAWMATYLNDHL  AAWMATYLN 0.5402 145 WB BclX(L) DRB1_0405 99 LRYRRAFSDLTSQLH  YRRAFSDLT 0.5100 201 WB BclX(L) DRB1_0405 97 FELRYRRAFSDLTSQ  YRRAFSDLT 0.5085 204 WB BclX(L) DRB1_0405 96 EFELRYRRAFSDLTS  YRRAFSDLT 0.5069 208 WB BclX(L) DRB1_0405 165 RIAAWMATYLNDHLE  AAWMATYLN 0.5055 211 WB BclX(L) DRB1_0405 119 AYQSFEQVVNELFRD  YQSFEQVVN 0.4974 230 WB BclX(L) DRB1_0405 120 YQSFEQVVNELFRDG  YQSFEQVVN 0.4968 231 WB BclX(L) DRB1_0405 98 ELRYRRAFSDLTSQL  YRRAFSDLT 0.4923 243 WB BclX(L) DRB1_0405 18 SQKGYSWSQFSDVEE  GYSWSQFSD 0.4575 354 WB BclX(L) DRB1_0405 95 DEFELRYRRAFSDLT  LRYRRAFSD 0.4574 355 WB BclX(L) DRB1_0405 19 QKGYSWSQFSDVEEN  WSQFSDVEE 0.4562 359 WB BclX(L) DRB1_0405 100 RYRRAFSDLTSQLHI  YRRAFSDLT 0.4475 395 WB BclX(L) DRB1_0405 20 KGYSWSQFSDVEENR  WSQFSDVEE 0.4430 414 WB BclX(L) DRB1_0405 166 IAAWMATYLNDHLEP  AAWMATYLN 0.4423 418 WB BclX(L) DRB1_0405 21 GYSWSQFSDVEENRT  WSQFSDVEE 0.4353 450 WB BclX(L) DRB1_0701 157 KEMQVLVSRIAAWMA  VLVSRIAAW 0.5228 175 WB BclX(L) DRB1_0701 159 MQVLVSRIAAWMATY  VLVSRIAAW 0.5194 181 WB BclX(L) DRB1_0701 158 EMQVLVSRIAAWMAT  VLVSRIAAW 0.5191 182 WB BclX(L) DRB1_0701 156 DKEMQVLVSRIAAWM  VLVSRIAAW 0.4971 231 WB BclX(L) DRB1_0701 160 QVLVSRIAAWMATYL  VLVSRIAAW 0.4833 268 WB BclX(L) DRB1_0701 46 ETPSAINGNPSWHLA  INGNPSWHL 0.4783 283 WB BclX(L) DRB1_0701 45 METPSAINGNPSWHL  AINGNPSWH 0.4779 284 WB BclX(L) DRB1_0701 155 VDKEMQVLVSRIAAW  MQVLVSRIA 0.4772 286 WB BclX(L) DRB1_0701 47 TPSAINGNPSWHLAD  INGNPSWHL 0.4774 286 WB BclX(L) DRB1_0701 48 PSAINGNPSWHLADS  INGNPSWHL 0.4764 289 WB BclX(L) DRB1_0701 161 VLVSRIAAWMATYLN  VLVSRIAAW 0.4745 295 WB BclX(L) DRB1_0701 49 SAINGNPSWHLADSP  INGNPSWHL 0.4718 303 WB BclX(L) DRB1_0701 99 LRYRRAFSDLTSQLH  YRRAFSDLT 0.4627 335 WB BclX(L) DRB1_0701 100 RYRRAFSDLTSQLHI  FSDLTSQLH 0.4416 420 WB BclX(L) DRB1_0701 101 YRRAFSDLTSQLHIT  FSDLTSQLH 0.4344 455 WB BclX(L) DRB1_0701 51 INGNPSWHLADSPAV  INGNPSWHL 0.4291 481 WB BclX(L) DRB1_0901 55 PSWHLADSPAVNGAT  WHLADSPAV 0.5482 133 WB BclX(L) DRB1_0901 54 NPSWHLADSPAVNGA  WHLADSPAV 0.5414 143 WB BclX(L) DRB1_0901 53 GNPSWHLADSPAVNG  WHLADSPAV 0.5408 144 WB BclX(L) DRB1_0901 51 INGNPSWHLADSPAV  SWHLADSPA 0.5289 164 WB BclX(L) DRB1_0901 52 NGNPSWHLADSPAVN  WHLADSPAV 0.5284 164 WB BclX(L) DRB1_0901 56 SWHLADSPAVNGATG  WHLADSPAV 0.4678 317 WB BclX(L) DRB1_0901 57 WHLADSPAVNGATGH  WHLADSPAV 0.4636 331 WB BclX(L) DRB1_0901 212 RWFLTGMTVAGVVLL  FLTGMTVAG 0.4483 391 WB BclX(L) DRB1_0901 213 WFLTGMTVAGVVLLG  MTVAGVVLL 0.4445 408 WB BclX(L) DRB1_0901 214 FLTGMTVAGVVLLGS  MTVAGVVLL 0.4327 463 WB BclX(L) DRB1_1101 157 KEMQVLVSRIAAWMA  MQVLVSRIA 0.4319 467 WB BclX(L) DRB1_1101 131 FRDGVNWGRIVAFFS  GVNWGRIVA 0.4310 472 WB BclX(L) DRB1_1101 156 DKEMQVLVSRIAAWM  MQVLVSRIA 0.4308 473 WB BclX(L) DRB1_1101 155 VDKEMQVLVSRIAAW  MQVLVSRIA 0.4292 481 WB BclX(L) DRB1_1101 132 RDGVNWGRIVAFFSF  GVNWGRIVA 0.4283 486 WB BclX(L) DRB1_1101 154 SVDKEMQVLVSRIAA  MQVLVSRIA 0.4267 494 WB BclX(L) DRB1_1302 218 MTVAGVVLLGSLFSR  VVLLGSLFS 0.4945 237 WB BclX(L) DRB1_1302 216 TGMTVAGVVLLGSLF  MTVAGVVLL 0.4855 262 WB BclX(L) DRB1_1302 214 FLTGMTVAGVVLLGS  MTVAGVVLL 0.4842 265 WB BclX(L) DRB1_1302 217 GMTVAGVVLLGSLFS  MTVAGVVLL 0.4840 266 WB BclX(L) DRB1_1302 212 RWFLTGMTVAGVVLL  FLTGMTVAG 0.4832 268 WB BclX(L) DRB1_1302 215 LTGMTVAGVVLLGSL  MTVAGVVLL 0.4775 285 WB BclX(L) DRB1_1302 213 WFLTGMTVAGVVLLG  MTVAGVVLL 0.4716 304 WB BclX(L) DRB1_1302 189 DTFVELYGNNAAAES  VELYGNNAA 0.4688 313 WB BclX(L) DRB1_1302 190 TFVELYGNNAAAESR  YGNNAAAES 0.4615 339 WB BclX(L) DRB1_1302 191 FVELYGNNAAAESRK  YGNNAAAES 0.4526 373 WB BclX(L) DRB1_1302 192 VELYGNNAAAESRKG  YGNNAAAES 0.4415 421 WB BclX(L) DRB1_1302 219 TVAGVVLLGSLFSRK  VVLLGSLFS 0.4384 436 WB BclX(L) DRB1_1302 193 ELYGNNAAAESRKGQ  YGNNAAAES 0.4275 490 WB BclX(L) DRB1_1501 219 TVAGVVLLGSLFSRK  VLLGSLFSR 0.6681 36 SB BclX(L) DRB1_1501 218 MTVAGVVLLGSLFSR  VVLLGSLFS 0.6441 47 SB BclX(L) DRB1_1501 6 RELVVDFLSYKLSQK  LVVDFLSYK 0.5208 179 WB BclX(L) DRB1_1501 7 ELVVDFLSYKLSQKG  FLSYKLSQK 0.5009 221 WB BclX(L) DRB1_1501 157 KEMQVLVSRIAAWMA  MQVLVSRIA 0.4968 231 WB BclX(L) DRB1_1501 156 DKEMQVLVSRIAAWM  MQVLVSRIA 0.4965 232 WB BclX(L) DRB1_1501 209 RFNRWFLTGMTVAGV  FNRWFLTGM 0.4870 257 WB BclX(L) DRB1_1501 164 SRIAAWMATYLNDHL  WMATYLNDH 0.4849 263 WB BclX(L) DRB1_1501 210 FNRWFLTGMTVAGVV  LTGMTVAGV 0.4836 267 WB BclX(L) DRB1_1501 8 LVVDFLSYKLSQKGY  FLSYKLSQK 0.4778 284 WB BclX(L) DRB1_1501 5 NRELVVDFLSYKLSQ  LVVDFLSYK 0.4777 285 WB BclX(L) DRB1_1501 135 VNWGRIVAFFSFGGA  IVAFFSFGG 0.4756 291 WB BclX(L) DRB1_1501 4 SNRELVVDFLSYKLS  LVVDFLSYK 0.4755 291 WB BclX(L) DRB1_1501 159 MQVLVSRIAAWMATY  LVSRIAAWM 0.4693 312 WB BclX(L) DRB1_1501 163 VSRIAAWMATYLNDH  IAAWMATYL 0.4691 312 WB BclX(L) DRB1_1501 158 EMQVLVSRIAAWMAT  VLVSRIAAW 0.4683 315 WB BclX(L) DRB1_1501 165 RIAAWMATYLNDHLE  WMATYLNDH 0.4685 315 WB BclX(L) DRB1_1501 128 NELFRDGVNWGRIVA  LFRDGVNWG 0.4675 318 WB BclX(L) DRB1_1501 125 QVVNELFRDGVNWGR  LFRDGVNWG 0.4668 320 WB BclX(L) DRB1_1501 126 VVNELFRDGVNWGRI  LFRDGVNWG 0.4668 320 WB BclX(L) DRB1_1501 166 IAAWMATYLNDHLEP  WMATYLNDH 0.4649 327 WB BclX(L) DRB1_1501 137 WGRIVAFFSFGGALC  IVAFFSFGG 0.4643 329 WB BclX(L) DRB1_1501 136 NWGRIVAFFSFGGAL  IVAFFSFGG 0.4638 331 WB BclX(L) DRB1_1501 207 QERFNRWFLTGMTVA  FNRWFLTGM 0.4608 342 WB BclX(L) DRB1_1501 208 ERFNRWFLTGMTVAG  FNRWFLTGM 0.4602 344 WB BclX(L) DRB1_1501 138 GRIVAFFSFGGALCV  IVAFFSFGG 0.4587 350 WB BclX(L) DRB1_1501 9 VVDFLSYKLSQKGYS  FLSYKLSQK 0.4584 351 WB BclX(L) DRB1_1501 155 VDKEMQVLVSRIAAW  MQVLVSRIA 0.4570 356 WB BclX(L) DRB1_1501 167 AAWMATYLNDHLEPW  WMATYLNDH 0.4551 364 WB BclX(L) DRB1_1501 3 QSNRELVVDFLSYKL  LVVDFLSYK 0.4543 367 WB BclX(L) DRB1_1501 127 VNELFRDGVNWGRIV  LFRDGVNWG 0.4431 414 WB BclX(L) DRB1_1501 134 GVNWGRIVAFFSFGG  VNWGRIVAF 0.4391 432 WB BclX(L) DRB1_1501 129 ELFRDGVNWGRIVAF  LFRDGVNWG 0.4390 433 WB BclX(L) DRB1_1501 217 GMTVAGVVLLGSLFS  VAGVVLLGS 0.4377 439 WB BclX(L) DRB1_1501 124 EQVVNELFRDGVNWG  VVNELFRDG 0.4373 441 WB BclX(L) DRB1_1501 139 RIVAFFSFGGALCVE  IVAFFSFGG 0.4300 477 WB BclX(L) DRB1_1501 211 NRWFLTGMTVAGVVL  LTGMTVAGV 0.4264 496 WB BclX(L) DRB4_0101 99 LRYRRAFSDLTSQLH  YRRAFSDLT 0.4654 325 WB BclX(L) DRB4_0101 100 RYRRAFSDLTSQLHI  FSDLTSQLH 0.4328 463 WB BclX(L) SEQ ID NOS: 47134-47645

Preferred fragments of Bcl-2 capable of interacting with one or more MHC class 2 molecules are listed in table E.

TABLE E Prediction of cancer antigen Bcl-2 specific MHC class 2, 15-mer peptide binders for 14 MHC class 2 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHCII/ database. The MHC class 2 molecules for which no binders were found are not listed. Allele pos peptide  core 1−log50k(aff) affinity(nM) Bind Level Identity DRB1_0101 211 DFSWLSLKTLLSLAL  WLSLKTLLS 0.8912 3 SB Bcl-2 DRB1_0101 212 FSWLSLKTLLSLALV  LKTLLSLAL 0.8917 3 SB Bcl-2 DRB1_0101 214 WLSLKTLLSLALVGA  LKTLLSLAL 0.8933 3 SB Bcl-2 DRB1_0101 215 LSLKTLLSLALVGAC  LKTLLSLAL 0.8867 3 SB Bcl-2 DRB1_0101 213 SWLSLKTLLSLALVG  LKTLLSLAL 0.8776 4 SB Bcl-2 DRB1_0101 216 SLKTLLSLALVGACI  LKTLLSLAL 0.8024 8 SB Bcl-2 DRB1_0101 217 LKTLLSLALVGACIT  LKTLLSLAL 0.8038 8 SB Bcl-2 DRB1_0101 68 RTSPLQTPAAPGAAA  LQTPAAPGA 0.7623 13 SB Bcl-2 DRB1_0101 69 TSPLQTPAAPGAAAG  LQTPAAPGA 0.7650 13 SB Bcl-2 DRB1_0101 70 SPLQTPAAPGAAAGP  LQTPAAPGA 0.7631 13 SB Bcl-2 DRB1_0101 66 VARTSPLQTPAAPGA  TSPLQTPAA 0.7565 14 SB Bcl-2 DRB1_0101 67 ARTSPLQTPAAPGAA  LQTPAAPGA 0.7584 14 SB Bcl-2 DRB1_0101 209 LFDFSWLSLKTLLSL  WLSLKTLLS 0.7419 16 SB Bcl-2 DRB1_0101 208 PLFDFSWLSLKTLLS  FSWLSLKTL 0.7389 17 SB Bcl-2 DRB1_0101 210 FDFSWLSLKTLLSLA  WLSLKTLLS 0.7403 17 SB Bcl-2 DRB1_0101 219 TLLSLALVGACITLG  LLSLALVGA 0.7270 19 SB Bcl-2 DRB1_0101 220 LLSLALVGACITLGA  LVGACITLG 0.7299 19 SB Bcl-2 DRB1_0101 223 LALVGACITLGAYLG  LVGACITLG 0.7079 24 SB Bcl-2 DRB1_0101 221 LSLALVGACITLGAY  LVGACITLG 0.7021 25 SB Bcl-2 DRB1_0101 222 SLALVGACITLGAYL  LVGACITLG 0.7016 25 SB Bcl-2 DRB1_0101 106 RRYRRDFAEMSSQLH  YRRDFAEMS 0.6774 33 SB Bcl-2 DRB1_0101 72 LQTPAAPGAAAGPAL  LQTPAAPGA 0.6778 33 SB Bcl-2 DRB1_0101 71 PLQTPAAPGAAAGPA  LQTPAAPGA 0.6750 34 SB Bcl-2 DRB1_0101 108 YRRDFAEMSSQLHLT  FAEMSSQLH 0.6686 36 SB Bcl-2 DRB1_0101 107 RYRRDFAEMSSQLHL  FAEMSSQLH 0.6670 37 SB Bcl-2 DRB1_0101 218 KTLLSLALVGACITL  LLSLALVGA 0.6642 38 SB Bcl-2 DRB1_0101 109 RRDFAEMSSQLHLTP  FAEMSSQLH 0.6615 39 SB Bcl-2 DRB1_0101 110 RDFAEMSSQLHLTPF  FAEMSSQLH 0.6572 41 SB Bcl-2 DRB1_0101 31 DAGDVGAAPPGAAPA  VGAAPPGAA 0.6561 41 SB Bcl-2 DRB1_0101 32 AGDVGAAPPGAAPAP  VGAAPPGAA 0.6565 41 SB Bcl-2 DRB1_0101 29 EWDAGDVGAAPPGAA  DVGAAPPGA 0.6512 44 SB Bcl-2 DRB1_0101 30 WDAGDVGAAPPGAAP  VGAAPPGAA 0.6504 44 SB Bcl-2 DRB1_0101 33 GDVGAAPPGAAPAPG  VGAAPPGAA 0.6438 47 SB Bcl-2 DRB1_0101 207 RPLFDFSWLSLKTLL  FSWLSLKTL 0.6332 53 WB Bcl-2 DRB1_0101 224 ALVGACITLGAYLGH  LVGACITLG 0.6316 54 WB Bcl-2 DRB1_0101 206 MRPLFDFSWLSLKTL  DFSWLSLKT 0.6303 55 WB Bcl-2 DRB1_0101 225 LVGACITLGAYLGHK  LVGACITLG 0.6212 60 WB Bcl-2 DRB1_0101 13 EIVMKYIHYKLSQRG  MKYIHYKLS 0.6124 66 WB Bcl-2 DRB1_0101 14 IVMKYIHYKLSQRGY  IHYKLSQRG 0.6114 67 WB Bcl-2 DRB1_0101 15 VMKYIHYKLSQRGYE  IHYKLSQRG 0.6087 69 WB Bcl-2 DRB1_0101 16 MKYIHYKLSQRGYEW  IHYKLSQRG 0.6059 71 WB Bcl-2 DRB1_0101 17 KYIHYKLSQRGYEWD  IHYKLSQRG 0.6042 72 WB Bcl-2 DRB1_0101 164 REMSPLVDNIALWMT  LVDNIALWM 0.5967 79 WB Bcl-2 DRB1_0101 165 EMSPLVDNIALWMTE  VDNIALWMT 0.5914 83 WB Bcl-2 DRB1_0101 167 SPLVDNIALWMTEYL  VDNIALWMT 0.5912 83 WB Bcl-2 DRB1_0101 166 MSPLVDNIALWMTEY  VDNIALWMT 0.5908 84 WB Bcl-2 DRB1_0101 63 RDPVARTSPLQTPAA  VARTSPLQT 0.5908 84 WB Bcl-2 DRB1_0101 64 DPVARTSPLQTPAAP  VARTSPLQT 0.5876 87 WB Bcl-2 DRB1_0101 168 PLVDNIALWMTEYLN  VDNIALWMT 0.5794 95 WB Bcl-2 DRB1_0101 196 DAFVELYGPSMRPLF  FVELYGPSM 0.5684 107 WB Bcl-2 DRB1_0101 34 DVGAAPPGAAPAPGI  VGAAPPGAA 0.5672 108 WB Bcl-2 DRB1_0101 62 SRDPVARTSPLQTPA  VARTSPLQT 0.5669 108 WB Bcl-2 DRB1_0101 195 WDAFVELYGPSMRPL  FVELYGPSM 0.5666 109 WB Bcl-2 DRB1_0101 61 ASRDPVARTSPLQTP  VARTSPLQT 0.5637 112 WB Bcl-2 DRB1_0101 86 LSPVPPVVHLTLRQA  LSPVPPVVH 0.5639 112 WB Bcl-2 DRB1_0101 111 DFAEMSSQLHLTPFT  FAEMSSQLH 0.5615 115 WB Bcl-2 DRB1_0101 89 VPPVVHLTLRQAGDD  VVHLTLRQA 0.5593 118 WB Bcl-2 DRB1_0101 87 SPVPPVVHLTLRQAG  VVHLTLRQA 0.5579 119 WB Bcl-2 DRB1_0101 88 PVPPVVHLTLRQAGD  VVHLTLRQA 0.5581 119 WB Bcl-2 DRB1_0101 112 FAEMSSQLHLTPFTA  FAEMSSQLH 0.5577 120 WB Bcl-2 DRB1_0101 35 VGAAPPGAAPAPGIF  VGAAPPGAA 0.5569 121 WB Bcl-2 DRB1_0101 90 PPVVHLTLRQAGDDF  VVHLTLRQA 0.5563 122 WB Bcl-2 DRB1_0101 80 AAAGPALSPVPPVVH  AAAGPALSP 0.5545 124 WB Bcl-2 DRB1_0101 160 ESVNREMSPLVDNIA  VNREMSPLV 0.5523 127 WB Bcl-2 DRB1_0101 60 AASRDPVARTSPLQT  SRDPVARTS 0.5524 127 WB Bcl-2 DRB1_0101 117 SQLHLTPFTARGRFA  LTPFTARGR 0.5480 133 WB Bcl-2 DRB1_0101 115 MSSQLHLTPFTARGR  LHLTPFTAR 0.5456 137 WB Bcl-2 DRB1_0101 116 SSQLHLTPFTARGRF  LTPFTARGR 0.5418 142 WB Bcl-2 DRB1_0101 81 AAGPALSPVPPVVHL  LSPVPPVVH 0.5390 147 WB Bcl-2 DRB1_0101 118 QLHLTPFTARGRFAT  LTPFTARGR 0.5379 148 WB Bcl-2 DRB1_0101 197 AFVELYGPSMRPLFD  LYGPSMRPL 0.5381 148 WB Bcl-2 DRB1_0101 156 VMCVESVNREMSPLV  VMCVESVNR 0.5366 151 WB Bcl-2 DRB1_0101 158 CVESVNREMSPLVDN  VNREMSPLV 0.5360 151 WB Bcl-2 DRB1_0101 159 VESVNREMSPLVDNI  VNREMSPLV 0.5364 151 WB Bcl-2 DRB1_0101 198 FVELYGPSMRPLFDF  LYGPSMRPL 0.5345 154 WB Bcl-2 DRB1_0101 157 MCVESVNREMSPLVD  VNREMSPLV 0.5315 159 WB Bcl-2 DRB1_0101 119 LHLTPFTARGRFATV  LTPFTARGR 0.5307 160 WB Bcl-2 DRB1_0101 82 AGPALSPVPPVVHLT  LSPVPPVVH 0.5312 160 WB Bcl-2 DRB1_0101 83 GPALSPVPPVVHLTL  LSPVPPVVH 0.5307 160 WB Bcl-2 DRB1_0101 148 VAFFEFGGVMCVESV  FEFGGVMCV 0.5291 163 WB Bcl-2 DRB1_0101 149 AFFEFGGVMCVESVN  FEFGGVMCV 0.5288 164 WB Bcl-2 DRB1_0101 46 PGIFSSQPGHTPHPA  FSSQPGHTP 0.5270 167 WB Bcl-2 DRB1_0101 170 VDNIALWMTEYLNRH  VDNIALWMT 0.5265 168 WB Bcl-2 DRB1_0101 43 APAPGIFSSQPGHTP  IFSSQPGHT 0.5223 176 WB Bcl-2 DRB1_0101 84 PALSPVPPVVHLTLR  LSPVPPVVH 0.5195 181 WB Bcl-2 DRB1_0101 147 IVAFFEFGGVMCVES  FEFGGVMCV 0.5190 182 WB Bcl-2 DRB1_0101 65 PVARTSPLQTPAAPG  VARTSPLQT 0.5190 182 WB Bcl-2 DRB1_0101 45 APGIFSSQPGHTPHP  FSSQPGHTP 0.5186 183 WB Bcl-2 DRB1_0101 120 HLTPFTARGRFATVV  LTPFTARGR 0.5178 184 WB Bcl-2 DRB1_0101 121 LTPFTARGRFATVVE  ARGRFATVV 0.5182 184 WB Bcl-2 DRB1_0101 136 ELFRDGVNWGRIVAF  FRDGVNWGR 0.5154 189 WB Bcl-2 DRB1_0101 44 PAPGIFSSQPGHTPH  FSSQPGHTP 0.5142 192 WB Bcl-2 DRB1_0101 138 FRDGVNWGRIVAFFE  VNWGRIVAF 0.5122 196 WB Bcl-2 DRB1_0101 169 LVDNIALWMTEYLNR  VDNIALWMT 0.5062 209 WB Bcl-2 DRB1_0101 18 YIHYKLSQRGYEWDA  IHYKLSQRG 0.5057 210 WB Bcl-2 DRB1_0101 137 LFRDGVNWGRIVAFF  VNWGRIVAF 0.5023 218 WB Bcl-2 DRB1_0101 19 IHYKLSQRGYEWDAG  IHYKLSQRG 0.5022 218 WB Bcl-2 DRB1_0101 47 GIFSSQPGHTPHPAA  FSSQPGHTP 0.5023 218 WB Bcl-2 DRB1_0101 76 AAPGAAAGPALSPVP  AAAGPALSP 0.5005 222 WB Bcl-2 DRB1_0101 139 RDGVNWGRIVAFFEF  VNWGRIVAF 0.4998 224 WB Bcl-2 DRB1_0101 74 TPAAPGAAAGPALSP  GAAAGPALS 0.4991 226 WB Bcl-2 DRB1_0101 194 GWDAFVELYGPSMRP  FVELYGPSM 0.4987 227 WB Bcl-2 DRB1_0101 75 PAAPGAAAGPALSPV  AAAGPALSP 0.4981 228 WB Bcl-2 DRB1_0101 77 APGAAAGPALSPVPP  AAAGPALSP 0.4980 229 WB Bcl-2 DRB1_0101 140 DGVNWGRIVAFFEFG  VNWGRIVAF 0.4959 234 WB Bcl-2 DRB1_0101 105 SRRYRRDFAEMSSQL  YRRDFAEMS 0.4945 237 WB Bcl-2 DRB1_0101 91 PVVHLTLRQAGDDFS  VVHLTLRQA 0.4935 240 WB Bcl-2 DRB1_0101 199 VELYGPSMRPLFDFS  LYGPSMRPL 0.4895 251 WB Bcl-2 DRB1_0101 92 VVHLTLRQAGDDFSR  VVHLTLRQA 0.4870 257 WB Bcl-2 DRB1_0101 104 FSRRYRRDFAEMSSQ  YRRDFAEMS 0.4851 263 WB Bcl-2 DRB1_0101 103 DFSRRYRRDFAEMSS  YRRDFAEMS 0.4834 268 WB Bcl-2 DRB1_0101 102 DDFSRRYRRDFAEMS  RYRRDFAEM 0.4800 278 WB Bcl-2 DRB1_0101 145 GRIVAFFEFGGVMCV  FFEFGGVMC 0.4796 279 WB Bcl-2 DRB1_0101 146 RIVAFFEFGGVMCVE  FEFGGVMCV 0.4791 280 WB Bcl-2 DRB1_0101 78 PGAAAGPALSPVPPV  AAAGPALSP 0.4771 286 WB Bcl-2 DRB1_0101 161 SVNREMSPLVDNIAL  VNREMSPLV 0.4763 289 WB Bcl-2 DRB1_0101 150 FFEFGGVMCVESVNR  FEFGGVMCV 0.4737 297 WB Bcl-2 DRB1_0101 162 VNREMSPLVDNIALW  VNREMSPLV 0.4734 298 WB Bcl-2 DRB1_0101 151 FEFGGVMCVESVNRE  FEFGGVMCV 0.4731 299 WB Bcl-2 DRB1_0101 114 EMSSQLHLTPFTARG  LHLTPFTAR 0.4711 306 WB Bcl-2 DRB1_0101 122 TPFTARGRFATVVEE  ARGRFATVV 0.4638 331 WB Bcl-2 DRB1_0101 73 QTPAAPGAAAGPALS  APGAAAGPA 0.4635 332 WB Bcl-2 DRB1_0101 49 FSSQPGHTPHPAASR  FSSQPGHTP 0.4615 339 WB Bcl-2 DRB1_0101 48 IFSSQPGHTPHPAAS  FSSQPGHTP 0.4531 371 WB Bcl-2 DRB1_0101 36 GAAPPGAAPAPGIFS  PGAAPAPGI 0.4518 376 WB Bcl-2 DRB1_0101 123 PFTARGRFATVVEEL  ARGRFATVV 0.4516 377 WB Bcl-2 DRB1_0101 124 FTARGRFATVVEELF  ARGRFATVV 0.4490 388 WB Bcl-2 DRB1_0101 174 ALWMTEYLNRHLHTW  WMTEYLNRH 0.4444 408 WB Bcl-2 DRB1_0101 85 ALSPVPPVVHLTLRQ  LSPVPPVVH 0.4436 411 WB Bcl-2 DRB1_0101 113 AEMSSQLHLTPFTAR  SQLHLTPFT 0.4430 414 WB Bcl-2 DRB1_0101 171 DNIALWMTEYLNRHL  WMTEYLNRH 0.4414 421 WB Bcl-2 DRB1_0101 193 GGWDAFVELYGPSMR  FVELYGPSM 0.4396 430 WB Bcl-2 DRB1_0101 200 ELYGPSMRPLFDFSW  LYGPSMRPL 0.4395 430 WB Bcl-2 DRB1_0101 37 AAPPGAAPAPGIFSS  AAPAPGIFS 0.4393 431 WB Bcl-2 DRB1_0101 79 GAAAGPALSPVPPVV  AAAGPALSP 0.4394 431 WB Bcl-2 DRB1_0101 172 NIALWMTEYLNRHLH  WMTEYLNRH 0.4279 488 WB Bcl-2 DRB1_0101 28 YEWDAGDVGAAPPGA  WDAGDVGAA 0.4274 490 WB Bcl-2 DRB1_0101 42 AAPAPGIFSSQPGHT  AAPAPGIFS 0.4268 494 WB Bcl-2 DRB1_0101 163 NREMSPLVDNIALWM  MSPLVDNIA 0.4266 495 WB Bcl-2 DRB1_0401 208 PLFDFSWLSLKTLLS  DFSWLSLKT 0.5448 138 WB Bcl-2 DRB1_0401 211 DFSWLSLKTLLSLAL  WLSLKTLLS 0.5436 139 WB Bcl-2 DRB1_0401 212 FSWLSLKTLLSLALV  WLSLKTLLS 0.5395 146 WB Bcl-2 DRB1_0401 209 LFDFSWLSLKTLLSL  WLSLKTLLS 0.5358 152 WB Bcl-2 DRB1_0401 210 FDFSWLSLKTLLSLA  WLSLKTLLS 0.5305 161 WB Bcl-2 DRB1_0401 156 VMCVESVNREMSPLV  MCVESVNRE 0.4924 243 WB Bcl-2 DRB1_0401 158 CVESVNREMSPLVDN  VNREMSPLV 0.4915 245 WB Bcl-2 DRB1_0401 157 MCVESVNREMSPLVD  VNREMSPLV 0.4907 247 WB Bcl-2 DRB1_0401 160 ESVNREMSPLVDNIA  VNREMSPLV 0.4909 247 WB Bcl-2 DRB1_0401 159 VESVNREMSPLVDNI  VNREMSPLV 0.4870 257 WB Bcl-2 DRB1_0401 214 WLSLKTLLSLALVGA  WLSLKTLLS 0.4662 322 WB Bcl-2 DRB1_0401 213 SWLSLKTLLSLALVG  WLSLKTLLS 0.4661 323 WB Bcl-2 DRB1_0401 106 RRYRRDFAEMSSQLH  YRRDFAEMS 0.4563 359 WB Bcl-2 DRB1_0401 170 VDNIALWMTEYLNRH  NIALWMTEY 0.4319 467 WB Bcl-2 DRB1_0404 174 ALWMTEYLNRHLHTW  WMTEYLNRH 0.5813 93 WB Bcl-2 DRB1_0404 170 VDNIALWMTEYLNRH  IALWMTEYL 0.5418 142 WB Bcl-2 DRB1_0404 171 DNIALWMTEYLNRHL  WMTEYLNRH 0.5422 142 WB Bcl-2 DRB1_0404 172 NIALWMTEYLNRHLH  WMTEYLNRH 0.5371 150 WB Bcl-2 DRB1_0404 173 IALWMTEYLNRHLHT  WMTEYLNRH 0.5341 155 WB Bcl-2 DRB1_0404 175 LWMTEYLNRHLHTWI  WMTEYLNRH 0.5171 186 WB Bcl-2 DRB1_0404 115 MSSQLHLTPFTARGR  HLTPFTARG 0.5121 196 WB Bcl-2 DRB1_0404 114 EMSSQLHLTPFTARG  LHLTPFTAR 0.5118 197 WB Bcl-2 DRB1_0404 176 WMTEYLNRHLHTWIQ  WMTEYLNRH 0.5110 199 WB Bcl-2 DRB1_0404 116 SSQLHLTPFTARGRF  HLTPFTARG 0.5043 213 WB Bcl-2 DRB1_0404 117 SQLHLTPFTARGRFA  HLTPFTARG 0.5004 223 WB Bcl-2 DRB1_0404 118 QLHLTPFTARGRFAT  HLTPFTARG 0.4918 244 WB Bcl-2 DRB1_0404 45 APGIFSSQPGHTPHP  FSSQPGHTP 0.4688 313 WB Bcl-2 DRB1_0404 46 PGIFSSQPGHTPHPA  FSSQPGHTP 0.4665 321 WB Bcl-2 DRB1_0404 47 GIFSSQPGHTPHPAA  SQPGHTPHP 0.4485 390 WB Bcl-2 DRB1_0404 109 RRDFAEMSSQLHLTP  FAEMSSQLH 0.4422 418 WB Bcl-2 DRB1_0404 210 FDFSWLSLKTLLSLA  WLSLKTLLS 0.4405 426 WB Bcl-2 DRB1_0404 110 RDFAEMSSQLHLTPF  FAEMSSQLH 0.4393 431 WB Bcl-2 DRB1_0404 211 DFSWLSLKTLLSLAL  WLSLKTLLS 0.4316 469 WB Bcl-2 DRB1_0404 212 FSWLSLKTLLSLALV  WLSLKTLLS 0.4313 470 WB Bcl-2 DRB1_0405 208 PLFDFSWLSLKTLLS  FSWLSLKTL 0.6517 43 SB Bcl-2 DRB1_0405 209 LFDFSWLSLKTLLSL  WLSLKTLLS 0.6415 48 SB Bcl-2 DRB1_0405 210 FDFSWLSLKTLLSLA  WLSLKTLLS 0.6398 49 SB Bcl-2 DRB1_0405 211 DFSWLSLKTLLSLAL  WLSLKTLLS 0.6392 50 WB Bcl-2 DRB1_0405 212 FSWLSLKTLLSLALV  WLSLKTLLS 0.6381 50 WB Bcl-2 DRB1_0405 213 SWLSLKTLLSLALVG  WLSLKTLLS 0.5584 119 WB Bcl-2 DRB1_0405 214 WLSLKTLLSLALVGA  WLSLKTLLS 0.5575 120 WB Bcl-2 DRB1_0405 160 ESVNREMSPLVDNIA  NREMSPLVD 0.5021 219 WB Bcl-2 DRB1_0405 158 CVESVNREMSPLVDN  NREMSPLVD 0.4974 230 WB Bcl-2 DRB1_0405 159 VESVNREMSPLVDNI  NREMSPLVD 0.4930 241 WB Bcl-2 DRB1_0405 170 VDNIALWMTEYLNRH  IALWMTEYL 0.4903 248 WB Bcl-2 DRB1_0405 168 PLVDNIALWMTEYLN  IALWMTEYL 0.4841 266 WB Bcl-2 DRB1_0405 171 DNIALWMTEYLNRHL  IALWMTEYL 0.4841 266 WB Bcl-2 DRB1_0405 169 LVDNIALWMTEYLNR  IALWMTEYL 0.4812 274 WB Bcl-2 DRB1_0405 157 MCVESVNREMSPLVD  VNREMSPLV 0.4756 291 WB Bcl-2 DRB1_0405 167 SPLVDNIALWMTEYL  NIALWMTEY 0.4744 295 WB Bcl-2 DRB1_0405 161 SVNREMSPLVDNIAL  NREMSPLVD 0.4718 303 WB Bcl-2 DRB1_0405 106 RRYRRDFAEMSSQLH  YRRDFAEMS 0.4486 390 WB Bcl-2 DRB1_0405 162 VNREMSPLVDNIALW  NREMSPLVD 0.4294 480 WB Bcl-2 DRB1_0701 83 GPALSPVPPVVHLTL  LSPVPPVVH 0.5316 159 WB Bcl-2 DRB1_0701 82 AGPALSPVPPVVHLT  LSPVPPVVH 0.5286 164 WB Bcl-2 DRB1_0701 81 AAGPALSPVPPVVHL  LSPVPPVVH 0.5256 169 WB Bcl-2 DRB1_0701 84 PALSPVPPVVHLTLR  LSPVPPVVH 0.5210 178 WB Bcl-2 DRB1_0701 80 AAAGPALSPVPPVVH  ALSPVPPVV 0.5179 184 WB Bcl-2 DRB1_0701 85 ALSPVPPVVHLTLRQ  LSPVPPVVH 0.4370 442 WB Bcl-2 DRB1_0701 86 LSPVPPVVHLTLRQA  LSPVPPVVH 0.4291 482 WB Bcl-2 DRB1_0901 196 DAFVELYGPSMRPLF  VELYGPSMR 0.4599 345 WB Bcl-2 DRB1_0901 197 AFVELYGPSMRPLFD  YGPSMRPLF 0.4582 352 WB Bcl-2 DRB1_0901 198 FVELYGPSMRPLFDF  YGPSMRPLF 0.4429 415 WB Bcl-2 DRB1_0901 199 VELYGPSMRPLFDFS  YGPSMRPLF 0.4428 415 WB Bcl-2 DRB1_1302 212 FSWLSLKTLLSLALV  WLSLKTLLS 0.5351 153 WB Bcl-2 DRB1_1302 211 DFSWLSLKTLLSLAL  WLSLKTLLS 0.5323 158 WB Bcl-2 DRB1_1302 209 LFDFSWLSLKTLLSL  WLSLKTLLS 0.4963 233 WB Bcl-2 DRB1_1302 210 FDFSWLSLKTLLSLA  WLSLKTLLS 0.4951 236 WB Bcl-2 DRB1_1302 208 PLFDFSWLSLKTLLS  FSWLSLKTL 0.4783 283 WB Bcl-2 DRB1_1302 213 SWLSLKTLLSLALVG  WLSLKTLLS 0.4770 287 WB Bcl-2 DRB1_1302 214 WLSLKTLLSLALVGA  WLSLKTLLS 0.4769 287 WB Bcl-2 DRB1_1302 196 DAFVELYGPSMRPLF  VELYGPSMR 0.4640 330 WB Bcl-2 DRB1_1302 197 AFVELYGPSMRPLFD  VELYGPSMR 0.4607 342 WB Bcl-2 DRB1_1302 167 SPLVDNIALWMTEYL  VDNIALWMT 0.4494 387 WB Bcl-2 DRB1_1302 168 PLVDNIALWMTEYLN  VDNIALWMT 0.4385 435 WB Bcl-2 DRB1_1501 13 EIVMKYIHYKLSQRG  YIHYKLSQR 0.6338 53 WB Bcl-2 DRB1_1501 14 IVMKYIHYKLSQRGY  YIHYKLSQR 0.6318 54 WB Bcl-2 DRB1_1501 15 VMKYIHYKLSQRGYE  YIHYKLSQR 0.6170 63 WB Bcl-2 DRB1_1501 16 MKYIHYKLSQRGYEW  YIHYKLSQR 0.6121 66 WB Bcl-2 DRB1_1501 12 REIVMKYIHYKLSQR  IVMKYIHYK 0.6057 71 WB Bcl-2 DRB1_1501 17 KYIHYKLSQRGYEWD  YIHYKLSQR 0.5372 150 WB Bcl-2 DRB1_1501 115 MSSQLHLTPFTARGR  LHLTPFTAR 0.5174 185 WB Bcl-2 DRB1_1501 116 SSQLHLTPFTARGRF  LHLTPFTAR 0.5162 188 WB Bcl-2 DRB1_1501 18 YIHYKLSQRGYEWDA  YIHYKLSQR 0.5136 193 WB Bcl-2 DRB1_1501 117 SQLHLTPFTARGRFA  LHLTPFTAR 0.5054 211 WB Bcl-2 DRB1_1501 119 LHLTPFTARGRFATV  LTPFTARGR 0.4756 291 WB Bcl-2 DRB1_1501 135 EELFRDGVNWGRIVA  LFRDGVNWG 0.4694 311 WB Bcl-2 DRB1_1501 212 FSWLSLKTLLSLALV  WLSLKTLLS 0.4694 312 WB Bcl-2 DRB1_1501 211 DFSWLSLKTLLSLAL  WLSLKTLLS 0.4655 325 WB Bcl-2 DRB1_1501 118 QLHLTPFTARGRFAT  LHLTPFTAR 0.4592 348 WB Bcl-2 DRB1_1501 87 SPVPPVVHLTLRQAG  VVHLTLRQA 0.4553 363 WB Bcl-2 DRB1_1501 88 PVPPVVHLTLRQAGD  VVHLTLRQA 0.4528 373 WB Bcl-2 DRB1_1501 214 WLSLKTLLSLALVGA  LKTLLSLAL 0.4517 377 WB Bcl-2 DRB1_1501 209 LFDFSWLSLKTLLSL  WLSLKTLLS 0.4495 386 WB Bcl-2 DRB1_1501 156 VMCVESVNREMSPLV  VMCVESVNR 0.4490 388 WB Bcl-2 DRB1_1501 193 GGWDAFVELYGPSMR  FVELYGPSM 0.4489 389 WB Bcl-2 DRB1_1501 195 WDAFVELYGPSMRPL  VELYGPSMR 0.4483 391 WB Bcl-2 DRB1_1501 196 DAFVELYGPSMRPLF  FVELYGPSM 0.4482 392 WB Bcl-2 DRB1_1501 132 TVVEELFRDGVNWGR  LFRDGVNWG 0.4470 397 WB Bcl-2 DRB1_1501 133 VVEELFRDGVNWGRI  LFRDGVNWG 0.4467 398 WB Bcl-2 DRB1_1501 194 GWDAFVELYGPSMRP  VELYGPSMR 0.4467 398 WB Bcl-2 DRB1_1501 174 ALWMTEYLNRHLHTW  WMTEYLNRH 0.4463 400 WB Bcl-2 DRB1_1501 208 PLFDFSWLSLKTLLS  LFDFSWLSL 0.4459 401 WB Bcl-2 DRB1_1501 172 NIALWMTEYLNRHLH  WMTEYLNRH 0.4448 406 WB Bcl-2 DRB1_1501 173 IALWMTEYLNRHLHT  WMTEYLNRH 0.4448 407 WB Bcl-2 DRB1_1501 134 VEELFRDGVNWGRIV  LFRDGVNWG 0.4431 414 WB Bcl-2 DRB1_1501 171 DNIALWMTEYLNRHL  WMTEYLNRH 0.4431 414 WB Bcl-2 DRB1_1501 89 VPPVVHLTLRQAGDD  VVHLTLRQA 0.4422 418 WB Bcl-2 DRB1_1501 210 FDFSWLSLKTLLSLA  WLSLKTLLS 0.4399 429 WB Bcl-2 DRB1_1501 136 ELFRDGVNWGRIVAF  LFRDGVNWG 0.4390 433 WB Bcl-2 DRB1_1501 86 LSPVPPVVHLTLRQA  PPVVHLTLR 0.4378 438 WB Bcl-2 DRB1_1501 213 SWLSLKTLLSLALVG  LKTLLSLAL 0.4330 461 WB Bcl-2 DRB1_1501 90 PPVVHLTLRQAGDDF  VVHLTLRQA 0.4313 470 WB Bcl-2 DRB4_0101 196 DAFVELYGPSMRPLF  VELYGPSMR 0.5364 151 WB Bcl-2 DRB4_0101 197 AFVELYGPSMRPLFD  VELYGPSMR 0.5361 151 WB Bcl-2 DRB4_0101 195 WDAFVELYGPSMRPL  VELYGPSMR 0.5323 158 WB Bcl-2 DRB4_0101 193 GGWDAFVELYGPSMR  FVELYGPSM 0.4796 279 WB Bcl-2 DRB4_0101 194 GWDAFVELYGPSMRP  VELYGPSMR 0.4785 282 WB Bcl-2 DRB4_0101 198 FVELYGPSMRPLFDF  VELYGPSMR 0.4761 289 WB Bcl-2 DRB4_0101 199 VELYGPSMRPLFDFS  VELYGPSMR 0.4763 289 WB Bcl-2 DRB4_0101 81 AAGPALSPVPPVVHL  LSPVPPVVH 0.4638 331 WB Bcl-2 DRB4_0101 80 AAAGPALSPVPPVVH  ALSPVPPVV 0.4614 339 WB Bcl-2 DRB4_0101 170 VDNIALWMTEYLNRH  IALWMTEYL 0.4593 347 WB Bcl-2 DRB4_0101 83 GPALSPVPPVVHLTL  LSPVPPVVH 0.4589 349 WB Bcl-2 DRB4_0101 82 AGPALSPVPPVVHLT  LSPVPPVVH 0.4574 354 WB Bcl-2 DRB4_0101 84 PALSPVPPVVHLTLR  LSPVPPVVH 0.4565 358 WB Bcl-2 DRB4_0101 171 DNIALWMTEYLNRHL  WMTEYLNRH 0.4552 363 WB Bcl-2 DRB4_0101 172 NIALWMTEYLNRHLH  LWMTEYLNR 0.4326 464 WB Bcl-2 DRB4_0101 173 IALWMTEYLNRHLHT  WMTEYLNRH 0.4273 491 WB Bcl-2 DRB5_0101 16 MKYIHYKLSQRGYEW  YIHYKLSQR 0.4394 431 WB Bcl-2 DRB5_0101 15 VMKYIHYKLSQRGYE  YIHYKLSQR 0.4386 435 WB Bcl-2 SEQ ID NOS: 46594-47133

Preferred fragments of Survivin capable of interacting with one or more MHC class 1 molecules are listed in table F.

TABLE F Prediction of cancer antigen Survivin specific MHC class 1 peptide sequences. Prediction of 8-, 9-, 10-, 11-mers using the program displayed in FIG. 2. 8 mers: MGAPTLPP; GAPTLPPA; APTLPPAW; PTLPPAWQ; TLPPAWQP; LPPAWQPF; PPAWQPFL; PAWQPFLK; AWQPFLKD; WQPFLKDH; QPFLKDHR; PFLKDHRI; FLKDHRIS; LKDHRIST; KDHRISTF; DHRISTFK; HRISTFKN; RISTFKNW; ISTFKNWP; STFKNWPF; TFKNWPFL; FKNWPFLE; KNWPFLEG; NWPFLEGC; WPFLEGCA; PFLEGCAC; FLEGCACT; LEGCACTP; EGCACTPE; GCACTPER; CACTPERM; ACTPERMA; CTPERMAE; TPERMAEA; PERMAEAG; ERMAEAGF; RMAEAGFI; MAEAGFIH; AEAGFIHC; EAGFIHCP; AGFIHCPT; GFIHCPTE; FIHCPTEN; IHCPTENE; HCPTENEP; CPTENEPD; PTENEPDL; TENEPDLA; ENEPDLAQ; NEPDLAQC; EPDLAQCF; PDLAQCFF; DLAQCFFC; LAQCFFCF; AQCFFCFK; QCFFCFKE; CFFCFKEL; FFCFKELE; FCFKELEG; CFKELEGW; FKELEGWE; KELEGWEP; ELEGWEPD; LEGWEPDD; EGWEPDDD; GWEPDDDP; WEPDDDPI; EPDDDPIE; PDDDPIEE; DDDPIEEH; DDPIEEHK; DPIEEHKK; PIEEHKKH; IEEHKKHS; EEHKKHSS; EHKKHSSG; HKKHSSGC; KKHSSGCA; KHSSGCAF; HSSGCAFL; SSGCAFLS; SGCAFLSV; GCAFLSVK; CAFLSVKK; AFLSVKKQ; FLSVKKQF; LSVKKQFE; SVKKQFEE; VKKQFEEL; KKQFEELT; KQFEELTL; QFEELTLG; FEELTLGE; EELTLGEF; ELTLGEFL; LTLGEFLK; TLGEFLKL; LGEFLKLD; GEFLKLDR; EFLKLDRE; FLKLDRER; LKLDRERA; KLDRERAK; LDRERAKN; DRERAKNK; RERAKNKI; ERAKNKIA; RAKNKIAK; AKNKIAKE; KNKIAKET; NKIAKETN; KIAKETNN; IAKETNNK; AKETNNKK; KETNNKKK; ETNNKKKE; TNNKKKEF; NNKKKEFE; NKKKEFEE; KKKEFEET; KKEFEETA; KEFEETAK; EFEETAKK; FEETAKKV; EETAKKVR; ETAKKVRR; TAKKVRRA; AKKVRRAI; KKVRRAIE; KVRRAIEQ; VRRAIEQL; RRAIEQLA; RAIEQLAA; AIEQLAAM; IEQLAAMD; EQLAAMD□ 9 mers: MGAPTLPPA; GAPTLPPAW; APTLPPAWQ; PTLPPAWQP; TLPPAWQPF; LPPAWQPFL; PPAWQPFLK; PAWQPFLKD; AWQPFLKDH; WQPFLKDHR; QPFLKDHRI; PFLKDHRIS; FLKDHRIST; LKDHRISTF; KDHRISTFK; DHRISTFKN; HRISTFKNW; RISTFKNWP; ISTFKNWPF; STFKNWPFL; TFKNWPFLE; FKNWPFLEG; KNWPFLEGC; NWPFLEGCA; WPFLEGCAC; PFLEGCACT; FLEGCACTP; LEGCACTPE; EGCACTPER; GCACTPERM; CACTPERMA; ACTPERMAE; CTPERMAEA; TPERMAEAG; PERMAEAGF; ERMAEAGFI; RMAEAGFIH; MAEAGFIHC; AEAGFIHCP; EAGFIHCPT; AGFIHCPTE; GFIHCPTEN; FIHCPTENE; IHCPTENEP; HCPTENEPD; CPTENEPDL; PTENEPDLA; TENEPDLAQ; ENEPDLAQC; NEPDLAQCF; EPDLAQCFF; PDLAQCFFC; DLAQCFFCF; LAQCFFCFK; AQCFFCFKE; QCFFCFKEL; CFFCFKELE; FFCFKELEG; FCFKELEGW; CFKELEGWE; FKELEGWEP; KELEGWEPD; ELEGWEPDD; LEGWEPDDD; EGWEPDDDP; GWEPDDDPI; WEPDDDPIE; EPDDDPIEE; PDDDPIEEH; DDDPIEEHK; DDPIEEHKK; DPIEEHKKH; PIEEHKKHS; IEEHKKHSS; EEHKKHSSG; EHKKHSSGC; HKKHSSGCA; KKHSSGCAF; KHSSGCAFL; HSSGCAFLS; SSGCAFLSV; SGCAFLSVK; GCAFLSVKK; CAFLSVKKQ; AFLSVKKQF; FLSVKKQFE; LSVKKQFEE; SVKKQFEEL; VKKQFEELT; KKQFEELTL; KQFEELTLG; QFEELTLGE; FEELTLGEF; EELTLGEFL; ELTLGEFLK; LTLGEFLKL; TLGEFLKLD; LGEFLKLDR; GEFLKLDRE; EFLKLDRER; FLKLDRERA; LKLDRERAK; KLDRERAKN; LDRERAKNK; DRERAKNKI; RERAKNKIA; ERAKNKIAK; RAKNKIAKE; AKNKIAKET; KNKIAKETN; NKIAKETNN; KIAKETNNK; IAKETNNKK; AKETNNKKK; KETNNKKKE; ETNNKKKEF; TNNKKKEFE; NNKKKEFEE; NKKKEFEET; KKKEFEETA; KKEFEETAK; KEFEETAKK; EFEETAKKV; FEETAKKVR; EETAKKVRR; ETAKKVRRA; TAKKVRRAI; AKKVRRAIE; KKVRRAIEQ; KVRRAIEQL; VRRAIEQLA; RRAIEQLAA; RAIEQLAAM; AIEQLAAMD; □ 10 mers: MGAPTLPPAW; GAPTLPPAWQ; APTLPPAWQP; PTLPPAWQPF; TLPPAWQPFL; LPPAWQPFLK; PPAWQPFLKD; PAWQPFLKDH; AWQPFLKDHR; WQPFLKDHRI; QPFLKDHRIS; PFLKDHRIST; FLKDHRISTF; LKDHRISTFK; KDHRISTFKN; DHRISTFKNW; HRISTFKNWP; RISTFKNWPF; ISTFKNWPFL; STFKNWPFLE; TFKNWPFLEG; FKNWPFLEGC; KNWPFLEGCA; NWPFLEGCAC; WPFLEGCACT; PFLEGCACTP; FLEGCACTPE; LEGCACTPER; EGCACTPERM; GCACTPERMA; CACTPERMAE; ACTPERMAEA; CTPERMAEAG; TPERMAEAGF; PERMAEAGFI; ERMAEAGFIH; RMAEAGFIHC; MAEAGFIHCP; AEAGFIHCPT; EAGFIHCPTE; AGFIHCPTEN; GFIHCPTENE; FIHCPTENEP; IHCPTENEPD; HCPTENEPDL; CPTENEPDLA; PTENEPDLAQ; TENEPDLAQC; ENEPDLAQCF; NEPDLAQCFF; EPDLAQCFFC; PDLAQCFFCF; DLAQCFFCFK; LAQCFFCFKE; AQCFFCFKEL; QCFFCFKELE; CFFCFKELEG; FFCFKELEGW; FCFKELEGWE; CFKELEGWEP; FKELEGWEPD; KELEGWEPDD; ELEGWEPDDD; LEGWEPDDDP; EGWEPDDDPI; GWEPDDDPIE; WEPDDDPIEE; EPDDDPIEEH; PDDDPIEEHK; DDDPIEEHKK; DDPIEEHKKH; DPIEEHKKHS; PIEEHKKHSS; IEEHKKHSSG; EEHKKHSSGC; EHKKHSSGCA; HKKHSSGCAF; KKHSSGCAFL; KHSSGCAFLS; HSSGCAFLSV; SSGCAFLSVK; SGCAFLSVKK; GCAFLSVKKQ; CAFLSVKKQF; AFLSVKKQFE; FLSVKKQFEE; LSVKKQFEEL; SVKKQFEELT; VKKQFEELTL; KKQFEELTLG; KQFEELTLGE; QFEELTLGEF; FEELTLGEFL; EELTLGEFLK; ELTLGEFLKL; LTLGEFLKLD; TLGEFLKLDR; LGEFLKLDRE; GEFLKLDRER; EFLKLDRERA; FLKLDRERAK; LKLDRERAKN; KLDRERAKNK; LDRERAKNKI; DRERAKNKIA; RERAKNKIAK; ERAKNKIAKE; RAKNKIAKET; AKNKIAKETN; KNKIAKETNN; NKIAKETNNK; KIAKETNNKK; IAKETNNKKK; AKETNNKKKE; KETNNKKKEF; ETNNKKKEFE; TNNKKKEFEE; NNKKKEFEET; NKKKEFEETA; KKKEFEETAK; KKEFEETAKK; KEFEETAKKV; EFEETAKKVR; FEETAKKVRR; EETAKKVRRA; ETAKKVRRAI; TAKKVRRAIE; AKKVRRAIEQ; KKVRRAIEQL; KVRRAIEQLA; VRRAIEQLAA; RRAIEQLAAM; RAIEQLAAMD; 11 mers: MGAPTLPPAWQ; GAPTLPPAWQP; APTLPPAWQPF; PTLPPAWQPFL; TLPPAWQPFLK; LPPAWQPFLKD; PPAWQPFLKDH; PAWQPFLKDHR; AWQPFLKDHRI; WQPFLKDHRIS; QPFLKDHRIST; PFLKDHRISTF; FLKDHRISTFK; LKDHRISTFKN; KDHRISTFKNW; DHRISTFKNWP; HRISTFKNWPF; RISTFKNWPFL; ISTFKNWPFLE; STFKNWPFLEG; TFKNWPFLEGC; FKNWPFLEGCA; KNWPFLEGCAC; NWPFLEGCACT; WPFLEGCACTP; PFLEGCACTPE; FLEGCACTPER; LEGCACTPERM; EGCACTPERMA; GCACTPERMAE; CACTPERMAEA; ACTPERMAEAG; CTPERMAEAGF; TPERMAEAGFI; PERMAEAGFIH; ERMAEAGFIHC; RMAEAGFIHCP; MAEAGFIHCPT; AEAGFIHCPTE; EAGFIHCPTEN; AGFIHCPTENE; GFIHCPTENEP; FIHCPTENEPD; IHCPTENEPDL; HCPTENEPDLA; CPTENEPDLAQ; PTENEPDLAQC; TENEPDLAQCF; ENEPDLAQCFF; NEPDLAQCFFC; EPDLAQCFFCF; PDLAQCFFCFK; DLAQCFFCFKE; LAQCFFCFKEL; AQCFFCFKELE; QCFFCFKELEG; CFFCFKELEGW; FFCFKELEGWE; FCFKELEGWEP; CFKELEGWEPD; FKELEGWEPDD; KELEGWEPDDD; ELEGWEPDDDP; LEGWEPDDDPI; EGWEPDDDPIE; GWEPDDDPIEE; WEPDDDPIEEH; EPDDDPIEEHK; PDDDPIEEHKK; DDDPIEEHKKH; DDPIEEHKKHS; DPIEEHKKHSS; PIEEHKKHSSG; IEEHKKHSSGC; EEHKKHSSGCA; EHKKHSSGCAF; HKKHSSGCAFL; KKHSSGCAFLS; KHSSGCAFLSV; HSSGCAFLSVK; SSGCAFLSVKK; SGCAFLSVKKQ; GCAFLSVKKQF; CAFLSVKKQFE; AFLSVKKQFEE; FLSVKKQFEEL; LSVKKQFEELT; SVKKQFEELTL; VKKQFEELTLG; KKQFEELTLGE; KQFEELTLGEF; QFEELTLGEFL; FEELTLGEFLK; EELTLGEFLKL; ELTLGEFLKLD; LTLGEFLKLDR; TLGEFLKLDRE; LGEFLKLDRER; GEFLKLDRERA; EFLKLDRERAK; FLKLDRERAKN; LKLDRERAKNK; KLDRERAKNKI; LDRERAKNKIA; DRERAKNKIAK; RERAKNKIAKE; ERAKNKIAKET; RAKNKIAKETN; AKNKIAKETNN; KNKIAKETNNK; NKIAKETNNKK; KIAKETNNKKK; IAKETNNKKKE; AKETNNKKKEF; KETNNKKKEFE; ETNNKKKEFEE; TNNKKKEFEET; NNKKKEFEETA; NKKKEFEETAK; KKKEFEETAKK; KKEFEETAKKV; KEFEETAKKVR; EFEETAKKVRR; FEETAKKVRRA; EETAKKVRRAI; ETAKKVRRAIE; TAKKVRRAIEQ; AKKVRRAIEQL; KKVRRAIEQLA; KVRRAIEQLAA; VRRAIEQLAAM; RRAIEQLAAMD SEQ ID NOS: 47646-48180

Preferred fragments of Mcl-1 capable of interacting with one or more MHC class 2 molecules are listed in table G.

TABLE G Prediction of cancer antigen Mcl-1 specific MHC class 2 peptide sequences. Prediction of 13-, 14-, 15-, 16-mers using the program displayed in FIG. 2.; 13 mers: MFGLKRNAVIGLN; FGLKRNAVIGLNL; GLKRNAVIGLNLY; LKRNAVIGLNLYC; KRNAVIGLNLYCG; RNAVIGLNLYCGG; NAVIGLNLYCGGA; AVIGLNLYCGGAG; VIGLNLYCGGAGL; IGLNLYCGGAGLG; GLNLYCGGAGLGA; LNLYCGGAGLGAG; NLYCGGAGLGAGS; LYCGGAGLGAGSG; YCGGAGLGAGSGG; CGGAGLGAGSGGA; GGAGLGAGSGGAT; GAGLGAGSGGATR; AGLGAGSGGATRP; GLGAGSGGATRPG; LGAGSGGATRPGG; GAGSGGATRPGGR; AGSGGATRPGGRL; GSGGATRPGGRLL; SGGATRPGGRLLA; GGATRPGGRLLAT; GATRPGGRLLATE; ATRPGGRLLATEK; TRPGGRLLATEKE; RPGGRLLATEKEA; PGGRLLATEKEAS; GGRLLATEKEASA; GRLLATEKEASAR; RLLATEKEASARR; LLATEKEASARRE; LATEKEASARREI; ATEKEASARREIG; TEKEASARREIGG; EKEASARREIGGG; KEASARREIGGGE; EASARREIGGGEA; ASARREIGGGEAG; SARREIGGGEAGA; ARREIGGGEAGAV; RREIGGGEAGAVI; REIGGGEAGAVIG; EIGGGEAGAVIGG; IGGGEAGAVIGGS; GGGEAGAVIGGSA; GGEAGAVIGGSAG; GEAGAVIGGSAGA; EAGAVIGGSAGAS; AGAVIGGSAGASP; GAVIGGSAGASPP; AVIGGSAGASPPS; VIGGSAGASPPST; IGGSAGASPPSTL; GGSAGASPPSTLT; GSAGASPPSTLTP; SAGASPPSTLTPD; AGASPPSTLTPDS; GASPPSTLTPDSR; ASPPSTLTPDSRR; SPPSTLTPDSRRV; PPSTLTPDSRRVA; PSTLTPDSRRVAR; STLTPDSRRVARP; TLTPDSRRVARPP; LTPDSRRVARPPP; TPDSRRVARPPPI; PDSRRVARPPPIG; DSRRVARPPPIGA; SRRVARPPPIGAE; RRVARPPPIGAEV; RVARPPPIGAEVP; VARPPPIGAEVPD; ARPPPIGAEVPDV; RPPPIGAEVPDVT; PPPIGAEVPDVTA; PPIGAEVPDVTAT; PIGAEVPDVTATP; IGAEVPDVTATPA; GAEVPDVTATPAR; AEVPDVTATPARL; EVPDVTATPARLL; VPDVTATPARLLF; PDVTATPARLLFF; DVTATPARLLFFA; VTATPARLLFFAP; TATPARLLFFAPT; ATPARLLFFAPTR; TPARLLFFAPTRR; PARLLFFAPTRRA; ARLLFFAPTRRAA; RLLFFAPTRRAAP; LLFFAPTRRAAPL; LFFAPTRRAAPLE; FFAPTRRAAPLEE; FAPTRRAAPLEEM; APTRRAAPLEEME; PTRRAAPLEEMEA; TRRAAPLEEMEAP; RRAAPLEEMEAPA; RAAPLEEMEAPAA; AAPLEEMEAPAAD; APLEEMEAPAADA; PLEEMEAPAADAI; LEEMEAPAADAIM; EEMEAPAADAIMS; EMEAPAADAIMSP; MEAPAADAIMSPE; EAPAADAIMSPEE; APAADAIMSPEEE; PAADAIMSPEEEL; AADAIMSPEEELD; ADAIMSPEEELDG; DAIMSPEEELDGY; AIMSPEEELDGYE; IMSPEEELDGYEP; MSPEEELDGYEPE; SPEEELDGYEPEP; PEEELDGYEPEPL; EEELDGYEPEPLG; EELDGYEPEPLGK; ELDGYEPEPLGKR; LDGYEPEPLGKRP; DGYEPEPLGKRPA; GYEPEPLGKRPAV; YEPEPLGKRPAVL; EPEPLGKRPAVLP; PEPLGKRPAVLPL; EPLGKRPAVLPLL; PLGKRPAVLPLLE; LGKRPAVLPLLEL; GKRPAVLPLLELV; KRPAVLPLLELVG; RPAVLPLLELVGE; PAVLPLLELVGES; AVLPLLELVGESG; VLPLLELVGESGN; LPLLELVGESGNN; PLLELVGESGNNT; LLELVGESGNNTS; LELVGESGNNTST; ELVGESGNNTSTD; LVGESGNNTSTDG; VGESGNNTSTDGS; GESGNNTSTDGSL; ESGNNTSTDGSLP; SGNNTSTDGSLPS; GNNTSTDGSLPST; NNTSTDGSLPSTP; NTSTDGSLPSTPP; TSTDGSLPSTPPP; STDGSLPSTPPPA; TDGSLPSTPPPAE; DGSLPSTPPPAEE; GSLPSTPPPAEEE; SLPSTPPPAEEEE; LPSTPPPAEEEED; PSTPPPAEEEEDD; STPPPAEEEEDDL; TPPPAEEEEDDLY; PPPAEEEEDDLYR; PPAEEEEDDLYRQ; PAEEEEDDLYRQS; AEEEEDDLYRQSL; EEEEDDLYRQSLE; EEEDDLYRQSLEI; EEDDLYRQSLEII; EDDLYRQSLEIIS; DDLYRQSLEIISR; DLYRQSLEIISRY; LYRQSLEIISRYL; YRQSLEIISRYLR; RQSLEIISRYLRE; QSLEIISRYLREQ; SLEIISRYLREQA; LEIISRYLREQAT; EIISRYLREQATG; IISRYLREQATGA; ISRYLREQATGAK; SRYLREQATGAKD; RYLREQATGAKDT; YLREQATGAKDTK; LREQATGAKDTKP; REQATGAKDTKPM; EQATGAKDTKPMG; QATGAKDTKPMGR; ATGAKDTKPMGRS; TGAKDTKPMGRSG; GAKDTKPMGRSGA; AKDTKPMGRSGAT; KDTKPMGRSGATS; DTKPMGRSGATSR; TKPMGRSGATSRK; KPMGRSGATSRKA; PMGRSGATSRKAL; MGRSGATSRKALE; GRSGATSRKALET; RSGATSRKALETL; SGATSRKALETLR; GATSRKALETLRR; ATSRKALETLRRV; TSRKALETLRRVG; SRKALETLRRVGD; RKALETLRRVGDG; KALETLRRVGDGV; ALETLRRVGDGVQ; LETLRRVGDGVQR; ETLRRVGDGVQRN; TLRRVGDGVQRNH; LRRVGDGVQRNHE; RRVGDGVQRNHET; RVGDGVQRNHETA; VGDGVQRNHETAF; GDGVQRNHETAFQ; DGVQRNHETAFQG; GVQRNHETAFQGM; VQRNHETAFQGML; QRNHETAFQGMLR; RNHETAFQGMLRK; NHETAFQGMLRKL; HETAFQGMLRKLD; ETAFQGMLRKLDI; TAFQGMLRKLDIK; AFQGMLRKLDIKN; FQGMLRKLDIKNE; QGMLRKLDIKNED; GMLRKLDIKNEDD; MLRKLDIKNEDDV; LRKLDIKNEDDVK; RKLDIKNEDDVKS; KLDIKNEDDVKSL; LDIKNEDDVKSLS; DIKNEDDVKSLSR; IKNEDDVKSLSRV; KNEDDVKSLSRVM; NEDDVKSLSRVMI; EDDVKSLSRVMIH; DDVKSLSRVMIHV; DVKSLSRVMIHVF; VKSLSRVMIHVFS; KSLSRVMIHVFSD; SLSRVMIHVFSDG; LSRVMIHVFSDGV; SRVMIHVFSDGVT; RVMIHVFSDGVTN; VMIHVFSDGVTNW; MIHVFSDGVTNWG; IHVFSDGVTNWGR; HVFSDGVTNWGRI; VFSDGVTNWGRIV; FSDGVTNWGRIVT; SDGVTNWGRIVTL; DGVTNWGRIVTLI; GVTNWGRIVTLIS; VTNWGRIVTLISF; TNWGRIVTLISFG; NWGRIVTLISFGA; WGRIVTLISFGAF; GRIVTLISFGAFV; RIVTLISFGAFVA; IVTLISFGAFVAK; VTLISFGAFVAKH; TLISFGAFVAKHL; LISFGAFVAKHLK; ISFGAFVAKHLKT; SFGAFVAKHLKTI; FGAFVAKHLKTIN; GAFVAKHLKTINQ; AFVAKHLKTINQE; FVAKHLKTINQES; VAKHLKTINQESC; AKHLKTINQESCI; KHLKTINQESCIE; HLKTINQESCIEP; LKTINQESCIEPL; KTINQESCIEPLA; TINQESCIEPLAE; INQESCIEPLAES; NQESCIEPLAESI; QESCIEPLAESIT; ESCIEPLAESITD; SCIEPLAESITDV; CIEPLAESITDVL; IEPLAESITDVLV; EPLAESITDVLVR; PLAESITDVLVRT; LAESITDVLVRTK; AESITDVLVRTKR; ESITDVLVRTKRD; SITDVLVRTKRDW; ITDVLVRTKRDWL; TDVLVRTKRDWLV; DVLVRTKRDWLVK; VLVRTKRDWLVKQ; LVRTKRDWLVKQR; VRTKRDWLVKQRG; RTKRDWLVKQRGW; TKRDWLVKQRGWD; KRDWLVKQRGWDG; RDWLVKQRGWDGF; DWLVKQRGWDGFV; WLVKQRGWDGFVE; LVKQRGWDGFVEF; VKQRGWDGFVEFF; KQRGWDGFVEFFH; QRGWDGFVEFFHV; RGWDGFVEFFHVE; GWDGFVEFFHVED; WDGFVEFFHVEDL; DGFVEFFHVEDLE; GFVEFFHVEDLEG; FVEFFHVEDLEGG; VEFFHVEDLEGGI; EFFHVEDLEGGIR; FFHVEDLEGGIRN; FHVEDLEGGIRNV; HVEDLEGGIRNVL; VEDLEGGIRNVLL; EDLEGGIRNVLLA; DLEGGIRNVLLAF; LEGGIRNVLLAFA; EGGIRNVLLAFAG; GGIRNVLLAFAGV; GIRNVLLAFAGVA; IRNVLLAFAGVAG; RNVLLAFAGVAGV; NVLLAFAGVAGVG; VLLAFAGVAGVGA; LLAFAGVAGVGAG; LAFAGVAGVGAGL; AFAGVAGVGAGLA; FAGVAGVGAGLAY; AGVAGVGAGLAYL; GVAGVGAGLAYLI; VAGVGAGLAYLIR 14 mers: MFGLKRNAVIGLNL; FGLKRNAVIGLNLY; GLKRNAVIGLNLYC; LKRNAVIGLNLYCG; KRNAVIGLNLYCGG; RNAVIGLNLYCGGA; NAVIGLNLYCGGAG; AVIGLNLYCGGAGL; VIGLNLYCGGAGLG; IGLNLYCGGAGLGA; GLNLYCGGAGLGAG; LNLYCGGAGLGAGS; NLYCGGAGLGAGSG; LYCGGAGLGAGSGG; YCGGAGLGAGSGGA; CGGAGLGAGSGGAT; GGAGLGAGSGGATR; GAGLGAGSGGATRP; AGLGAGSGGATRPG; GLGAGSGGATRPGG; LGAGSGGATRPGGR; GAGSGGATRPGGRL; AGSGGATRPGGRLL; GSGGATRPGGRLLA; SGGATRPGGRLLAT; GGATRPGGRLLATE; GATRPGGRLLATEK; ATRPGGRLLATEKE; TRPGGRLLATEKEA; RPGGRLLATEKEAS; PGGRLLATEKEASA; GGRLLATEKEASAR; GRLLATEKEASARR; RLLATEKEASARRE; LLATEKEASARREI; LATEKEASARREIG; ATEKEASARREIGG; TEKEASARREIGGG; EKEASARREIGGGE; KEASARREIGGGEA; EASARREIGGGEAG; ASARREIGGGEAGA; SARREIGGGEAGAV; ARREIGGGEAGAVI; RREIGGGEAGAVIG; REIGGGEAGAVIGG; EIGGGEAGAVIGGS; IGGGEAGAVIGGSA; GGGEAGAVIGGSAG; GGEAGAVIGGSAGA; GEAGAVIGGSAGAS; EAGAVIGGSAGASP; AGAVIGGSAGASPP; GAVIGGSAGASPPS; AVIGGSAGASPPST; VIGGSAGASPPSTL; IGGSAGASPPSTLT; GGSAGASPPSTLTP; GSAGASPPSTLTPD; SAGASPPSTLTPDS; AGASPPSTLTPDSR; GASPPSTLTPDSRR; ASPPSTLTPDSRRV; SPPSTLTPDSRRVA; PPSTLTPDSRRVAR; PSTLTPDSRRVARP; STLTPDSRRVARPP; TLTPDSRRVARPPP; LTPDSRRVARPPPI; TPDSRRVARPPPIG; PDSRRVARPPPIGA; DSRRVARPPPIGAE; SRRVARPPPIGAEV; RRVARPPPIGAEVP; RVARPPPIGAEVPD; VARPPPIGAEVPDV; ARPPPIGAEVPDVT; RPPPIGAEVPDVTA; PPPIGAEVPDVTAT; PPIGAEVPDVTATP; PIGAEVPDVTATPA; IGAEVPDVTATPAR; GAEVPDVTATPARL; AEVPDVTATPARLL; EVPDVTATPARLLF; VPDVTATPARLLFF; PDVTATPARLLFFA; DVTATPARLLFFAP; VTATPARLLFFAPT; TATPARLLFFAPTR; ATPARLLFFAPTRR; TPARLLFFAPTRRA; PARLLFFAPTRRAA; ARLLFFAPTRRAAP; RLLFFAPTRRAAPL; LLFFAPTRRAAPLE; LFFAPTRRAAPLEE; FFAPTRRAAPLEEM; FAPTRRAAPLEEME; APTRRAAPLEEMEA; PTRRAAPLEEMEAP; TRRAAPLEEMEAPA; RRAAPLEEMEAPAA; RAAPLEEMEAPAAD; AAPLEEMEAPAADA; APLEEMEAPAADAI; PLEEMEAPAADAIM; LEEMEAPAADAIMS; EEMEAPAADAIMSP; EMEAPAADAIMSPE; MEAPAADAIMSPEE; EAPAADAIMSPEEE; APAADAIMSPEEEL; PAADAIMSPEEELD; AADAIMSPEEELDG; ADAIMSPEEELDGY; DAIMSPEEELDGYE; AIMSPEEELDGYEP; IMSPEEELDGYEPE; MSPEEELDGYEPEP; SPEEELDGYEPEPL; PEEELDGYEPEPLG; EEELDGYEPEPLGK; EELDGYEPEPLGKR; ELDGYEPEPLGKRP; LDGYEPEPLGKRPA; DGYEPEPLGKRPAV; GYEPEPLGKRPAVL; YEPEPLGKRPAVLP; EPEPLGKRPAVLPL; PEPLGKRPAVLPLL; EPLGKRPAVLPLLE; PLGKRPAVLPLLEL; LGKRPAVLPLLELV; GKRPAVLPLLELVG; KRPAVLPLLELVGE; RPAVLPLLELVGES; PAVLPLLELVGESG; AVLPLLELVGESGN; VLPLLELVGESGNN; LPLLELVGESGNNT; PLLELVGESGNNTS; LLELVGESGNNTST; LELVGESGNNTSTD; ELVGESGNNTSTDG; LVGESGNNTSTDGS; VGESGNNTSTDGSL; GESGNNTSTDGSLP; ESGNNTSTDGSLPS; SGNNTSTDGSLPST; GNNTSTDGSLPSTP; NNTSTDGSLPSTPP; NTSTDGSLPSTPPP; TSTDGSLPSTPPPA; STDGSLPSTPPPAE; TDGSLPSTPPPAEE; DGSLPSTPPPAEEE; GSLPSTPPPAEEEE; SLPSTPPPAEEEED; LPSTPPPAEEEEDD; PSTPPPAEEEEDDL; STPPPAEEEEDDLY; TPPPAEEEEDDLYR; PPPAEEEEDDLYRQ; PPAEEEEDDLYRQS; PAEEEEDDLYRQSL; AEEEEDDLYRQSLE; EEEEDDLYRQSLEI; EEEDDLYRQSLEII; EEDDLYRQSLEIIS; EDDLYRQSLEIISR; DDLYRQSLEIISRY; DLYRQSLEIISRYL; LYRQSLEIISRYLR; YRQSLEIISRYLRE; RQSLEIISRYLREQ; QSLEIISRYLREQA; SLEIISRYLREQAT; LEIISRYLREQATG; EIISRYLREQATGA; IISRYLREQATGAK; ISRYLREQATGAKD; SRYLREQATGAKDT; RYLREQATGAKDTK; YLREQATGAKDTKP; LREQATGAKDTKPM; REQATGAKDTKPMG; EQATGAKDTKPMGR; QATGAKDTKPMGRS; ATGAKDTKPMGRSG; TGAKDTKPMGRSGA; GAKDTKPMGRSGAT; AKDTKPMGRSGATS; KDTKPMGRSGATSR; DTKPMGRSGATSRK; TKPMGRSGATSRKA; KPMGRSGATSRKAL; PMGRSGATSRKALE; MGRSGATSRKALET; GRSGATSRKALETL; RSGATSRKALETLR; SGATSRKALETLRR; GATSRKALETLRRV; ATSRKALETLRRVG; TSRKALETLRRVGD; SRKALETLRRVGDG; RKALETLRRVGDGV; KALETLRRVGDGVQ; ALETLRRVGDGVQR; LETLRRVGDGVQRN; ETLRRVGDGVQRNH; TLRRVGDGVQRNHE; LRRVGDGVQRNHET; RRVGDGVQRNHETA; RVGDGVQRNHETAF; VGDGVQRNHETAFQ; GDGVQRNHETAFQG; DGVQRNHETAFQGM; GVQRNHETAFQGML; VQRNHETAFQGMLR; QRNHETAFQGMLRK; RNHETAFQGMLRKL; NHETAFQGMLRKLD; HETAFQGMLRKLDI; ETAFQGMLRKLDIK; TAFQGMLRKLDIKN; AFQGMLRKLDIKNE; FQGMLRKLDIKNED; QGMLRKLDIKNEDD; GMLRKLDIKNEDDV; MLRKLDIKNEDDVK; LRKLDIKNEDDVKS; RKLDIKNEDDVKSL; KLDIKNEDDVKSLS; LDIKNEDDVKSLSR; DIKNEDDVKSLSRV; IKNEDDVKSLSRVM; KNEDDVKSLSRVMI; NEDDVKSLSRVMIH; EDDVKSLSRVMIHV; DDVKSLSRVMIHVF; DVKSLSRVMIHVFS; VKSLSRVMIHVFSD; KSLSRVMIHVFSDG; SLSRVMIHVFSDGV; LSRVMIHVFSDGVT; SRVMIHVFSDGVTN; RVMIHVFSDGVTNW; VMIHVFSDGVTNWG; MIHVFSDGVTNWGR; IHVFSDGVTNWGRI; HVFSDGVTNWGRIV; VFSDGVTNWGRIVT; FSDGVTNWGRIVTL; SDGVTNWGRIVTLI; DGVTNWGRIVTLIS; GVTNWGRIVTLISF; VTNWGRIVTLISFG; TNWGRIVTLISFGA; NWGRIVTLISFGAF; WGRIVTLISFGAFV; GRIVTLISFGAFVA; RIVTLISFGAFVAK; IVTLISFGAFVAKH; VTLISFGAFVAKHL; TLISFGAFVAKHLK; LISFGAFVAKHLKT; ISFGAFVAKHLKTI; SFGAFVAKHLKTIN; FGAFVAKHLKTINQ; GAFVAKHLKTINQE; AFVAKHLKTINQES; FVAKHLKTINQESC; VAKHLKTINQESCI; AKHLKTINQESCIE; KHLKTINQESCIEP; HLKTINQESCIEPL; LKTINQESCIEPLA; KTINQESCIEPLAE; TINQESCIEPLAES; INQESCIEPLAESI; NQESCIEPLAESIT; QESCIEPLAESITD; ESCIEPLAESITDV; SCIEPLAESITDVL; CIEPLAESITDVLV; IEPLAESITDVLVR; EPLAESITDVLVRT; PLAESITDVLVRTK; LAESITDVLVRTKR; AESITDVLVRTKRD; ESITDVLVRTKRDW; SITDVLVRTKRDWL; ITDVLVRTKRDWLV; TDVLVRTKRDWLVK; DVLVRTKRDWLVKQ; VLVRTKRDWLVKQR; LVRTKRDWLVKQRG; VRTKRDWLVKQRGW; RTKRDWLVKQRGWD; TKRDWLVKQRGWDG; KRDWLVKQRGWDGF; RDWLVKQRGWDGFV; DWLVKQRGWDGFVE; WLVKQRGWDGFVEF; LVKQRGWDGFVEFF; VKQRGWDGFVEFFH; KQRGWDGFVEFFHV; QRGWDGFVEFFHVE; RGWDGFVEFFHVED; GWDGFVEFFHVEDL; WDGFVEFFHVEDLE; DGFVEFFHVEDLEG; GFVEFFHVEDLEGG; FVEFFHVEDLEGGI; VEFFHVEDLEGGIR; EFFHVEDLEGGIRN; FFHVEDLEGGIRNV; FHVEDLEGGIRNVL; HVEDLEGGIRNVLL; VEDLEGGIRNVLLA; EDLEGGIRNVLLAF; DLEGGIRNVLLAFA; LEGGIRNVLLAFAG; EGGIRNVLLAFAGV; GGIRNVLLAFAGVA; GIRNVLLAFAGVAG; IRNVLLAFAGVAGV; RNVLLAFAGVAGVG; NVLLAFAGVAGVGA; VLLAFAGVAGVGAG; LLAFAGVAGVGAGL; LAFAGVAGVGAGLA; AFAGVAGVGAGLAY; FAGVAGVGAGLAYL; AGVAGVGAGLAYLI; GVAGVGAGLAYLIR 15 mers: MFGLKRNAVIGLNLY; FGLKRNAVIGLNLYC; GLKRNAVIGLNLYCG; LKRNAVIGLNLYCGG; KRNAVIGLNLYCGGA; RNAVIGLNLYCGGAG; NAVIGLNLYCGGAGL; AVIGLNLYCGGAGLG; VIGLNLYCGGAGLGA; IGLNLYCGGAGLGAG; GLNLYCGGAGLGAGS; LNLYCGGAGLGAGSG; NLYCGGAGLGAGSGG; LYCGGAGLGAGSGGA; YCGGAGLGAGSGGAT; CGGAGLGAGSGGATR; GGAGLGAGSGGATRP; GAGLGAGSGGATRPG; AGLGAGSGGATRPGG; GLGAGSGGATRPGGR; LGAGSGGATRPGGRL; GAGSGGATRPGGRLL; AGSGGATRPGGRLLA; GSGGATRPGGRLLAT; SGGATRPGGRLLATE; GGATRPGGRLLATEK; GATRPGGRLLATEKE; ATRPGGRLLATEKEA; TRPGGRLLATEKEAS; RPGGRLLATEKEASA; PGGRLLATEKEASAR; GGRLLATEKEASARR; GRLLATEKEASARRE; RLLATEKEASARREI; LLATEKEASARREIG; LATEKEASARREIGG; ATEKEASARREIGGG; TEKEASARREIGGGE; EKEASARREIGGGEA; KEASARREIGGGEAG; EASARREIGGGEAGA; ASARREIGGGEAGAV; SARREIGGGEAGAVI; ARREIGGGEAGAVIG; RREIGGGEAGAVIGG; REIGGGEAGAVIGGS; EIGGGEAGAVIGGSA; IGGGEAGAVIGGSAG; GGGEAGAVIGGSAGA; GGEAGAVIGGSAGAS; GEAGAVIGGSAGASP; EAGAVIGGSAGASPP; AGAVIGGSAGASPPS; GAVIGGSAGASPPST; AVIGGSAGASPPSTL; VIGGSAGASPPSTLT; IGGSAGASPPSTLTP; GGSAGASPPSTLTPD; GSAGASPPSTLTPDS; SAGASPPSTLTPDSR; AGASPPSTLTPDSRR; GASPPSTLTPDSRRV; ASPPSTLTPDSRRVA; SPPSTLTPDSRRVAR; PPSTLTPDSRRVARP; PSTLTPDSRRVARPP; STLTPDSRRVARPPP; TLTPDSRRVARPPPI; LTPDSRRVARPPPIG; TPDSRRVARPPPIGA; PDSRRVARPPPIGAE; DSRRVARPPPIGAEV; SRRVARPPPIGAEVP; RRVARPPPIGAEVPD; RVARPPPIGAEVPDV; VARPPPIGAEVPDVT; ARPPPIGAEVPDVTA; RPPPIGAEVPDVTAT; PPPIGAEVPDVTATP; PPIGAEVPDVTATPA; PIGAEVPDVTATPAR; IGAEVPDVTATPARL; GAEVPDVTATPARLL; AEVPDVTATPARLLF; EVPDVTATPARLLFF; VPDVTATPARLLFFA; PDVTATPARLLFFAP; DVTATPARLLFFAPT; VTATPARLLFFAPTR; TATPARLLFFAPTRR; ATPARLLFFAPTRRA; TPARLLFFAPTRRAA; PARLLFFAPTRRAAP; ARLLFFAPTRRAAPL; RLLFFAPTRRAAPLE; LLFFAPTRRAAPLEE; LFFAPTRRAAPLEEM; FFAPTRRAAPLEEME; FAPTRRAAPLEEMEA; APTRRAAPLEEMEAP; PTRRAAPLEEMEAPA; TRRAAPLEEMEAPAA; RRAAPLEEMEAPAAD; RAAPLEEMEAPAADA; AAPLEEMEAPAADAI; APLEEMEAPAADAIM; PLEEMEAPAADAIMS; LEEMEAPAADAIMSP; EEMEAPAADAIMSPE; EMEAPAADAIMSPEE; MEAPAADAIMSPEEE; EAPAADAIMSPEEEL; APAADAIMSPEEELD; PAADAIMSPEEELDG; AADAIMSPEEELDGY; ADAIMSPEEELDGYE; DAIMSPEEELDGYEP; AIMSPEEELDGYEPE; IMSPEEELDGYEPEP; MSPEEELDGYEPEPL; SPEEELDGYEPEPLG; PEEELDGYEPEPLGK; EEELDGYEPEPLGKR; EELDGYEPEPLGKRP; ELDGYEPEPLGKRPA; LDGYEPEPLGKRPAV; DGYEPEPLGKRPAVL; GYEPEPLGKRPAVLP; YEPEPLGKRPAVLPL; EPEPLGKRPAVLPLL; PEPLGKRPAVLPLLE; EPLGKRPAVLPLLEL; PLGKRPAVLPLLELV; LGKRPAVLPLLELVG; GKRPAVLPLLELVGE; KRPAVLPLLELVGES; RPAVLPLLELVGESG; PAVLPLLELVGESGN; AVLPLLELVGESGNN; VLPLLELVGESGNNT; LPLLELVGESGNNTS; PLLELVGESGNNTST; LLELVGESGNNTSTD; LELVGESGNNTSTDG; ELVGESGNNTSTDGS; LVGESGNNTSTDGSL; VGESGNNTSTDGSLP; GESGNNTSTDGSLPS; ESGNNTSTDGSLPST; SGNNTSTDGSLPSTP; GNNTSTDGSLPSTPP; NNTSTDGSLPSTPPP; NTSTDGSLPSTPPPA; TSTDGSLPSTPPPAE; STDGSLPSTPPPAEE; TDGSLPSTPPPAEEE; DGSLPSTPPPAEEEE; GSLPSTPPPAEEEED; SLPSTPPPAEEEEDD; LPSTPPPAEEEEDDL; PSTPPPAEEEEDDLY; STPPPAEEEEDDLYR; TPPPAEEEEDDLYRQ; PPPAEEEEDDLYRQS; PPAEEEEDDLYRQSL; PAEEEEDDLYRQSLE; AEEEEDDLYRQSLEI; EEEEDDLYRQSLEII; EEEDDLYRQSLEIIS; EEDDLYRQSLEIISR; EDDLYRQSLEIISRY; DDLYRQSLEIISRYL; DLYRQSLEIISRYLR; LYRQSLEIISRYLRE; YRQSLEIISRYLREQ; RQSLEIISRYLREQA; QSLEIISRYLREQAT; SLEIISRYLREQATG; LEIISRYLREQATGA; EIISRYLREQATGAK; IISRYLREQATGAKD; ISRYLREQATGAKDT; SRYLREQATGAKDTK; RYLREQATGAKDTKP; YLREQATGAKDTKPM; LREQATGAKDTKPMG; REQATGAKDTKPMGR; EQATGAKDTKPMGRS; QATGAKDTKPMGRSG; ATGAKDTKPMGRSGA; TGAKDTKPMGRSGAT; GAKDTKPMGRSGATS; AKDTKPMGRSGATSR; KDTKPMGRSGATSRK; DTKPMGRSGATSRKA; TKPMGRSGATSRKAL; KPMGRSGATSRKALE; PMGRSGATSRKALET; MGRSGATSRKALETL; GRSGATSRKALETLR; RSGATSRKALETLRR; SGATSRKALETLRRV; GATSRKALETLRRVG; ATSRKALETLRRVGD; TSRKALETLRRVGDG; SRKALETLRRVGDGV; RKALETLRRVGDGVQ; KALETLRRVGDGVQR; ALETLRRVGDGVQRN; LETLRRVGDGVQRNH; ETLRRVGDGVQRNHE; TLRRVGDGVQRNHET; LRRVGDGVQRNHETA; RRVGDGVQRNHETAF; RVGDGVQRNHETAFQ; VGDGVQRNHETAFQG; GDGVQRNHETAFQGM; DGVQRNHETAFQGML; GVQRNHETAFQGMLR; VQRNHETAFQGMLRK; QRNHETAFQGMLRKL; RNHETAFQGMLRKLD; NHETAFQGMLRKLDI; HETAFQGMLRKLDIK; ETAFQGMLRKLDIKN; TAFQGMLRKLDIKNE; AFQGMLRKLDIKNED; FQGMLRKLDIKNEDD; QGMLRKLDIKNEDDV; GMLRKLDIKNEDDVK; MLRKLDIKNEDDVKS; LRKLDIKNEDDVKSL; RKLDIKNEDDVKSLS; KLDIKNEDDVKSLSR; LDIKNEDDVKSLSRV; DIKNEDDVKSLSRVM; IKNEDDVKSLSRVMI; KNEDDVKSLSRVMIH; NEDDVKSLSRVMIHV; EDDVKSLSRVMIHVF; DDVKSLSRVMIHVFS; DVKSLSRVMIHVFSD; VKSLSRVMIHVFSDG; KSLSRVMIHVFSDGV; SLSRVMIHVFSDGVT; LSRVMIHVFSDGVTN; SRVMIHVFSDGVTNW; RVMIHVFSDGVTNWG; VMIHVFSDGVTNWGR; MIHVFSDGVTNWGRI; IHVFSDGVTNWGRIV; HVFSDGVTNWGRIVT; VFSDGVTNWGRIVTL; FSDGVTNWGRIVTLI; SDGVTNWGRIVTLIS; DGVTNWGRIVTLISF; GVTNWGRIVTLISFG; VTNWGRIVTLISFGA; TNWGRIVTLISFGAF; NWGRIVTLISFGAFV; WGRIVTLISFGAFVA; GRIVTLISFGAFVAK; RIVTLISFGAFVAKH; IVTLISFGAFVAKHL; VTLISFGAFVAKHLK; TLISFGAFVAKHLKT; LISFGAFVAKHLKTI; ISFGAFVAKHLKTIN; SFGAFVAKHLKTINQ; FGAFVAKHLKTINQE; GAFVAKHLKTINQES; AFVAKHLKTINQESC; FVAKHLKTINQESCI; VAKHLKTINQESCIE; AKHLKTINQESCIEP; KHLKTINQESCIEPL; HLKTINQESCIEPLA; LKTINQESCIEPLAE; KTINQESCIEPLAES; TINQESCIEPLAESI; INQESCIEPLAESIT; NQESCIEPLAESITD; QESCIEPLAESITDV; ESCIEPLAESITDVL; SCIEPLAESITDVLV; CIEPLAESITDVLVR; IEPLAESITDVLVRT; EPLAESITDVLVRTK; PLAESITDVLVRTKR; LAESITDVLVRTKRD; AESITDVLVRTKRDW; ESITDVLVRTKRDWL; SITDVLVRTKRDWLV; ITDVLVRTKRDWLVK; TDVLVRTKRDWLVKQ; DVLVRTKRDWLVKQR; VLVRTKRDWLVKQRG; LVRTKRDWLVKQRGW; VRTKRDWLVKQRGWD; RTKRDWLVKQRGWDG; TKRDWLVKQRGWDGF; KRDWLVKQRGWDGFV; RDWLVKQRGWDGFVE; DWLVKQRGWDGFVEF; WLVKQRGWDGFVEFF; LVKQRGWDGFVEFFH; VKQRGWDGFVEFFHV; KQRGWDGFVEFFHVE; QRGWDGFVEFFHVED; RGWDGFVEFFHVEDL; GWDGFVEFFHVEDLE; WDGFVEFFHVEDLEG; DGFVEFFHVEDLEGG; GFVEFFHVEDLEGGI; FVEFFHVEDLEGGIR; VEFFHVEDLEGGIRN; EFFHVEDLEGGIRNV; FFHVEDLEGGIRNVL; FHVEDLEGGIRNVLL; HVEDLEGGIRNVLLA; VEDLEGGIRNVLLAF; EDLEGGIRNVLLAFA; DLEGGIRNVLLAFAG; LEGGIRNVLLAFAGV; EGGIRNVLLAFAGVA; GGIRNVLLAFAGVAG; GIRNVLLAFAGVAGV; IRNVLLAFAGVAGVG; RNVLLAFAGVAGVGA; NVLLAFAGVAGVGAG; VLLAFAGVAGVGAGL; LLAFAGVAGVGAGLA; LAFAGVAGVGAGLAY; AFAGVAGVGAGLAYL; FAGVAGVGAGLAYLI; AGVAGVGAGLAYLIR 16 mers: MFGLKRNAVIGLNLYC; FGLKRNAVIGLNLYCG; GLKRNAVIGLNLYCGG; LKRNAVIGLNLYCGGA; KRNAVIGLNLYCGGAG; RNAVIGLNLYCGGAGL; NAVIGLNLYCGGAGLG; AVIGLNLYCGGAGLGA; VIGLNLYCGGAGLGAG; IGLNLYCGGAGLGAGS; GLNLYCGGAGLGAGSG; LNLYCGGAGLGAGSGG; NLYCGGAGLGAGSGGA; LYCGGAGLGAGSGGAT; YCGGAGLGAGSGGATR; CGGAGLGAGSGGATRP; GGAGLGAGSGGATRPG; GAGLGAGSGGATRPGG; AGLGAGSGGATRPGGR; GLGAGSGGATRPGGRL; LGAGSGGATRPGGRLL; GAGSGGATRPGGRLLA; AGSGGATRPGGRLLAT; GSGGATRPGGRLLATE; SGGATRPGGRLLATEK; GGATRPGGRLLATEKE; GATRPGGRLLATEKEA; ATRPGGRLLATEKEAS; TRPGGRLLATEKEASA; RPGGRLLATEKEASAR; PGGRLLATEKEASARR; GGRLLATEKEASARRE; GRLLATEKEASARREI; RLLATEKEASARREIG; LLATEKEASARREIGG; LATEKEASARREIGGG; ATEKEASARREIGGGE; TEKEASARREIGGGEA; EKEASARREIGGGEAG; KEASARREIGGGEAGA; EASARREIGGGEAGAV; ASARREIGGGEAGAVI; SARREIGGGEAGAVIG; ARREIGGGEAGAVIGG; RREIGGGEAGAVIGGS; REIGGGEAGAVIGGSA; EIGGGEAGAVIGGSAG; IGGGEAGAVIGGSAGA; GGGEAGAVIGGSAGAS; GGEAGAVIGGSAGASP; GEAGAVIGGSAGASPP; EAGAVIGGSAGASPPS; AGAVIGGSAGASPPST; GAVIGGSAGASPPSTL; AVIGGSAGASPPSTLT; VIGGSAGASPPSTLTP; IGGSAGASPPSTLTPD; GGSAGASPPSTLTPDS; GSAGASPPSTLTPDSR; SAGASPPSTLTPDSRR; AGASPPSTLTPDSRRV; GASPPSTLTPDSRRVA; ASPPSTLTPDSRRVAR; SPPSTLTPDSRRVARP; PPSTLTPDSRRVARPP; PSTLTPDSRRVARPPP; STLTPDSRRVARPPPI; TLTPDSRRVARPPPIG; LTPDSRRVARPPPIGA; TPDSRRVARPPPIGAE; PDSRRVARPPPIGAEV; DSRRVARPPPIGAEVP; SRRVARPPPIGAEVPD; RRVARPPPIGAEVPDV; RVARPPPIGAEVPDVT; VARPPPIGAEVPDVTA; ARPPPIGAEVPDVTAT; RPPPIGAEVPDVTATP; PPPIGAEVPDVTATPA; PPIGAEVPDVTATPAR; PIGAEVPDVTATPARL; IGAEVPDVTATPARLL; GAEVPDVTATPARLLF; AEVPDVTATPARLLFF; EVPDVTATPARLLFFA; VPDVTATPARLLFFAP; PDVTATPARLLFFAPT; DVTATPARLLFFAPTR; VTATPARLLFFAPTRR; TATPARLLFFAPTRRA; ATPARLLFFAPTRRAA; TPARLLFFAPTRRAAP; PARLLFFAPTRRAAPL; ARLLFFAPTRRAAPLE; RLLFFAPTRRAAPLEE; LLFFAPTRRAAPLEEM; LFFAPTRRAAPLEEME; FFAPTRRAAPLEEMEA; FAPTRRAAPLEEMEAP; APTRRAAPLEEMEAPA; PTRRAAPLEEMEAPAA; TRRAAPLEEMEAPAAD; RRAAPLEEMEAPAADA; RAAPLEEMEAPAADAI; AAPLEEMEAPAADAIM; APLEEMEAPAADAIMS; PLEEMEAPAADAIMSP; LEEMEAPAADAIMSPE; EEMEAPAADAIMSPEE; EMEAPAADAIMSPEEE; MEAPAADAIMSPEEEL; EAPAADAIMSPEEELD; APAADAIMSPEEELDG; PAADAIMSPEEELDGY; AADAIMSPEEELDGYE; ADAIMSPEEELDGYEP; DAIMSPEEELDGYEPE; AIMSPEEELDGYEPEP; IMSPEEELDGYEPEPL; MSPEEELDGYEPEPLG; SPEEELDGYEPEPLGK; PEEELDGYEPEPLGKR; EEELDGYEPEPLGKRP; EELDGYEPEPLGKRPA; ELDGYEPEPLGKRPAV; LDGYEPEPLGKRPAVL; DGYEPEPLGKRPAVLP; GYEPEPLGKRPAVLPL; YEPEPLGKRPAVLPLL; EPEPLGKRPAVLPLLE; PEPLGKRPAVLPLLEL; EPLGKRPAVLPLLELV; PLGKRPAVLPLLELVG; LGKRPAVLPLLELVGE; GKRPAVLPLLELVGES; KRPAVLPLLELVGESG; RPAVLPLLELVGESGN; PAVLPLLELVGESGNN; AVLPLLELVGESGNNT; VLPLLELVGESGNNTS; LPLLELVGESGNNTST; PLLELVGESGNNTSTD; LLELVGESGNNTSTDG; LELVGESGNNTSTDGS; ELVGESGNNTSTDGSL; LVGESGNNTSTDGSLP; VGESGNNTSTDGSLPS; GESGNNTSTDGSLPST; ESGNNTSTDGSLPSTP; SGNNTSTDGSLPSTPP; GNNTSTDGSLPSTPPP; NNTSTDGSLPSTPPPA; NTSTDGSLPSTPPPAE; TSTDGSLPSTPPPAEE; STDGSLPSTPPPAEEE; TDGSLPSTPPPAEEEE; DGSLPSTPPPAEEEED; GSLPSTPPPAEEEEDD; SLPSTPPPAEEEEDDL; LPSTPPPAEEEEDDLY; PSTPPPAEEEEDDLYR; STPPPAEEEEDDLYRQ; TPPPAEEEEDDLYRQS; PPPAEEEEDDLYRQSL; PPAEEEEDDLYRQSLE; PAEEEEDDLYRQSLEI; AEEEEDDLYRQSLEII; EEEEDDLYRQSLEIIS; EEEDDLYRQSLEIISR; EEDDLYRQSLEIISRY; EDDLYRQSLEIISRYL; DDLYRQSLEIISRYLR; DLYRQSLEIISRYLRE; LYRQSLEIISRYLREQ; YRQSLEIISRYLREQA; RQSLEIISRYLREQAT; QSLEIISRYLREQATG; SLEIISRYLREQATGA; LEIISRYLREQATGAK; EIISRYLREQATGAKD; IISRYLREQATGAKDT; ISRYLREQATGAKDTK; SRYLREQATGAKDTKP; RYLREQATGAKDTKPM; YLREQATGAKDTKPMG; LREQATGAKDTKPMGR; REQATGAKDTKPMGRS; EQATGAKDTKPMGRSG; QATGAKDTKPMGRSGA; ATGAKDTKPMGRSGAT; TGAKDTKPMGRSGATS; GAKDTKPMGRSGATSR; AKDTKPMGRSGATSRK; KDTKPMGRSGATSRKA; DTKPMGRSGATSRKAL; TKPMGRSGATSRKALE; KPMGRSGATSRKALET; PMGRSGATSRKALETL; MGRSGATSRKALETLR; GRSGATSRKALETLRR; RSGATSRKALETLRRV; SGATSRKALETLRRVG; GATSRKALETLRRVGD; ATSRKALETLRRVGDG; TSRKALETLRRVGDGV; SRKALETLRRVGDGVQ; RKALETLRRVGDGVQR; KALETLRRVGDGVQRN; ALETLRRVGDGVQRNH; LETLRRVGDGVQRNHE; ETLRRVGDGVQRNHET; TLRRVGDGVQRNHETA; LRRVGDGVQRNHETAF; RRVGDGVQRNHETAFQ; RVGDGVQRNHETAFQG; VGDGVQRNHETAFQGM; GDGVQRNHETAFQGML; DGVQRNHETAFQGMLR; GVQRNHETAFQGMLRK; VQRNHETAFQGMLRKL; QRNHETAFQGMLRKLD; RNHETAFQGMLRKLDI; NHETAFQGMLRKLDIK; HETAFQGMLRKLDIKN; ETAFQGMLRKLDIKNE; TAFQGMLRKLDIKNED; AFQGMLRKLDIKNEDD; FQGMLRKLDIKNEDDV; QGMLRKLDIKNEDDVK; GMLRKLDIKNEDDVKS; MLRKLDIKNEDDVKSL; LRKLDIKNEDDVKSLS; RKLDIKNEDDVKSLSR; KLDIKNEDDVKSLSRV; LDIKNEDDVKSLSRVM; DIKNEDDVKSLSRVMI; IKNEDDVKSLSRVMIH; KNEDDVKSLSRVMIHV; NEDDVKSLSRVMIHVF; EDDVKSLSRVMIHVFS; DDVKSLSRVMIHVFSD; DVKSLSRVMIHVFSDG; VKSLSRVMIHVFSDGV; KSLSRVMIHVFSDGVT; SLSRVMIHVFSDGVTN; LSRVMIHVFSDGVTNW; SRVMIHVFSDGVTNWG; RVMIHVFSDGVTNWGR; VMIHVFSDGVTNWGRI; MIHVFSDGVTNWGRIV; IHVFSDGVTNWGRIVT; HVFSDGVTNWGRIVTL; VFSDGVTNWGRIVTLI; FSDGVTNWGRIVTLIS; SDGVTNWGRIVTLISF; DGVTNWGRIVTLISFG; GVTNWGRIVTLISFGA; VTNWGRIVTLISFGAF; TNWGRIVTLISFGAFV; NWGRIVTLISFGAFVA; WGRIVTLISFGAFVAK; GRIVTLISFGAFVAKH; RIVTLISFGAFVAKHL; IVTLISFGAFVAKHLK; VTLISFGAFVAKHLKT; TLISFGAFVAKHLKTI; LISFGAFVAKHLKTIN; ISFGAFVAKHLKTINQ; SFGAFVAKHLKTINQE; FGAFVAKHLKTINQES; GAFVAKHLKTINQESC; AFVAKHLKTINQESCI; FVAKHLKTINQESCIE; VAKHLKTINQESCIEP; AKHLKTINQESCIEPL; KHLKTINQESCIEPLA; HLKTINQESCIEPLAE; LKTINQESCIEPLAES; KTINQESCIEPLAESI; TINQESCIEPLAESIT; INQESCIEPLAESITD; NQESCIEPLAESITDV; QESCIEPLAESITDVL; ESCIEPLAESITDVLV; SCIEPLAESITDVLVR; CIEPLAESITDVLVRT; IEPLAESITDVLVRTK; EPLAESITDVLVRTKR; PLAESITDVLVRTKRD; LAESITDVLVRTKRDW; AESITDVLVRTKRDWL; ESITDVLVRTKRDWLV; SITDVLVRTKRDWLVK; ITDVLVRTKRDWLVKQ; TDVLVRTKRDWLVKQR; DVLVRTKRDWLVKQRG; VLVRTKRDWLVKQRGW; LVRTKRDWLVKQRGWD; VRTKRDWLVKQRGWDG; RTKRDWLVKQRGWDGF; TKRDWLVKQRGWDGFV; KRDWLVKQRGWDGFVE; RDWLVKQRGWDGFVEF; DWLVKQRGWDGFVEFF; WLVKQRGWDGFVEFFH; LVKQRGWDGFVEFFHV; VKQRGWDGFVEFFHVE; KQRGWDGFVEFFHVED; QRGWDGFVEFFHVEDL; RGWDGFVEFFHVEDLE; GWDGFVEFFHVEDLEG; WDGFVEFFHVEDLEGG; DGFVEFFHVEDLEGGI; GFVEFFHVEDLEGGIR; FVEFFHVEDLEGGIRN; VEFFHVEDLEGGIRNV; EFFHVEDLEGGIRNVL; FFHVEDLEGGIRNVLL; FHVEDLEGGIRNVLLA; HVEDLEGGIRNVLLAF; VEDLEGGIRNVLLAFA; EDLEGGIRNVLLAFAG; DLEGGIRNVLLAFAGV; LEGGIRNVLLAFAGVA; EGGIRNVLLAFAGVAG; GGIRNVLLAFAGVAGV; GIRNVLLAFAGVAGVG; IRNVLLAFAGVAGVGA; RNVLLAFAGVAGVGAG; NVLLAFAGVAGVGAGL; VLLAFAGVAGVGAGLA; LLAFAGVAGVGAGLAY; LAFAGVAGVGAGLAYL; AFAGVAGVGAGLAYLI; FAGVAGVGAGLAYLIR SEQ ID NOS: 48181-49526

The one or more antigenic peptides can in one embodiment comprise a fragment of one or more BK virus antigens.

The one or more BK virus antigens can be selected from Table H.

TABLE H Protein designation and accession numbers for the proteins encoded by the BK virus genome. The amino acid sequence of each protein is displayed. BK virus protein accession data Amino acid sequence >gi|118752|sp|P14998|DNBI_POVBA MFCEPKNLVVLRQLSRQASVKVGKTWTGTKKRAQRIFIFILELL DNA- LEFCRGEDSVDGKNKSTTALPAVKDSVKDS binding protein (Agnoprotein) >gi|135313|sp|P15000|TASM_POVBA MDKVLNREESMELMDLLGLERAAWGNLPLMRKAYLKKCKEFHPD Small T KGGDEDKMKRMNTLYKKMEQDVKVAHQPDFGTWNSSEVCADFPL antigen CPDTLYCKEWPICSKKPSVHCPCMLCQLRLRHLNRKFLRKEPLV WIDCYCIDCFTQWFGLDLTEETLQWWVQIIGETPFRDLKL >gi|135279|sp|P14999|TALA_POVBA MDKVLNREESMELMDLLGLERAAWGNLPLMRKAYLKKCKEFHPD Large T KGGDEDKMKRMNTLYKKMEQDVKVAHQPDFGTWNSSEVPTYGTE antigen EWESWWSSFNEKWDEDLFCHEDMFASDEEATADSQHSTPPKKKR KVEDPKDFPSDLHQFLSQAVFSNRTLACFAVYTTKEKAQILYKK LMEKYSVTFISRHMCAGHNIIFFLTPHRHRVSAINNFCQKLCTF SFLICKGVNKEYLLYSALTRDPYHIIEESIQGGLKEHDFNPEEP EETKQVSWKLITEYAVETKCEDVFLLLGMYLEFQYNVEECKKCQ KKDQPYHFKYHEKHFANAIIFAESKNQKSICQQAVDTVLAKKRV DTLHMTREEMLTERFNHILDKMDLIFGAHGNAVLEQYMAGVAWL HCLLPKMDSVIFDFLHCVVFNVPKRRYWLFKGPIDSGKTTLAAG LLDLCGGKALNVNLPMERLTFELGVAIDQYMVVFEDVKGTGAES KDLPSGHGINNLDSLRDYLDGSVKVNLEKKHLNKRTQIFPPGLV TMNEYPVPKTLQARFVRQIDFRPKIYLRKSLQNSEFLLEKRILQ SGMTLLLLLIWFRPVADFSKDIQSRIVEWKERLDSEISMYTFSR MKYNICMGKCILDITREEDSETEDSGHGSSTESQSQCSSQVSDT SAPDSENPHSQELHLCKGFQCFKRPKTPPPK >gi|116622|sp|P14996|COA1_POVBA MAPTKRKGECPGAAPKKPKEPVQVPKLLIKGGVEVLEVKTGVDA Coat ITEVECFLNPEMGDPDDNLRGYSQHLSAENAFESDSPDRKMLPC protein VP1 YSTARIPLPNLNEDLTCGNLLMWEAVTVKTEVIGITSMLNLHAG SQKVHENGGGKPVQGSNFHFFAVGGDPLEMQGVLMNYRTKYPQG TITPKNPTAQSQVMNTDHKAYLDKNNAYPVECWIPDPSRNENTR YFGTYTGGENVPPVLHVTNTATTVLLDEQGVGPLCKADSLYVSA ADICGLFTNSSGTQQWRGLARYFKIRLRKRSVKNPYPISFLLSD LINRRTQKVDGQPMYGMESQVEEVRVFDGTEQLPGDPDMIRYID RQGQLQTKMV >gi|116641|sp|P14997|COA2_POVBA MGAALALLGDLVASVSEAAAATGFSVAEIAAGEAAAAIEVQIAS Coat LATVEGITTTSEAIAAIGLTPQTYAVIAGAPGAIAGFAALIQTV protein VP2/VP3 TGISSLAQVGYRFFSDWDHKVSTVGLYQQSGMALELFNPDEYYD ILFPGVNTFVNNIQYLDPRHWGPSLFATISQALWHVIRDDIPAI TSQELQRRTERFFRDSLARFLEETTWTIVNAPINFYNYIQDYYS NLSPIRPSMVRQVAEREGTHVNFGHTYSIDNADSIEEVTQRMDL RNKESVHSGEFIEKTIAPGGANQRTAPQWMLPLLLGLYGTVTPA LEAYEDGPNQKKRRVSRGSSQKAKGTRASAKTTNKRRSRSSRS MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAP APGIFSSQPGHTPHPAASRDPVARTS PLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAE MSSQLHLTPFTARGRFATVVEELFRD GVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRH LHTWIQDNGGWDAFVELYGPSMRPLF DFSWLSLKTLLSLALVGACITLGAYLGHK SEQ ID NOS: 1-6

Preferred BK virus fragments capable of interacting with one or more MHC class 1 molecules are listed in Table I.

TABLE I Predicted MHC class 1 BK virus peptide sequences. Prediction of 8-, 9-, 10-, 11-mers from all 6 reading frames of the genome (access no #V01108) obtained using the program displayed in FIG. 2. BK virus reading frame 1 8 mers: FCKNCKRI; CKNCKRIG; KNCKRIGI; NCKRIGIS; CKRIGISP; KRIGISPN; RIGISPNS; IGISPNSF; GISPNSFA; ISPNSFAR; SPNSFARP; PNSFARPQ; NSFARPQK; SFARPQKK; FARPQKKP; ARPQKKPP; RPQKKPPH; PQKKPPHP; QKKPPHPY; KKPPHPYY; KPPHPYYL; PPHPYYLR; PHPYYLRE; HPYYLRER; PYYLRERV; YYLRERVE; YLRERVEA; LRERVEAE; RERVEAEA; ERVEAEAA; RVEAEAAS; VEAEAASA; EAEAASAS; AEAASASY; EAASASYI; AASASYIL; KKRPQGGA; KRPQGGAA; RPQGGAAY; PQGGAAYP; QGGAAYPW; GGAAYPWN; GAAYPWNA; AAYPWNAA; AYPWNAAK; YPWNAAKP; PQEGKCMT; QEGKCMTH; EGKCMTHR; GKCMTHRG; KCMTHRGM; CMTHRGMQ; MTHRGMQP; THRGMQPN; HRGMQPNH; RGMQPNHD; GMQPNHDL; MQPNHDLR; QPNHDLRK; PNHDLRKE; NHDLRKES; HDLRKESA; LTGRSCLP; TGRSCLPM; GRSCLPME; RSCLPMEC; SCLPMECS; CLPMECSQ; LPMECSQT; PMECSQTM; MECSQTMT; ECSQTMTS; CSQTMTSG; SQTMTSGR; QTMTSGRK; TMTSGRKV; MTSGRKVH; TSGRKVHD; SGRKVHDR; GRKVHDRH; RKVHDRHV; KVHDRHVL; VHDRHVLR; HDRHVLRA; ESWPCPQL; SWPCPQLN; WPCPQLNW; PCPQLNWT; CPQLNWTK; PQLNWTKA; QLNWTKAM; LNWTKAMV; NWTKAMVL; WTKAMVLR; TKAMVLRQ; KAMVLRQL; AMVLRQLS; MVLRQLSR; VLRQLSRQ; LRQLSRQA; RQLSRQAS; QLSRQASV; LSRQASVK; SRQASVKV; RQASVKVG; QASVKVGK; ASVKVGKT; SVKVGKTW; VKVGKTWT; KVGKTWTG; VGKTWTGT; GKTWTGTK; KTWTGTKK; TWTGTKKR; WTGTKKRA; TGTKKRAQ; GTKKRAQR; TKKRAQRI; KKRAQRIF; KRAQRIFI; RAQRIFIF; AQRIFIFI; QRIFIFIL; RIFIFILE; IFIFILEL; FIFILELL; IFILELLL; FILELLLE; ILELLLEF; LELLLEFC; ELLLEFCR; LLLEFCRG; LLEFCRGE; LEFCRGED; EFCRGEDS; FCRGEDSV; CRGEDSVD; RGEDSVDG; GEDSVDGK; EDSVDGKN; DSVDGKNK; SVDGKNKS; VDGKNKST; DGKNKSTT; GKNKSTTA; KNKSTTAL; NKSTTALP; KSTTALPA; STTALPAV; TTALPAVK; TALPAVKD; ALPAVKDS; LPAVKDSV; PAVKDSVK; AVKDSVKD; VKDSVKDS; VSNPFFFV; SNPFFFVF; NPFFFVFP; PFFFVFPG; FFFVFPGS; FFVFPGSW; FVFPGSWV; VFPGSWVL; FPGSWVLL; LPVYLRLL; PVYLRLLL; VYLRLLLP; YLRLLLPQ; LRLLLPQD; RLLLPQDF; LLLPQDFQ; LLPQDFQW; LPQDFQWL; PQDFQWLK; QDFQWLKL; DFQWLKLL; FQWLKLLL; QWLKLLLG; WLKLLLGR; LKLLLGRL; KLLLGRLL; LLLGRLLL; LLGRLLLL; KFKLHPLL; FKLHPLLL; LLVLLGLL; LVLLGLLL; VLLGLLLG; LLGLLLGL; LGLLLGLL; GLLLGLLL; FKLLVVLV; KLLVVLVP; GISSLMIG; ISSLMIGI; SSLMIGIT; SLMIGITK; LMIGITKF; MIGITKFP; IGITKFPL; ASISNQAW; SISNQAWL; ISNQAWLW; SNQAWLWN; NQAWLWNC; QAWLWNCL; AWLWNCLT; WLWNCLTQ; LWNCLTQM; WNCLTQMS; NCLTQMST; CLTQMSTM; LTQMSTMI; TQMSTMIF; QMSTMIFC; MSTMIFCF; STMIFCFL; TMIFCFLV; ILLLIIFN; LLLIIFNT; LLIIFNTL; LIIFNTLI; IIFNTLIL; IFNTLILG; FNTLILGI; NTLILGIG; TLILGIGV; LILGIGVL; ILGIGVLL; LGIGVLLC; GIGVLLCL; IGVLLCLL; GVLLCLLL; VLLCLLLF; LLCLLLFP; LCLLLFPR; CLLLFPRL; LLLFPRLC; LLFPRLCG; LFPRLCGM; FPRLCGML; PRLCGMLL; RLCGMLLG; LCGMLLGM; CGMLLGMI; GMLLGMIY; MLLGMIYL; LLGMIYLL; PHRNCREE; HRNCREEQ; RNCREEQK; NCREEQKD; CREEQKDF; REEQKDFL; EEQKDFLE; EQKDFLET; QKDFLETP; KDFLETPW; DFLETPWL; FLETPWLD; LETPWLDF; ETPWLDFW; TPWLDFWR; PWLDFWRK; WLDFWRKL; LDFWRKLP; DFWRKLPG; FWRKLPGQ; WRKLPGQL; TFIIIFNN; FIIIFNNI; IIIFNNII; IIFNNIIL; IFNNIILI; FNNIILIF; NNIILIFP; NIILIFPL; IILIFPLL; ILIFPLLG; LIFPLLGP; IFPLLGPQ; FPLLGPQW; PLLGPQWL; LLGPQWLD; LGPQWLDK; LKGKVPVY; KGKVPVYI; GKVPVYIL; KVPVYILA; VPVYILAI; PVYILAIL; VYILAILI; YILAILIV; KKLHKEWT; EINKVYIQ; INKVYIQE; NKVYIQES; KVYIQESL; KKLLPQEV; KLLPQEVL; LLPQEVLI; LPQEVLIK; PQEVLIKE; QEVLIKEL; EVLIKELL; VLIKELLL; LIKELLLN; IKELLLNG; KELLLNGC; ELLLNGCC; LLLNGCCL; LLNGCCLY; LNGCCLYF; HLLLKHMK; LLLKHMKM; LLKHMKMA; LKHMKMAP; KHMKMAPT; HMKMAPTK; MKMAPTKR; KMAPTKRK; MAPTKRKG; APTKRKGE; PTKRKGEC; TKRKGECP; KRKGECPG; RKGECPGA; KGECPGAA; GECPGAAP; ECPGAAPK; CPGAAPKK; PGAAPKKP; GAAPKKPK; AAPKKPKE; APKKPKEP; PKKPKEPV; KKPKEPVQ; KPKEPVQV; PKEPVQVP; KEPVQVPK; EPVQVPKL; PVQVPKLL; VQVPKLLI; QVPKLLIK; VPKLLIKG; PKLLIKGG; KLLIKGGV; LLIKGGVE; LIKGGVEV; IKGGVEVL; KGGVEVLE; GGVEVLEV; GVEVLEVK; VEVLEVKT; EVLEVKTG; VLEVKTGV; LEVKTGVD; EVKTGVDA; VKTGVDAI; KTGVDAIT; TGVDAITE; GVDAITEV; VDAITEVE; DAITEVEC; AITEVECF; ITEVECFL; TEVECFLN; EVECFLNP; VECFLNPE; ECFLNPEM; CFLNPEMG; FLNPEMGD; LNPEMGDP; NPEMGDPD; PEMGDPDE; EMGDPDEN; MGDPDENL; GDPDENLR; DPDENLRG; PDENLRGF; DENLRGFS; ENLRGFSL; NLRGFSLK; LRGFSLKL; RGFSLKLS; GFSLKLSA; FSLKLSAE; SLKLSAEN; LKLSAEND; KLSAENDF; LSAENDFS; SAENDFSS; AENDFSSD; ENDFSSDS; NDFSSDSP; DFSSDSPE; FSSDSPER; SSDSPERK; SDSPERKM; DSPERKML; SPERKMLP; PERKMLPC; ERKMLPCY; RKMLPCYS; KMLPCYST; MLPCYSTA; LPCYSTAR; PCYSTARI; CYSTARIP; YSTARIPL; STARIPLP; TARIPLPN; ARIPLPNL; RIPLPNLN; IPLPNLNE; PLPNLNED; LPNLNEDL; PNLNEDLT; NLNEDLTC; LNEDLTCG; NEDLTCGN; EDLTCGNL; DLTCGNLL; LTCGNLLM; TCGNLLMW; CGNLLMWE; GNLLMWEA; NLLMWEAV; LLMWEAVT; LMWEAVTV; MWEAVTVQ; WEAVTVQT; EAVTVQTE; AVTVQTEV; VTVQTEVI; TVQTEVIG; VQTEVIGI; QTEVIGIT; TEVIGITS; EVIGITSM; VIGITSML; IGITSMLN; GITSMLNL; ITSMLNLH; TSMLNLHA; SMLNLHAG; MLNLHAGS; LNLHAGSQ; NLHAGSQK; LHAGSQKV; HAGSQKVH; AGSQKVHE; GSQKVHEH; SQKVHEHG; QKVHEHGG; KVHEHGGG; VHEHGGGK; HEHGGGKP; EHGGGKPI; HGGGKPIQ; GGGKPIQG; GGKPIQGS; GKPIQGSN; KPIQGSNF; PIQGSNFH; IQGSNFHF; QGSNFHFF; GSNFHFFA; SNFHFFAV; NFHFFAVG; FHFFAVGG; HFFAVGGE; FFAVGGEP; FAVGGEPL; AVGGEPLE; VGGEPLEM; GGEPLEMQ; GEPLEMQG; EPLEMQGV; PLEMQGVL; LEMQGVLM; EMQGVLMN; MQGVLMNY; QGVLMNYR; GVLMNYRS; VLMNYRSK; LMNYRSKY; MNYRSKYP; NYRSKYPD; YRSKYPDG; RSKYPDGT; SKYPDGTI; KYPDGTIT; YPDGTITP; PDGTITPK; DGTITPKN; GTITPKNP; TITPKNPT; ITPKNPTA; TPKNPTAQ; PKNPTAQS; KNPTAQSQ; NPTAQSQV; PTAQSQVM; TAQSQVMN; AQSQVMNT; QSQVMNTD; SQVMNTDH; QVMNTDHK; VMNTDHKA; MNTDHKAY; NTDHKAYL; TDHKAYLD; DHKAYLDK; HKAYLDKN; KAYLDKNN; AYLDKNNA; YLDKNNAY; LDKNNAYP; DKNNAYPV; KNNAYPVE; NNAYPVEC; NAYPVECW; AYPVECWV; YPVECWVP; PVECWVPD; VECWVPDP; ECWVPDPS; CWVPDPSR; WVPDPSRN; VPDPSRNE; PDPSRNEN; DPSRNENA; PSRNENAR; SRNENARY; RNENARYF; NENARYFG; ENARYFGT; NARYFGTF; ARYFGTFT; RYFGTFTG; YFGTFTGG; FGTFTGGE; GTFTGGEN; TFTGGENV; FTGGENVP; TGGENVPP; GGENVPPV; GENVPPVL; ENVPPVLH; NVPPVLHV; VPPVLHVT; PPVLHVTN; PVLHVTNT; VLHVTNTA; LHVTNTAT; HVTNTATT; VTNTATTV; TNTATTVL; NTATTVLL; TATTVLLD; ATTVLLDE; TTVLLDEQ; TVLLDEQG; VLLDEQGV; LLDEQGVG; LDEQGVGP; DEQGVGPL; EQGVGPLC; QGVGPLCK; GVGPLCKA; VGPLCKAD; GPLCKADS; PLCKADSL; LCKADSLY; CKADSLYV; KADSLYVS; ADSLYVSA; DSLYVSAA; SLYVSAAD; LYVSAADI; YVSAADIC; VSAADICG; SAADICGL; AADICGLF; ADICGLFT; DICGLFTN; ICGLFTNS; CGLFTNSS; GLFTNSSG; LFTNSSGT; FTNSSGTQ; TNSSGTQQ; NSSGTQQW; SSGTQQWR; SGTQQWRG; GTQQWRGL; TQQWRGLA; QQWRGLAR; QWRGLARY; WRGLARYF; RGLARYFK; GLARYFKI; LARYFKIR; ARYFKIRL; RYFKIRLR; YFKIRLRK; FKIRLRKR; KIRLRKRS; IRLRKRSV; RLRKRSVK; LRKRSVKN; RKRSVKNP; KRSVKNPY; RSVKNPYP; SVKNPYPI; VKNPYPIS; KNPYPISF; NPYPISFL; PYPISFLL; YPISFLLS; PISFLLSD; ISFLLSDL; SFLLSDLI; FLLSDLIN; LLSDLINR; LSDLINRR; SDLINRRT; DLINRRTQ; LINRRTQR; INRRTQRV; NRRTQRVD; RRTQRVDG; RTQRVDGQ; TQRVDGQP; QRVDGQPM; RVDGQPMY; VDGQPMYG; DGQPMYGM; GQPMYGME; QPMYGMES; PMYGMESQ; MYGMESQV; YGMESQVE; GMESQVEE; MESQVEEV; ESQVEEVR; SQVEEVRV; QVEEVRVF; VEEVRVFD; EEVRVFDG; EVRVFDGT; VRVFDGTE; RVFDGTER; VFDGTERL; FDGTERLP; DGTERLPG; GTERLPGD; TERLPGDP; ERLPGDPD; RLPGDPDM; LPGDPDMI; PGDPDMIR; GDPDMIRY; DPDMIRYI; PDMIRYID; DMIRYIDK; MIRYIDKQ; IRYIDKQG; RYIDKQGQ; YIDKQGQL; IDKQGQLQ; DKQGQLQT; KQGQLQTK; QGQLQTKM; GQLQTKML; TGAFIVHI; GAFIVHIH; AFIVHIHL; FIVHIHLI; IVHIHLIN; VHIHLINA; HIHLINAA; IHLINAAF; HLINAAFV; ATFKLVLF; TFKLVLFW; FKLVLFWG; KLVLFWGW; LVLFWGWC; VLFWGWCF; LFWGWCFR; FWGWCFRP; WGWCFRPF; GWCFRPFK; WCFRPFKT; CFRPFKTL; FRPFKTLK; RPFKTLKA; PFKTLKAF; FKTLKAFT; KTLKAFTQ; TLKAFTQM; LKAFTQMQ; KAFTQMQL; AFTQMQLL; FTQMQLLT; TQMQLLTM; QMQLLTMG; MQLLTMGV; PLGIFSRG; SMSRVFSF; ILFSCNIK; LFSCNIKN; FSCNIKNT; SCNIKNTF; CNIKNTFP; NIKNTFPH; IKNTFPHA; KNTFPHAY; NTFPHAYI; TFPHAYII; FPHAYIIF; PHAYIIFH; HAYIIFHP; KSIHTYLR; SIHTYLRI; IHTYLRIQ; HTYLRIQP; TYLRIQPF; YLRIQPFL; LRIQPFLP; RIQPFLPF; IQPFLPFN; QPFLPFNN; PFLPFNNS; FLPFNNSR; LPFNNSRL; PFNNSRLY; FNNSRLYI; NNSRLYIS; NSRLYISC; SRLYISCK; RLYISCKI; LYISCKIS; YISCKISY; ISCKISYR; SCKISYRP; CKISYRPK; KISYRPKP; ISYRPKPN; IYFGPKIY; YFGPKIYL; FGPKIYLS; GPKIYLSY; PKIYLSYK; KIYLSYKS; IYLSYKSS; YLSYKSSL; LSYKSSLQ; SYKSSLQG; YKSSLQGF; KSSLQGFR; SSLQGFRD; SLQGFRDR; LQGFRDRI; QGFRDRIL; GFRDRILI; FRDRILIH; RDRILIHC; DRILIHCN; RILIHCNQ; ILIHCNQA; LIHCNQAW; IHCNQAWW; HCNQAWWK; CNQAWWKY; NQAWWKYL; QAWWKYLG; AWWKYLGS; WWKYLGSF; WKYLGSFV; FSSCPFYI; SSCPFYIF; SCPFYIFK; CPFYIFKN; PFYIFKNN; FYIFKNNH; YIFKNNHV; IFKNNHVL; FKNNHVLI; KNNHVLIY; NNHVLIYS; NHVLIYSY; HVLIYSYT; CCFSTING; CFSTINGT; FSTINGTF; STINGTFK; PVSSFRYI; VSSFRYIE; SSFRYIEN; SFRYIENN; FRYIENNT; RYIENNTV; YIENNTVQ; IENNTVQK; ENNTVQKI; NNTVQKIK; NTVQKIKY; TVQKIKYY; VQKIKYYR; QKIKYYRI; KIKYYRIH; IKYYRIHF; KYYRIHFR; QTVQPSNT; TVQPSNTC; VQPSNTCH; QPSNTCHI; PSNTCHIL; SNTCHILF; YSISMSSK; SISMSSKY; HFFPGHMK; FFPGHMKG; FPGHMKGI; PGHMKGIY; GHMKGIYS; HMKGIYSF; MKGIYSFF; KGIYSFFS; NCIYCLLT; CIYCLLTN; IYCLLTNT; YCLLTNTF; CLLTNTFL; LLTNTFLI; LTNTFLIF; TNTFLIFT; NTFLIFTF; TFLIFTFC; FLIFTFCK; LIFTFCKN; IFTFCKNN; FTFCKNNS; TFCKNNSI; FCKNNSIC; CKNNSICK; KNNSICKV; NNSICKVL; NSICKVLF; SICKVLFM; ICKVLFMI; CKVLFMIL; KVLFMILK; VLFMILKV; LFMILKVI; FMILKVIR; MILKVIRL; ILKVIRLV; LKVIRLVF; KVIRLVFF; VIRLVFFL; IRLVFFLT; RLVFFLTL; LVFFLTLF; VFFLTLFT; FFLTLFTL; FLTLFTLL; LTLFTLLY; TLFTLLYI; LFTLLYIV; FTLLYIVL; TLLYIVLK; LLYIVLKF; KHILTLCL; HILTLCLY; ILTLCLYC; LTLCLYCI; TLCLYCIL; LCLYCILS; CLYCILSN; FPRHLLCF; PRHLLCFF; RHLLCFFR; HLLCFFRL; LLCFFRLF; LCFFRLFW; CFFRLFWA; FFRLFWAK; FRLFWAKI; RLFWAKIM; LFWAKIML; FWAKIMLL; APLNAFFY; PLNAFFYS; LNAFFYSM; NAFFYSMV; AFFYSMVW; FFYSMVWI; FYSMVWIS; YSMVWISS; VFLINTLT; FLINTLTN; KTKGTQLL; TKGTQLLT; KGTQLLTE; GTQLLTEI; TQLLTEII; QLLTEIIN; LLTEIINC; LTEIINCR; TEIINCRN; EIINCRNS; IINCRNSM; INCRNSMS; NCRNSMSM; CRNSMSMW; RNSMSMWS; KEYNIMPS; EYNIMPST; YNIMPSTH; NIMPSTHV; IMPSTHVS; MPSTHVST; PSTHVSTN; STHVSTNK; THVSTNKS; HVSTNKSY; VSTNKSYR; STNKSYRI; TNKSYRIF; NKSYRIFF; KSYRIFFH; SYRIFFHK; YRIFFHKF; RIFFHKFF; IFFHKFFI; FFHKFFIQ; FHKFFIQN; HKFFIQNL; KFFIQNLS; FFIQNLSF; FIQNLSFF; IQNLSFFF; QNLSFFFS; NLSFFFSS; LSFFFSSI; SFFFSSIH; FFFSSIHS; FFSSIHSK; FSSIHSKA; SSIHSKAG; SIHSKAGK; IHSKAGKG; HSKAGKGS; SKAGKGSI; KAGKGSIT; AGKGSITK; GKGSITKY; KGSITKYS; GSITKYSL; SITKYSLT; ITKYSLTK; TKYSLTKK; KYSLTKKL; YSLTKKLV; IRGKVFRV; RGKVFRVF; GKVFRVFY; KVFRVFYL; VFRVFYLS; FRVFYLSF; RVFYLSFF; VFYLSFFF; FYLSFFFG; YLSFFFGW; LSFFFGWC; VLRICCCF; LRICCCFF; RICCCFFI; ICCCFFIT; CCCFFITG; CCFFITGK; CFFITGKH; FFITGKHI; FITGKHIF; ITGKHIFM; TGKHIFMA; GKHIFMAK; IFIPFFIK; FIPFFIKG; IPFFIKGT; PFFIKGTP; FFIKGTPP; FIKGTPPG; IKGTPPGL; KGTPPGLP; GTPPGLPL; TPPGLPLF; PPGLPLFC; PGLPLFCS; GLPLFCSI; LPLFCSIG; PLFCSIGW; LFCSIGWH; FCSIGWHL; YFIIYLNI; FIIYLNIS; SFRSLKGV; FRSLKGVS; RSLKGVSP; SLKGVSPI; LKGVSPII; KGVSPIIW; GVSPIIWT; VSPIIWTH; SPIIWTHH; PIIWTHHC; IIWTHHCR; IWTHHCRV; WTHHCRVS; THHCRVSS; HHCRVSSV; HCRVSSVR; CRVSSVRS; RVSSVRSK; VSSVRSKP; SSVRSKPN; SVRSKPNH; VRSKPNHC; RSKPNHCV; SKPNHCVK; KPNHCVKQ; PNHCVKQS; NHCVKQSM; HCVKQSMQ; QSIQTKGS; SIQTKGSF; IQTKGSFL; QTKGSFLK; TKGSFLKN; KGSFLKNF; GSFLKNFL; SFLKNFLF; FLKNFLFK; LKNFLFKC; KNFLFKCL; NFLFKCLN; FLFKCLNL; LFKCLNLS; HSMQGQCT; SMQGQCTE; MQGQCTEG; QGQCTEGF; GQCTEGFL; QCTEGFLE; CTEGFLEQ; TEGFLEQI; EGFLEQIG; GFLEQIGH; FLEQIGHS; LEQIGHSL; EQIGHSLQ; QIGHSLQY; IGHSLQYR; GHSLQYRV; HSLQYRVS; SLQYRVSG; LQYRVSGQ; QYRVSGQR; YRVSGQRG; RVSGQRGK; VSGQRGKS; SGQRGKSA; GQRGKSAQ; QRGKSAQT; RGKSAQTS; GKSAQTSE; KSAQTSEL; SAQTSELL; AQTSELLQ; QTSELLQV; TSELLQVP; SELLQVPK; ELLQVPKS; LLQVPKSG; ATFTSCSI; TFTSCSIF; FTSCSIFL; TSCSIFLY; SCSIFLYK; CSIFLYKV; SIFLYKVF; IFLYKVFI; FLYKVFIL; LYKVFILF; YKVFILFI; KVFILFIL; VFILFILS; FILFILSS; ILFILSSS; LFILSSSP; FILSSSPP; ILSSSPPL; LSSSPPLS; SSSPPLSG; AFLIKGRF; FLIKGRFP; LIKGRFPQ; IKGRFPQA; KGRFPQAA; GRFPQAAL; RFPQAALS; FPQAALSR; PQAALSRP; QAALSRPK; AALSRPKR; ALSRPKRS; LSRPKRSM; SRPKRSMS; RPKRSMSS; PKRSMSSM; KRSMSSMD; RSMSSMDS; SMSSMDSS; MSSMDSSL; SSMDSSLL; SMDSSLLR; MDSSLLRT; DSSLLRTL; SSLLRTLS 9 mers: FCKNCKRIG; CKNCKRIGI; KNCKRIGIS; NCKRIGISP; CKRIGISPN; KRIGISPNS; RIGISPNSF; IGISPNSFA; GISPNSFAR; ISPNSFARP; SPNSFARPQ; PNSFARPQK; NSFARPQKK; SFARPQKKP; FARPQKKPP; ARPQKKPPH; RPQKKPPHP; PQKKPPHPY; QKKPPHPYY; KKPPHPYYL; KPPHPYYLR; PPHPYYLRE; PHPYYLRER; HPYYLRERV; PYYLRERVE; YYLRERVEA; YLRERVEAE; LRERVEAEA; RERVEAEAA; ERVEAEAAS; RVEAEAASA; VEAEAASAS; EAEAASASY; AEAASASYI; EAASASYIL; KKRPQGGAA; KRPQGGAAY; RPQGGAAYP; PQGGAAYPW; QGGAAYPWN; GGAAYPWNA; GAAYPWNAA; AAYPWNAAK; AYPWNAAKP; PQEGKCMTH; QEGKCMTHR; EGKCMTHRG; GKCMTHRGM; KCMTHRGMQ; CMTHRGMQP; MTHRGMQPN; THRGMQPNH; HRGMQPNHD; RGMQPNHDL; GMQPNHDLR; MQPNHDLRK; QPNHDLRKE; PNHDLRKES; NHDLRKESA; LTGRSCLPM; TGRSCLPME; GRSCLPMEC; RSCLPMECS; SCLPMECSQ; CLPMECSQT; LPMECSQTM; PMECSQTMT; MECSQTMTS; ECSQTMTSG; CSQTMTSGR; SQTMTSGRK; QTMTSGRKV; TMTSGRKVH; MTSGRKVHD; TSGRKVHDR; SGRKVHDRH; GRKVHDRHV; RKVHDRHVL; KVHDRHVLR; VHDRHVLRA; ESWPCPQLN; SWPCPQLNW; WPCPQLNWT; PCPQLNWTK; CPQLNWTKA; PQLNWTKAM; QLNWTKAMV; LNWTKAMVL; NWTKAMVLR; WTKAMVLRQ; TKAMVLRQL; KAMVLRQLS; AMVLRQLSR; MVLRQLSRQ; VLRQLSRQA; LRQLSRQAS; RQLSRQASV; QLSRQASVK; LSRQASVKV; SRQASVKVG; RQASVKVGK; QASVKVGKT; ASVKVGKTW; SVKVGKTWT; VKVGKTWTG; KVGKTWTGT; VGKTWTGTK; GKTWTGTKK; KTWTGTKKR; TWTGTKKRA; WTGTKKRAQ; TGTKKRAQR; GTKKRAQRI; TKKRAQRIF; KKRAQRIFI; KRAQRIFIF; RAQRIFIFI; AQRIFIFIL; QRIFIFILE; RIFIFILEL; IFIFILELL; FIFILELLL; IFILELLLE; FILELLLEF; ILELLLEFC; LELLLEFCR; ELLLEFCRG; LLLEFCRGE; LLEFCRGED; LEFCRGEDS; EFCRGEDSV; FCRGEDSVD; CRGEDSVDG; RGEDSVDGK; GEDSVDGKN; EDSVDGKNK; DSVDGKNKS; SVDGKNKST; VDGKNKSTT; DGKNKSTTA; GKNKSTTAL; KNKSTTALP; NKSTTALPA; KSTTALPAV; STTALPAVK; TTALPAVKD; TALPAVKDS; ALPAVKDSV; LPAVKDSVK; PAVKDSVKD; AVKDSVKDS; VSNPFFFVF; SNPFFFVFP; NPFFFVFPG; PFFFVFPGS; FFFVFPGSW; FFVFPGSWV; FVFPGSWVL; VFPGSWVLL; LPVYLRLLL; PVYLRLLLP; VYLRLLLPQ; YLRLLLPQD; LRLLLPQDF; RLLLPQDFQ; LLLPQDFQW; LLPQDFQWL; LPQDFQWLK; PQDFQWLKL; QDFQWLKLL; DFQWLKLLL; FQWLKLLLG; QWLKLLLGR; WLKLLLGRL; LKLLLGRLL; KLLLGRLLL; LLLGRLLLL; KFKLHPLLL; LLVLLGLLL; LVLLGLLLG; VLLGLLLGL; LLGLLLGLL; LGLLLGLLL; FKLLVVLVP; GISSLMIGI; ISSLMIGIT; SSLMIGITK; SLMIGITKF; LMIGITKFP; MIGITKFPL; ASISNQAWL; SISNQAWLW; ISNQAWLWN; SNQAWLWNC; NQAWLWNCL; QAWLWNCLT; AWLWNCLTQ; WLWNCLTQM; LWNCLTQMS; WNCLTQMST; NCLTQMSTM; CLTQMSTMI; LTQMSTMIF; TQMSTMIFC; QMSTMIFCF; MSTMIFCFL; STMIFCFLV; ILLLIIFNT; LLLIIFNTL; LLIIFNTLI; LIIFNTLIL; IIFNTLILG; IFNTLILGI; FNTLILGIG; NTLILGIGV; TLILGIGVL; LILGIGVLL; ILGIGVLLC; LGIGVLLCL; GIGVLLCLL; IGVLLCLLL; GVLLCLLLF; VLLCLLLFP; LLCLLLFPR; LCLLLFPRL; CLLLFPRLC; LLLFPRLCG; LLFPRLCGM; LFPRLCGML; FPRLCGMLL; PRLCGMLLG; RLCGMLLGM; LCGMLLGMI; CGMLLGMIY; GMLLGMIYL; MLLGMIYLL; PHRNCREEQ; HRNCREEQK; RNCREEQKD; NCREEQKDF; CREEQKDFL; REEQKDFLE; EEQKDFLET; EQKDFLETP; QKDFLETPW; KDFLETPWL; DFLETPWLD; FLETPWLDF; LETPWLDFW; ETPWLDFWR; TPWLDFWRK; PWLDFWRKL; WLDFWRKLP; LDFWRKLPG; DFWRKLPGQ; FWRKLPGQL; TFIIIFNNI; FIIIFNNII; IIIFNNIIL; IIFNNIILI; IFNNIILIF; FNNIILIFP; NNIILIFPL; NIILIFPLL; IILIFPLLG; ILIFPLLGP; LIFPLLGPQ; IFPLLGPQW; FPLLGPQWL; PLLGPQWLD; LLGPQWLDK; LKGKVPVYI; KGKVPVYIL; GKVPVYILA; KVPVYILAI; VPVYILAIL; PVYILAILI; VYILAILIV; EINKVYIQE; INKVYIQES; NKVYIQESL; KKLLPQEVL; KLLPQEVLI; LLPQEVLIK; LPQEVLIKE; PQEVLIKEL; QEVLIKELL; EVLIKELLL; VLIKELLLN; LIKELLLNG; IKELLLNGC; KELLLNGCC; ELLLNGCCL; LLLNGCCLY; LLNGCCLYF; HLLLKHMKM; LLLKHMKMA; LLKHMKMAP; LKHMKMAPT; KHMKMAPTK; HMKMAPTKR; MKMAPTKRK; KMAPTKRKG; MAPTKRKGE; APTKRKGEC; PTKRKGECP; TKRKGECPG; KRKGECPGA; RKGECPGAA; KGECPGAAP; GECPGAAPK; ECPGAAPKK; CPGAAPKKP; PGAAPKKPK; GAAPKKPKE; AAPKKPKEP; APKKPKEPV; PKKPKEPVQ; KKPKEPVQV; KPKEPVQVP; PKEPVQVPK; KEPVQVPKL; EPVQVPKLL; PVQVPKLLI; VQVPKLLIK; QVPKLLIKG; VPKLLIKGG; PKLLIKGGV; KLLIKGGVE; LLIKGGVEV; LIKGGVEVL; IKGGVEVLE; KGGVEVLEV; GGVEVLEVK; GVEVLEVKT; VEVLEVKTG; EVLEVKTGV; VLEVKTGVD; LEVKTGVDA; EVKTGVDAI; VKTGVDAIT; KTGVDAITE; TGVDAITEV; GVDAITEVE; VDAITEVEC; DAITEVECF; AITEVECFL; ITEVECFLN; TEVECFLNP; EVECFLNPE; VECFLNPEM; ECFLNPEMG; CFLNPEMGD; FLNPEMGDP; LNPEMGDPD; NPEMGDPDE; PEMGDPDEN; EMGDPDENL; MGDPDENLR; GDPDENLRG; DPDENLRGF; PDENLRGFS; DENLRGFSL; ENLRGFSLK; NLRGFSLKL; LRGFSLKLS; RGFSLKLSA; GFSLKLSAE; FSLKLSAEN; SLKLSAEND; LKLSAENDF; KLSAENDFS; LSAENDFSS; SAENDFSSD; AENDFSSDS; ENDFSSDSP; NDFSSDSPE; DFSSDSPER; FSSDSPERK; SSDSPERKM; SDSPERKML; DSPERKMLP; SPERKMLPC; PERKMLPCY; ERKMLPCYS; RKMLPCYST; KMLPCYSTA; MLPCYSTAR; LPCYSTARI; PCYSTARIP; CYSTARIPL; YSTARIPLP; STARIPLPN; TARIPLPNL; ARIPLPNLN; RIPLPNLNE; IPLPNLNED; PLPNLNEDL; LPNLNEDLT; PNLNEDLTC; NLNEDLTCG; LNEDLTCGN; NEDLTCGNL; EDLTCGNLL; DLTCGNLLM; LTCGNLLMW; TCGNLLMWE; CGNLLMWEA; GNLLMWEAV; NLLMWEAVT; LLMWEAVTV; LMWEAVTVQ; MWEAVTVQT; WEAVTVQTE; EAVTVQTEV; AVTVQTEVI; VTVQTEVIG; TVQTEVIGI; VQTEVIGIT; QTEVIGITS; TEVIGITSM; EVIGITSML; VIGITSMLN; IGITSMLNL; GITSMLNLH; ITSMLNLHA; TSMLNLHAG; SMLNLHAGS; MLNLHAGSQ; LNLHAGSQK; NLHAGSQKV; LHAGSQKVH; HAGSQKVHE; AGSQKVHEH; GSQKVHEHG; SQKVHEHGG; QKVHEHGGG; KVHEHGGGK; VHEHGGGKP; HEHGGGKPI; EHGGGKPIQ; HGGGKPIQG; GGGKPIQGS; GGKPIQGSN; GKPIQGSNF; KPIQGSNFH; PIQGSNFHF; IQGSNFHFF; QGSNFHFFA; GSNFHFFAV; SNFHFFAVG; NFHFFAVGG; FHFFAVGGE; HFFAVGGEP; FFAVGGEPL; FAVGGEPLE; AVGGEPLEM; VGGEPLEMQ; GGEPLEMQG; GEPLEMQGV; EPLEMQGVL; PLEMQGVLM; LEMQGVLMN; EMQGVLMNY; MQGVLMNYR; QGVLMNYRS; GVLMNYRSK; VLMNYRSKY; LMNYRSKYP; MNYRSKYPD; NYRSKYPDG; YRSKYPDGT; RSKYPDGTI; SKYPDGTIT; KYPDGTITP; YPDGTITPK; PDGTITPKN; DGTITPKNP; GTITPKNPT; TITPKNPTA; ITPKNPTAQ; TPKNPTAQS; PKNPTAQSQ; KNPTAQSQV; NPTAQSQVM; PTAQSQVMN; TAQSQVMNT; AQSQVMNTD; QSQVMNTDH; SQVMNTDHK; QVMNTDHKA; VMNTDHKAY; MNTDHKAYL; NTDHKAYLD; TDHKAYLDK; DHKAYLDKN; HKAYLDKNN; KAYLDKNNA; AYLDKNNAY; YLDKNNAYP; LDKNNAYPV; DKNNAYPVE; KNNAYPVEC; NNAYPVECW; NAYPVECWV; AYPVECWVP; YPVECWVPD; PVECWVPDP; VECWVPDPS; ECWVPDPSR; CWVPDPSRN; WVPDPSRNE; VPDPSRNEN; PDPSRNENA; DPSRNENAR; PSRNENARY; SRNENARYF; RNENARYFG; NENARYFGT; ENARYFGTF; NARYFGTFT; ARYFGTFTG; RYFGTFTGG; YFGTFTGGE; FGTFTGGEN; GTFTGGENV; TFTGGENVP; FTGGENVPP; TGGENVPPV; GGENVPPVL; GENVPPVLH; ENVPPVLHV; NVPPVLHVT; VPPVLHVTN; PPVLHVTNT; PVLHVTNTA; VLHVTNTAT; LHVTNTATT; HVTNTATTV; VTNTATTVL; TNTATTVLL; NTATTVLLD; TATTVLLDE; ATTVLLDEQ; TTVLLDEQG; TVLLDEQGV; VLLDEQGVG; LLDEQGVGP; LDEQGVGPL; DEQGVGPLC; EQGVGPLCK; QGVGPLCKA; GVGPLCKAD; VGPLCKADS; GPLCKADSL; PLCKADSLY; LCKADSLYV; CKADSLYVS; KADSLYVSA; ADSLYVSAA; DSLYVSAAD; SLYVSAADI; LYVSAADIC; YVSAADICG; VSAADICGL; SAADICGLF; AADICGLFT; ADICGLFTN; DICGLFTNS; ICGLFTNSS; CGLFTNSSG; GLFTNSSGT; LFTNSSGTQ; FTNSSGTQQ; TNSSGTQQW; NSSGTQQWR; SSGTQQWRG; SGTQQWRGL; GTQQWRGLA; TQQWRGLAR; QQWRGLARY; QWRGLARYF; WRGLARYFK; RGLARYFKI; GLARYFKIR; LARYFKIRL; ARYFKIRLR; RYFKIRLRK; YFKIRLRKR; FKIRLRKRS; KIRLRKRSV; IRLRKRSVK; RLRKRSVKN; LRKRSVKNP; RKRSVKNPY; KRSVKNPYP; RSVKNPYPI; SVKNPYPIS; VKNPYPISF; KNPYPISFL; NPYPISFLL; PYPISFLLS; YPISFLLSD; PISFLLSDL; ISFLLSDLI; SFLLSDLIN; FLLSDLINR; LLSDLINRR; LSDLINRRT; SDLINRRTQ; DLINRRTQR; LINRRTQRV; INRRTQRVD; NRRTQRVDG; RRTQRVDGQ; RTQRVDGQP; TQRVDGQPM; QRVDGQPMY; RVDGQPMYG; VDGQPMYGM; DGQPMYGME; GQPMYGMES; QPMYGMESQ; PMYGMESQV; MYGMESQVE; YGMESQVEE; GMESQVEEV; MESQVEEVR; ESQVEEVRV; SQVEEVRVF; QVEEVRVFD; VEEVRVFDG; EEVRVFDGT; EVRVFDGTE; VRVFDGTER; RVFDGTERL; VFDGTERLP; FDGTERLPG; DGTERLPGD; GTERLPGDP; TERLPGDPD; ERLPGDPDM; RLPGDPDMI; LPGDPDMIR; PGDPDMIRY; GDPDMIRYI; DPDMIRYID; PDMIRYIDK; DMIRYIDKQ; MIRYIDKQG; IRYIDKQGQ; RYIDKQGQL; YIDKQGQLQ; IDKQGQLQT; DKQGQLQTK; KQGQLQTKM; QGQLQTKML; TGAFIVHIH; GAFIVHIHL; AFIVHIHLI; FIVHIHLIN; IVHIHLINA; VHIHLINAA; HIHLINAAF; IHLINAAFV; ATFKLVLFW; TFKLVLFWG; FKLVLFWGW; KLVLFWGWC; LVLFWGWCF; VLFWGWCFR; LFWGWCFRP; FWGWCFRPF; WGWCFRPFK; GWCFRPFKT; WCFRPFKTL; CFRPFKTLK; FRPFKTLKA; RPFKTLKAF; PFKTLKAFT; FKTLKAFTQ; KTLKAFTQM; TLKAFTQMQ; LKAFTQMQL; KAFTQMQLL; AFTQMQLLT; FTQMQLLTM; TQMQLLTMG; QMQLLTMGV; ILFSCNIKN; LFSCNIKNT; FSCNIKNTF; SCNIKNTFP; CNIKNTFPH; NIKNTFPHA; IKNTFPHAY; KNTFPHAYI; NTFPHAYII; TFPHAYIIF; FPHAYIIFH; PHAYIIFHP; KSIHTYLRI; SIHTYLRIQ; IHTYLRIQP; HTYLRIQPF; TYLRIQPFL; YLRIQPFLP; LRIQPFLPF; RIQPFLPFN; IQPFLPFNN; QPFLPFNNS; PFLPFNNSR; FLPFNNSRL; LPFNNSRLY; PFNNSRLYI; FNNSRLYIS; NNSRLYISC; NSRLYISCK; SRLYISCKI; RLYISCKIS; LYISCKISY; YISCKISYR; ISCKISYRP; SCKISYRPK; CKISYRPKP; KISYRPKPN; IYFGPKIYL; YFGPKIYLS; FGPKIYLSY; GPKIYLSYK; PKIYLSYKS; KIYLSYKSS; IYLSYKSSL; YLSYKSSLQ; LSYKSSLQG; SYKSSLQGF; YKSSLQGFR; KSSLQGFRD; SSLQGFRDR; SLQGFRDRI; LQGFRDRIL; QGFRDRILI; GFRDRILIH; FRDRILIHC; RDRILIHCN; DRILIHCNQ; RILIHCNQA; ILIHCNQAW; LIHCNQAWW; IHCNQAWWK; HCNQAWWKY; CNQAWWKYL; NQAWWKYLG; QAWWKYLGS; AWWKYLGSF; WWKYLGSFV; FSSCPFYIF; SSCPFYIFK; SCPFYIFKN; CPFYIFKNN; PFYIFKNNH; FYIFKNNHV; YIFKNNHVL; IFKNNHVLI; FKNNHVLIY; KNNHVLIYS; NNHVLIYSY; NHVLIYSYT; CCFSTINGT; CFSTINGTF; FSTINGTFK; PVSSFRYIE; VSSFRYIEN; SSFRYIENN; SFRYIENNT; FRYIENNTV; RYIENNTVQ; YIENNTVQK; IENNTVQKI; ENNTVQKIK; NNTVQKIKY; NTVQKIKYY; TVQKIKYYR; VQKIKYYRI; QKIKYYRIH; KIKYYRIHF; IKYYRIHFR; QTVQPSNTC; TVQPSNTCH; VQPSNTCHI; QPSNTCHIL; PSNTCHILF; YSISMSSKY; HFFPGHMKG; FFPGHMKGI; FPGHMKGIY; PGHMKGIYS; GHMKGIYSF; HMKGIYSFF; MKGIYSFFS; NCIYCLLTN; CIYCLLTNT; IYCLLTNTF; YCLLTNTFL; CLLTNTFLI; LLTNTFLIF; LTNTFLIFT; TNTFLIFTF; NTFLIFTFC; TFLIFTFCK; FLIFTFCKN; LIFTFCKNN; IFTFCKNNS; FTFCKNNSI; TFCKNNSIC; FCKNNSICK; CKNNSICKV; KNNSICKVL; NNSICKVLF; NSICKVLFM; SICKVLFMI; ICKVLFMIL; CKVLFMILK; KVLFMILKV; VLFMILKVI; LFMILKVIR; FMILKVIRL; MILKVIRLV; ILKVIRLVF; LKVIRLVFF; KVIRLVFFL; VIRLVFFLT; IRLVFFLTL; RLVFFLTLF; LVFFLTLFT; VFFLTLFTL; FFLTLFTLL; FLTLFTLLY; LTLFTLLYI; TLFTLLYIV; LFTLLYIVL; FTLLYIVLK; TLLYIVLKF; KHILTLCLY; HILTLCLYC; ILTLCLYCI; LTLCLYCIL; TLCLYCILS; LCLYCILSN; FPRHLLCFF; PRHLLCFFR; RHLLCFFRL; HLLCFFRLF; LLCFFRLFW; LCFFRLFWA; CFFRLFWAK; FFRLFWAKI; FRLFWAKIM; RLFWAKIML; LFWAKIMLL; APLNAFFYS; PLNAFFYSM; LNAFFYSMV; NAFFYSMVW; AFFYSMVWI; FFYSMVWIS; FYSMVWISS; VFLINTLTN; KTKGTQLLT; TKGTQLLTE; KGTQLLTEI; GTQLLTEII; TQLLTEIIN; QLLTEIINC; LLTEIINCR; LTEIINCRN; TEIINCRNS; EIINCRNSM; IINCRNSMS; INCRNSMSM; NCRNSMSMW; CRNSMSMWS; KEYNIMPST; EYNIMPSTH; YNIMPSTHV; NIMPSTHVS; IMPSTHVST; MPSTHVSTN; PSTHVSTNK; STHVSTNKS; THVSTNKSY; HVSTNKSYR; VSTNKSYRI; STNKSYRIF; TNKSYRIFF; NKSYRIFFH; KSYRIFFHK; SYRIFFHKF; YRIFFHKFF; RIFFHKFFI; IFFHKFFIQ; FFHKFFIQN; FHKFFIQNL; HKFFIQNLS; KFFIQNLSF; FFIQNLSFF; FIQNLSFFF; IQNLSFFFS; QNLSFFFSS; NLSFFFSSI; LSFFFSSIH; SFFFSSIHS; FFFSSIHSK; FFSSIHSKA; FSSIHSKAG; SSIHSKAGK; SIHSKAGKG; IHSKAGKGS; HSKAGKGSI; SKAGKGSIT; KAGKGSITK; AGKGSITKY; GKGSITKYS; KGSITKYSL; GSITKYSLT; SITKYSLTK; ITKYSLTKK; TKYSLTKKL; KYSLTKKLV; IRGKVFRVF; RGKVFRVFY; GKVFRVFYL; KVFRVFYLS; VFRVFYLSF; FRVFYLSFF; RVFYLSFFF; VFYLSFFFG; FYLSFFFGW; YLSFFFGWC; VLRICCCFF; LRICCCFFI; RICCCFFIT; ICCCFFITG; CCCFFITGK; CCFFITGKH; CFFITGKHI; FFITGKHIF; FITGKHIFM; ITGKHIFMA; TGKHIFMAK; IFIPFFIKG; FIPFFIKGT; IPFFIKGTP; PFFIKGTPP; FFIKGTPPG; FIKGTPPGL; IKGTPPGLP; KGTPPGLPL; GTPPGLPLF; TPPGLPLFC; PPGLPLFCS; PGLPLFCSI; GLPLFCSIG; LPLFCSIGW; PLFCSIGWH; LFCSIGWHL; YFIIYLNIS; SFRSLKGVS; FRSLKGVSP; RSLKGVSPI; SLKGVSPII; LKGVSPIIW; KGVSPIIWT; GVSPIIWTH; VSPIIWTHH; SPIIWTHHC; PIIWTHHCR; IIWTHHCRV; IWTHHCRVS; WTHHCRVSS; THHCRVSSV; HHCRVSSVR; HCRVSSVRS; CRVSSVRSK; RVSSVRSKP; VSSVRSKPN; SSVRSKPNH; SVRSKPNHC; VRSKPNHCV; RSKPNHCVK; SKPNHCVKQ; KPNHCVKQS; PNHCVKQSM; NHCVKQSMQ; QSIQTKGSF; SIQTKGSFL; IQTKGSFLK; QTKGSFLKN; TKGSFLKNF; KGSFLKNFL; GSFLKNFLF; SFLKNFLFK; FLKNFLFKC; LKNFLFKCL; KNFLFKCLN; NFLFKCLNL; FLFKCLNLS; HSMQGQCTE; SMQGQCTEG; MQGQCTEGF; QGQCTEGFL; GQCTEGFLE; QCTEGFLEQ; CTEGFLEQI; TEGFLEQIG; EGFLEQIGH; GFLEQIGHS; FLEQIGHSL; LEQIGHSLQ; EQIGHSLQY; QIGHSLQYR; IGHSLQYRV; GHSLQYRVS; HSLQYRVSG; SLQYRVSGQ; LQYRVSGQR; QYRVSGQRG; YRVSGQRGK; RVSGQRGKS; VSGQRGKSA; SGQRGKSAQ; GQRGKSAQT; QRGKSAQTS; RGKSAQTSE; GKSAQTSEL; KSAQTSELL; SAQTSELLQ; AQTSELLQV; QTSELLQVP; TSELLQVPK; SELLQVPKS; ELLQVPKSG; ATFTSCSIF; TFTSCSIFL; FTSCSIFLY; TSCSIFLYK; SCSIFLYKV; CSIFLYKVF; SIFLYKVFI; IFLYKVFIL; FLYKVFILF; LYKVFILFI; YKVFILFIL; KVFILFILS; VFILFILSS; FILFILSSS; ILFILSSSP; LFILSSSPP; FILSSSPPL; ILSSSPPLS; LSSSPPLSG; AFLIKGRFP; FLIKGRFPQ; LIKGRFPQA; IKGRFPQAA; KGRFPQAAL; GRFPQAALS; RFPQAALSR; FPQAALSRP; PQAALSRPK; QAALSRPKR; AALSRPKRS; ALSRPKRSM; LSRPKRSMS; SRPKRSMSS; RPKRSMSSM; PKRSMSSMD; KRSMSSMDS; RSMSSMDSS; SMSSMDSSL; MSSMDSSLL; SSMDSSLLR; SMDSSLLRT; MDSSLLRTL; DSSLLRTLS 10 mers: FCKNCKRIGI; CKNCKRIGIS; KNCKRIGISP; NCKRIGISPN; CKRIGISPNS; KRIGISPNSF; RIGISPNSFA; IGISPNSFAR; GISPNSFARP; ISPNSFARPQ; SPNSFARPQK; PNSFARPQKK; NSFARPQKKP; SFARPQKKPP; FARPQKKPPH; ARPQKKPPHP; RPQKKPPHPY; PQKKPPHPYY; QKKPPHPYYL; KKPPHPYYLR; KPPHPYYLRE; PPHPYYLRER; PHPYYLRERV; HPYYLRERVE; PYYLRERVEA; YYLRERVEAE; YLRERVEAEA; LRERVEAEAA; RERVEAEAAS; ERVEAEAASA; RVEAEAASAS; VEAEAASASY; EAEAASASYI; AEAASASYIL; KKRPQGGAAY; KRPQGGAAYP; RPQGGAAYPW; PQGGAAYPWN; QGGAAYPWNA; GGAAYPWNAA; GAAYPWNAAK; AAYPWNAAKP; PQEGKCMTHR; QEGKCMTHRG; EGKCMTHRGM; GKCMTHRGMQ; KCMTHRGMQP; CMTHRGMQPN; MTHRGMQPNH; THRGMQPNHD; HRGMQPNHDL; RGMQPNHDLR; GMQPNHDLRK; MQPNHDLRKE; QPNHDLRKES; PNHDLRKESA; LTGRSCLPME; TGRSCLPMEC; GRSCLPMECS; RSCLPMECSQ; SCLPMECSQT; CLPMECSQTM; LPMECSQTMT; PMECSQTMTS; MECSQTMTSG; ECSQTMTSGR; CSQTMTSGRK; SQTMTSGRKV; QTMTSGRKVH; TMTSGRKVHD; MTSGRKVHDR; TSGRKVHDRH; SGRKVHDRHV; GRKVHDRHVL; RKVHDRHVLR; KVHDRHVLRA; ESWPCPQLNW; SWPCPQLNWT; WPCPQLNWTK; PCPQLNWTKA; CPQLNWTKAM; PQLNWTKAMV; QLNWTKAMVL; LNWTKAMVLR; NWTKAMVLRQ; WTKAMVLRQL; TKAMVLRQLS; KAMVLRQLSR; AMVLRQLSRQ; MVLRQLSRQA; VLRQLSRQAS; LRQLSRQASV; RQLSRQASVK; QLSRQASVKV; LSRQASVKVG; SRQASVKVGK; RQASVKVGKT; QASVKVGKTW; ASVKVGKTWT; SVKVGKTWTG; VKVGKTWTGT; KVGKTWTGTK; VGKTWTGTKK; GKTWTGTKKR; KTWTGTKKRA; TWTGTKKRAQ; WTGTKKRAQR; TGTKKRAQRI; GTKKRAQRIF; TKKRAQRIFI; KKRAQRIFIF; KRAQRIFIFI; RAQRIFIFIL; AQRIFIFILE; QRIFIFILEL; RIFIFILELL; IFIFILELLL; FIFILELLLE; IFILELLLEF; FILELLLEFC; ILELLLEFCR; LELLLEFCRG; ELLLEFCRGE; LLLEFCRGED; LLEFCRGEDS; LEFCRGEDSV; EFCRGEDSVD; FCRGEDSVDG; CRGEDSVDGK; RGEDSVDGKN; GEDSVDGKNK; EDSVDGKNKS; DSVDGKNKST; SVDGKNKSTT; VDGKNKSTTA; DGKNKSTTAL; GKNKSTTALP; KNKSTTALPA; NKSTTALPAV; KSTTALPAVK; STTALPAVKD; TTALPAVKDS; TALPAVKDSV; ALPAVKDSVK; LPAVKDSVKD; PAVKDSVKDS; VSNPFFFVFP; SNPFFFVFPG; NPFFFVFPGS; PFFFVFPGSW; FFFVFPGSWV; FFVFPGSWVL; FVFPGSWVLL; LPVYLRLLLP; PVYLRLLLPQ; VYLRLLLPQD; YLRLLLPQDF; LRLLLPQDFQ; RLLLPQDFQW; LLLPQDFQWL; LLPQDFQWLK; LPQDFQWLKL; PQDFQWLKLL; QDFQWLKLLL; DFQWLKLLLG; FQWLKLLLGR; QWLKLLLGRL; WLKLLLGRLL; LKLLLGRLLL; KLLLGRLLLL; LLVLLGLLLG; LVLLGLLLGL; VLLGLLLGLL; LLGLLLGLLL; GISSLMIGIT; ISSLMIGITK; SSLMIGITKF; SLMIGITKFP; LMIGITKFPL; ASISNQAWLW; SISNQAWLWN; ISNQAWLWNC; SNQAWLWNCL; NQAWLWNCLT; QAWLWNCLTQ; AWLWNCLTQM; WLWNCLTQMS; LWNCLTQMST; WNCLTQMSTM; NCLTQMSTMI; CLTQMSTMIF; LTQMSTMIFC; TQMSTMIFCF; QMSTMIFCFL; MSTMIFCFLV; ILLLIIFNTL; LLLIIFNTLI; LLIIFNTLIL; LIIFNTLILG; IIFNTLILGI; IFNTLILGIG; FNTLILGIGV; NTLILGIGVL; TLILGIGVLL; LILGIGVLLC; ILGIGVLLCL; LGIGVLLCLL; GIGVLLCLLL; IGVLLCLLLF; GVLLCLLLFP; VLLCLLLFPR; LLCLLLFPRL; LCLLLFPRLC; CLLLFPRLCG; LLLFPRLCGM; LLFPRLCGML; LFPRLCGMLL; FPRLCGMLLG; PRLCGMLLGM; RLCGMLLGMI; LCGMLLGMIY; CGMLLGMIYL; GMLLGMIYLL; PHRNCREEQK; HRNCREEQKD; RNCREEQKDF; NCREEQKDFL; CREEQKDFLE; REEQKDFLET; EEQKDFLETP; EQKDFLETPW; QKDFLETPWL; KDFLETPWLD; DFLETPWLDF; FLETPWLDFW; LETPWLDFWR; ETPWLDFWRK; TPWLDFWRKL; PWLDFWRKLP; WLDFWRKLPG; LDFWRKLPGQ; DFWRKLPGQL; TFIIIFNNII; FIIIFNNIIL; IIIFNNIILI; IIFNNIILIF; IFNNIILIFP; FNNIILIFPL; NNIILIFPLL; NIILIFPLLG; IILIFPLLGP; ILIFPLLGPQ; LIFPLLGPQW; IFPLLGPQWL; FPLLGPQWLD; PLLGPQWLDK; LKGKVPVYIL; KGKVPVYILA; GKVPVYILAI; KVPVYILAIL; VPVYILAILI; PVYILAILIV; EINKVYIQES; INKVYIQESL; KKLLPQEVLI; KLLPQEVLIK; LLPQEVLIKE; LPQEVLIKEL; PQEVLIKELL; QEVLIKELLL; EVLIKELLLN; VLIKELLLNG; LIKELLLNGC; IKELLLNGCC; KELLLNGCCL; ELLLNGCCLY; LLLNGCCLYF; HLLLKHMKMA; LLLKHMKMAP; LLKHMKMAPT; LKHMKMAPTK; KHMKMAPTKR; HMKMAPTKRK; MKMAPTKRKG; KMAPTKRKGE; MAPTKRKGEC; APTKRKGECP; PTKRKGECPG; TKRKGECPGA; KRKGECPGAA; RKGECPGAAP; KGECPGAAPK; GECPGAAPKK; ECPGAAPKKP; CPGAAPKKPK; PGAAPKKPKE; GAAPKKPKEP; AAPKKPKEPV; APKKPKEPVQ; PKKPKEPVQV; KKPKEPVQVP; KPKEPVQVPK; PKEPVQVPKL; KEPVQVPKLL; EPVQVPKLLI; PVQVPKLLIK; VQVPKLLIKG; QVPKLLIKGG; VPKLLIKGGV; PKLLIKGGVE; KLLIKGGVEV; LLIKGGVEVL; LIKGGVEVLE; IKGGVEVLEV; KGGVEVLEVK; GGVEVLEVKT; GVEVLEVKTG; VEVLEVKTGV; EVLEVKTGVD; VLEVKTGVDA; LEVKTGVDAI; EVKTGVDAIT; VKTGVDAITE; KTGVDAITEV; TGVDAITEVE; GVDAITEVEC; VDAITEVECF; DAITEVECFL; AITEVECFLN; ITEVECFLNP; TEVECFLNPE; EVECFLNPEM; VECFLNPEMG; ECFLNPEMGD; CFLNPEMGDP; FLNPEMGDPD; LNPEMGDPDE; NPEMGDPDEN; PEMGDPDENL; EMGDPDENLR; MGDPDENLRG; GDPDENLRGF; DPDENLRGFS; PDENLRGFSL; DENLRGFSLK; ENLRGFSLKL; NLRGFSLKLS; LRGFSLKLSA; RGFSLKLSAE; GFSLKLSAEN; FSLKLSAEND; SLKLSAENDF; LKLSAENDFS; KLSAENDFSS; LSAENDFSSD; SAENDFSSDS; AENDFSSDSP; ENDFSSDSPE; NDFSSDSPER; DFSSDSPERK; FSSDSPERKM; SSDSPERKML; SDSPERKMLP; DSPERKMLPC; SPERKMLPCY; PERKMLPCYS; ERKMLPCYST; RKMLPCYSTA; KMLPCYSTAR; MLPCYSTARI; LPCYSTARIP; PCYSTARIPL; CYSTARIPLP; YSTARIPLPN; STARIPLPNL; TARIPLPNLN; ARIPLPNLNE; RIPLPNLNED; IPLPNLNEDL; PLPNLNEDLT; LPNLNEDLTC; PNLNEDLTCG; NLNEDLTCGN; LNEDLTCGNL; NEDLTCGNLL; EDLTCGNLLM; DLTCGNLLMW; LTCGNLLMWE; TCGNLLMWEA; CGNLLMWEAV; GNLLMWEAVT; NLLMWEAVTV; LLMWEAVTVQ; LMWEAVTVQT; MWEAVTVQTE; WEAVTVQTEV; EAVTVQTEVI; AVTVQTEVIG; VTVQTEVIGI; TVQTEVIGIT; VQTEVIGITS; QTEVIGITSM; TEVIGITSML; EVIGITSMLN; VIGITSMLNL; IGITSMLNLH; GITSMLNLHA; ITSMLNLHAG; TSMLNLHAGS; SMLNLHAGSQ; MLNLHAGSQK; LNLHAGSQKV; NLHAGSQKVH; LHAGSQKVHE; HAGSQKVHEH; AGSQKVHEHG; GSQKVHEHGG; SQKVHEHGGG; QKVHEHGGGK; KVHEHGGGKP; VHEHGGGKPI; HEHGGGKPIQ; EHGGGKPIQG; HGGGKPIQGS; GGGKPIQGSN; GGKPIQGSNF; GKPIQGSNFH; KPIQGSNFHF; PIQGSNFHFF; IQGSNFHFFA; QGSNFHFFAV; GSNFHFFAVG; SNFHFFAVGG; NFHFFAVGGE; FHFFAVGGEP; HFFAVGGEPL; FFAVGGEPLE; FAVGGEPLEM; AVGGEPLEMQ; VGGEPLEMQG; GGEPLEMQGV; GEPLEMQGVL; EPLEMQGVLM; PLEMQGVLMN; LEMQGVLMNY; EMQGVLMNYR; MQGVLMNYRS; QGVLMNYRSK; GVLMNYRSKY; VLMNYRSKYP; LMNYRSKYPD; MNYRSKYPDG; NYRSKYPDGT; YRSKYPDGTI; RSKYPDGTIT; SKYPDGTITP; KYPDGTITPK; YPDGTITPKN; PDGTITPKNP; DGTITPKNPT; GTITPKNPTA; TITPKNPTAQ; ITPKNPTAQS; TPKNPTAQSQ; PKNPTAQSQV; KNPTAQSQVM; NPTAQSQVMN; PTAQSQVMNT; TAQSQVMNTD; AQSQVMNTDH; QSQVMNTDHK; SQVMNTDHKA; QVMNTDHKAY; VMNTDHKAYL; MNTDHKAYLD; NTDHKAYLDK; TDHKAYLDKN; DHKAYLDKNN; HKAYLDKNNA; KAYLDKNNAY; AYLDKNNAYP; YLDKNNAYPV; LDKNNAYPVE; DKNNAYPVEC; KNNAYPVECW; NNAYPVECWV; NAYPVECWVP; AYPVECWVPD; YPVECWVPDP; PVECWVPDPS; VECWVPDPSR; ECWVPDPSRN; CWVPDPSRNE; WVPDPSRNEN; VPDPSRNENA; PDPSRNENAR; DPSRNENARY; PSRNENARYF; SRNENARYFG; RNENARYFGT; NENARYFGTF; ENARYFGTFT; NARYFGTFTG; ARYFGTFTGG; RYFGTFTGGE; YFGTFTGGEN; FGTFTGGENV; GTFTGGENVP; TFTGGENVPP; FTGGENVPPV; TGGENVPPVL; GGENVPPVLH; GENVPPVLHV; ENVPPVLHVT; NVPPVLHVTN; VPPVLHVTNT; PPVLHVTNTA; PVLHVTNTAT; VLHVTNTATT; LHVTNTATTV; HVTNTATTVL; VTNTATTVLL; TNTATTVLLD; NTATTVLLDE; TATTVLLDEQ; ATTVLLDEQG; TTVLLDEQGV; TVLLDEQGVG; VLLDEQGVGP; LLDEQGVGPL; LDEQGVGPLC; DEQGVGPLCK; EQGVGPLCKA; QGVGPLCKAD; GVGPLCKADS; VGPLCKADSL; GPLCKADSLY; PLCKADSLYV; LCKADSLYVS; CKADSLYVSA; KADSLYVSAA; ADSLYVSAAD; DSLYVSAADI; SLYVSAADIC; LYVSAADICG; YVSAADICGL; VSAADICGLF; SAADICGLFT; AADICGLFTN; ADICGLFTNS; DICGLFTNSS; ICGLFTNSSG; CGLFTNSSGT; GLFTNSSGTQ; LFTNSSGTQQ; FTNSSGTQQW; TNSSGTQQWR; NSSGTQQWRG; SSGTQQWRGL; SGTQQWRGLA; GTQQWRGLAR; TQQWRGLARY; QQWRGLARYF; QWRGLARYFK; WRGLARYFKI; RGLARYFKIR; GLARYFKIRL; LARYFKIRLR; ARYFKIRLRK; RYFKIRLRKR; YFKIRLRKRS; FKIRLRKRSV; KIRLRKRSVK; IRLRKRSVKN; RLRKRSVKNP; LRKRSVKNPY; RKRSVKNPYP; KRSVKNPYPI; RSVKNPYPIS; SVKNPYPISF; VKNPYPISFL; KNPYPISFLL; NPYPISFLLS; PYPISFLLSD; YPISFLLSDL; PISFLLSDLI; ISFLLSDLIN; SFLLSDLINR; FLLSDLINRR; LLSDLINRRT; LSDLINRRTQ; SDLINRRTQR; DLINRRTQRV; LINRRTQRVD; INRRTQRVDG; NRRTQRVDGQ; RRTQRVDGQP; RTQRVDGQPM; TQRVDGQPMY; QRVDGQPMYG; RVDGQPMYGM; VDGQPMYGME; DGQPMYGMES; GQPMYGMESQ; QPMYGMESQV; PMYGMESQVE; MYGMESQVEE; YGMESQVEEV; GMESQVEEVR; MESQVEEVRV; ESQVEEVRVF; SQVEEVRVFD; QVEEVRVFDG; VEEVRVFDGT; EEVRVFDGTE; EVRVFDGTER; VRVFDGTERL; RVFDGTERLP; VFDGTERLPG; FDGTERLPGD; DGTERLPGDP; GTERLPGDPD; TERLPGDPDM; ERLPGDPDMI; RLPGDPDMIR; LPGDPDMIRY; PGDPDMIRYI; GDPDMIRYID; DPDMIRYIDK; PDMIRYIDKQ; DMIRYIDKQG; MIRYIDKQGQ; IRYIDKQGQL; RYIDKQGQLQ; YIDKQGQLQT; IDKQGQLQTK; DKQGQLQTKM; KQGQLQTKML; TGAFIVHIHL; GAFIVHIHLI; AFIVHIHLIN; FIVHIHLINA; IVHIHLINAA; VHIHLINAAF; HIHLINAAFV; ATFKLVLFWG; TFKLVLFWGW; FKLVLFWGWC; KLVLFWGWCF; LVLFWGWCFR; VLFWGWCFRP; LFWGWCFRPF; FWGWCFRPFK; WGWCFRPFKT; GWCFRPFKTL; WCFRPFKTLK; CFRPFKTLKA; FRPFKTLKAF; RPFKTLKAFT; PFKTLKAFTQ; FKTLKAFTQM; KTLKAFTQMQ; TLKAFTQMQL; LKAFTQMQLL; KAFTQMQLLT; AFTQMQLLTM; FTQMQLLTMG; TQMQLLTMGV; ILFSCNIKNT; LFSCNIKNTF; FSCNIKNTFP; SCNIKNTFPH; CNIKNTFPHA; NIKNTFPHAY; IKNTFPHAYI; KNTFPHAYII; NTFPHAYIIF; TFPHAYIIFH; FPHAYIIFHP; KSIHTYLRIQ; SIHTYLRIQP; IHTYLRIQPF; HTYLRIQPFL; TYLRIQPFLP; YLRIQPFLPF; LRIQPFLPFN; RIQPFLPFNN; IQPFLPFNNS; QPFLPFNNSR; PFLPFNNSRL; FLPFNNSRLY; LPFNNSRLYI; PFNNSRLYIS; FNNSRLYISC; NNSRLYISCK; NSRLYISCKI; SRLYISCKIS; RLYISCKISY; LYISCKISYR; YISCKISYRP; ISCKISYRPK; SCKISYRPKP; CKISYRPKPN; IYFGPKIYLS; YFGPKIYLSY; FGPKIYLSYK; GPKIYLSYKS; PKIYLSYKSS; KIYLSYKSSL; IYLSYKSSLQ; YLSYKSSLQG; LSYKSSLQGF; SYKSSLQGFR; YKSSLQGFRD; KSSLQGFRDR; SSLQGFRDRI; SLQGFRDRIL; LQGFRDRILI; QGFRDRILIH; GFRDRILIHC; FRDRILIHCN; RDRILIHCNQ; DRILIHCNQA; RILIHCNQAW; ILIHCNQAWW; LIHCNQAWWK; IHCNQAWWKY; HCNQAWWKYL; CNQAWWKYLG; NQAWWKYLGS; QAWWKYLGSF; AWWKYLGSFV; FSSCPFYIFK; SSCPFYIFKN; SCPFYIFKNN; CPFYIFKNNH; PFYIFKNNHV; FYIFKNNHVL; YIFKNNHVLI; IFKNNHVLIY; FKNNHVLIYS; KNNHVLIYSY; NNHVLIYSYT; CCFSTINGTF; CFSTINGTFK; PVSSFRYIEN; VSSFRYIENN; SSFRYIENNT; SFRYIENNTV; FRYIENNTVQ; RYIENNTVQK; YIENNTVQKI; IENNTVQKIK; ENNTVQKIKY; NNTVQKIKYY; NTVQKIKYYR; TVQKIKYYRI; VQKIKYYRIH; QKIKYYRIHF; KIKYYRIHFR; QTVQPSNTCH; TVQPSNTCHI; VQPSNTCHIL; QPSNTCHILF; HFFPGHMKGI; FFPGHMKGIY; FPGHMKGIYS; PGHMKGIYSF; GHMKGIYSFF; HMKGIYSFFS; NCIYCLLTNT; CIYCLLTNTF; IYCLLTNTFL; YCLLTNTFLI; CLLTNTFLIF; LLTNTFLIFT; LTNTFLIFTF; TNTFLIFTFC; NTFLIFTFCK; TFLIFTFCKN; FLIFTFCKNN; LIFTFCKNNS; IFTFCKNNSI; FTFCKNNSIC; TFCKNNSICK; FCKNNSICKV; CKNNSICKVL; KNNSICKVLF; NNSICKVLFM; NSICKVLFMI; SICKVLFMIL; ICKVLFMILK; CKVLFMILKV; KVLFMILKVI; VLFMILKVIR; LFMILKVIRL; FMILKVIRLV; MILKVIRLVF; ILKVIRLVFF; LKVIRLVFFL; KVIRLVFFLT; VIRLVFFLTL; IRLVFFLTLF; RLVFFLTLFT; LVFFLTLFTL; VFFLTLFTLL; FFLTLFTLLY; FLTLFTLLYI; LTLFTLLYIV; TLFTLLYIVL; LFTLLYIVLK; FTLLYIVLKF; KHILTLCLYC; HILTLCLYCI; ILTLCLYCIL; LTLCLYCILS; TLCLYCILSN; FPRHLLCFFR; PRHLLCFFRL; RHLLCFFRLF; HLLCFFRLFW; LLCFFRLFWA; LCFFRLFWAK; CFFRLFWAKI; FFRLFWAKIM; FRLFWAKIML; RLFWAKIMLL; APLNAFFYSM; PLNAFFYSMV; LNAFFYSMVW; NAFFYSMVWI; AFFYSMVWIS; FFYSMVWISS; KTKGTQLLTE; TKGTQLLTEI; KGTQLLTEII; GTQLLTEIIN; TQLLTEIINC; QLLTEIINCR; LLTEIINCRN; LTEIINCRNS; TEIINCRNSM; EIINCRNSMS; IINCRNSMSM; INCRNSMSMW; NCRNSMSMWS; KEYNIMPSTH; EYNIMPSTHV; YNIMPSTHVS; NIMPSTHVST; IMPSTHVSTN; MPSTHVSTNK; PSTHVSTNKS; STHVSTNKSY; THVSTNKSYR; HVSTNKSYRI; VSTNKSYRIF; STNKSYRIFF; TNKSYRIFFH; NKSYRIFFHK; KSYRIFFHKF; SYRIFFHKFF; YRIFFHKFFI; RIFFHKFFIQ; IFFHKFFIQN; FFHKFFIQNL; FHKFFIQNLS; HKFFIQNLSF; KFFIQNLSFF; FFIQNLSFFF; FIQNLSFFFS; IQNLSFFFSS; QNLSFFFSSI; NLSFFFSSIH; LSFFFSSIHS; SFFFSSIHSK; FFFSSIHSKA; FFSSIHSKAG; FSSIHSKAGK; SSIHSKAGKG; SIHSKAGKGS; IHSKAGKGSI; HSKAGKGSIT; SKAGKGSITK; KAGKGSITKY; AGKGSITKYS; GKGSITKYSL; KGSITKYSLT; GSITKYSLTK; SITKYSLTKK; ITKYSLTKKL; TKYSLTKKLV; IRGKVFRVFY; RGKVFRVFYL; GKVFRVFYLS; KVFRVFYLSF; VFRVFYLSFF; FRVFYLSFFF; RVFYLSFFFG; VFYLSFFFGW; FYLSFFFGWC; VLRICCCFFI; LRICCCFFIT; RICCCFFITG; ICCCFFITGK; CCCFFITGKH; CCFFITGKHI; CFFITGKHIF; FFITGKHIFM; FITGKHIFMA; ITGKHIFMAK; IFIPFFIKGT; FIPFFIKGTP; IPFFIKGTPP; PFFIKGTPPG; FFIKGTPPGL; FIKGTPPGLP; IKGTPPGLPL; KGTPPGLPLF; GTPPGLPLFC; TPPGLPLFCS; PPGLPLFCSI; PGLPLFCSIG; GLPLFCSIGW; LPLFCSIGWH; PLFCSIGWHL; SFRSLKGVSP; FRSLKGVSPI; RSLKGVSPII; SLKGVSPIIW; LKGVSPIIWT; KGVSPIIWTH; GVSPIIWTHH; VSPIIWTHHC; SPIIWTHHCR; PIIWTHHCRV; IIWTHHCRVS; IWTHHCRVSS; WTHHCRVSSV; THHCRVSSVR; HHCRVSSVRS; HCRVSSVRSK; CRVSSVRSKP; RVSSVRSKPN; VSSVRSKPNH; SSVRSKPNHC; SVRSKPNHCV; VRSKPNHCVK; RSKPNHCVKQ; SKPNHCVKQS; KPNHCVKQSM; PNHCVKQSMQ; QSIQTKGSFL; SIQTKGSFLK; IQTKGSFLKN; QTKGSFLKNF; TKGSFLKNFL; KGSFLKNFLF; GSFLKNFLFK; SFLKNFLFKC; FLKNFLFKCL; LKNFLFKCLN; KNFLFKCLNL; NFLFKCLNLS; HSMQGQCTEG; SMQGQCTEGF; MQGQCTEGFL; QGQCTEGFLE; GQCTEGFLEQ; QCTEGFLEQI; CTEGFLEQIG; TEGFLEQIGH; EGFLEQIGHS; GFLEQIGHSL; FLEQIGHSLQ; LEQIGHSLQY; EQIGHSLQYR; QIGHSLQYRV; IGHSLQYRVS; GHSLQYRVSG; HSLQYRVSGQ; SLQYRVSGQR; LQYRVSGQRG; QYRVSGQRGK; YRVSGQRGKS; RVSGQRGKSA; VSGQRGKSAQ; SGQRGKSAQT; GQRGKSAQTS; QRGKSAQTSE; RGKSAQTSEL; GKSAQTSELL; KSAQTSELLQ; SAQTSELLQV; AQTSELLQVP; QTSELLQVPK; TSELLQVPKS; SELLQVPKSG; ATFTSCSIFL; TFTSCSIFLY; FTSCSIFLYK; TSCSIFLYKV; SCSIFLYKVF; CSIFLYKVFI; SIFLYKVFIL; IFLYKVFILF; FLYKVFILFI; LYKVFILFIL; YKVFILFILS; KVFILFILSS; VFILFILSSS; FILFILSSSP; ILFILSSSPP; LFILSSSPPL; FILSSSPPLS; ILSSSPPLSG; AFLIKGRFPQ; FLIKGRFPQA; LIKGRFPQAA; IKGRFPQAAL; KGRFPQAALS; GRFPQAALSR; RFPQAALSRP; FPQAALSRPK; PQAALSRPKR; QAALSRPKRS; AALSRPKRSM; ALSRPKRSMS; LSRPKRSMSS; SRPKRSMSSM; RPKRSMSSMD; PKRSMSSMDS; KRSMSSMDSS; RSMSSMDSSL; SMSSMDSSLL; MSSMDSSLLR; SSMDSSLLRT; SMDSSLLRTL; MDSSLLRTLS 11 mers: FCKNCKRIGIS; CKNCKRIGISP; KNCKRIGISPN; NCKRIGISPNS; CKRIGISPNSF; KRIGISPNSFA; RIGISPNSFAR; IGISPNSFARP; GISPNSFARPQ; ISPNSFARPQK; SPNSFARPQKK; PNSFARPQKKP; NSFARPQKKPP; SFARPQKKPPH; FARPQKKPPHP; ARPQKKPPHPY; RPQKKPPHPYY; PQKKPPHPYYL; QKKPPHPYYLR; KKPPHPYYLRE; KPPHPYYLRER; PPHPYYLRERV; PHPYYLRERVE; HPYYLRERVEA; PYYLRERVEAE; YYLRERVEAEA; YLRERVEAEAA; LRERVEAEAAS; RERVEAEAASA; ERVEAEAASAS; RVEAEAASASY; VEAEAASASYI; EAEAASASYIL; KKRPQGGAAYP; KRPQGGAAYPW; RPQGGAAYPWN; PQGGAAYPWNA; QGGAAYPWNAA; GGAAYPWNAAK; GAAYPWNAAKP; PQEGKCMTHRG; QEGKCMTHRGM; EGKCMTHRGMQ; GKCMTHRGMQP; KCMTHRGMQPN; CMTHRGMQPNH; MTHRGMQPNHD; THRGMQPNHDL; HRGMQPNHDLR; RGMQPNHDLRK; GMQPNHDLRKE; MQPNHDLRKES; QPNHDLRKESA; LTGRSCLPMEC; TGRSCLPMECS; GRSCLPMECSQ; RSCLPMECSQT; SCLPMECSQTM; CLPMECSQTMT; LPMECSQTMTS; PMECSQTMTSG; MECSQTMTSGR; ECSQTMTSGRK; CSQTMTSGRKV; SQTMTSGRKVH; QTMTSGRKVHD; TMTSGRKVHDR; MTSGRKVHDRH; TSGRKVHDRHV; SGRKVHDRHVL; GRKVHDRHVLR; RKVHDRHVLRA; ESWPCPQLNWT; SWPCPQLNWTK; WPCPQLNWTKA; PCPQLNWTKAM; CPQLNWTKAMV; PQLNWTKAMVL; QLNWTKAMVLR; LNWTKAMVLRQ; NWTKAMVLRQL; WTKAMVLRQLS; TKAMVLRQLSR; KAMVLRQLSRQ; AMVLRQLSRQA; MVLRQLSRQAS; VLRQLSRQASV; LRQLSRQASVK; RQLSRQASVKV; QLSRQASVKVG; LSRQASVKVGK; SRQASVKVGKT; RQASVKVGKTW; QASVKVGKTWT; ASVKVGKTWTG; SVKVGKTWTGT; VKVGKTWTGTK; KVGKTWTGTKK; VGKTWTGTKKR; GKTWTGTKKRA; KTWTGTKKRAQ; TWTGTKKRAQR; WTGTKKRAQRI; TGTKKRAQRIF; GTKKRAQRIFI; TKKRAQRIFIF; KKRAQRIFIFI; KRAQRIFIFIL; RAQRIFIFILE; AQRIFIFILEL; QRIFIFILELL; RIFIFILELLL; IFIFILELLLE; FIFILELLLEF; IFILELLLEFC; FILELLLEFCR; ILELLLEFCRG; LELLLEFCRGE; ELLLEFCRGED; LLLEFCRGEDS; LLEFCRGEDSV; LEFCRGEDSVD; EFCRGEDSVDG; FCRGEDSVDGK; CRGEDSVDGKN; RGEDSVDGKNK; GEDSVDGKNKS; EDSVDGKNKST; DSVDGKNKSTT; SVDGKNKSTTA; VDGKNKSTTAL; DGKNKSTTALP; GKNKSTTALPA; KNKSTTALPAV; NKSTTALPAVK; KSTTALPAVKD; STTALPAVKDS; TTALPAVKDSV; TALPAVKDSVK; ALPAVKDSVKD; LPAVKDSVKDS; VSNPFFFVFPG; SNPFFFVFPGS; NPFFFVFPGSW; PFFFVFPGSWV; FFFVFPGSWVL; FFVFPGSWVLL; LPVYLRLLLPQ; PVYLRLLLPQD; VYLRLLLPQDF; YLRLLLPQDFQ; LRLLLPQDFQW; RLLLPQDFQWL; LLLPQDFQWLK; LLPQDFQWLKL; LPQDFQWLKLL; PQDFQWLKLLL; QDFQWLKLLLG; DFQWLKLLLGR; FQWLKLLLGRL; QWLKLLLGRLL; WLKLLLGRLLL; LKLLLGRLLLL; LLVLLGLLLGL; LVLLGLLLGLL; VLLGLLLGLLL; GISSLMIGITK; ISSLMIGITKF; SSLMIGITKFP; SLMIGITKFPL; ASISNQAWLWN; SISNQAWLWNC; ISNQAWLWNCL; SNQAWLWNCLT; NQAWLWNCLTQ; QAWLWNCLTQM; AWLWNCLTQMS; WLWNCLTQMST; LWNCLTQMSTM; WNCLTQMSTMI; NCLTQMSTMIF; CLTQMSTMIFC; LTQMSTMIFCF; TQMSTMIFCFL; QMSTMIFCFLV; ILLLIIFNTLI; LLLIIFNTLIL; LLIIFNTLILG; LIIFNTLILGI; IIFNTLILGIG; IFNTLILGIGV; FNTLILGIGVL; NTLILGIGVLL; TLILGIGVLLC; LILGIGVLLCL; ILGIGVLLCLL; LGIGVLLCLLL; GIGVLLCLLLF; IGVLLCLLLFP; GVLLCLLLFPR; VLLCLLLFPRL; LLCLLLFPRLC; LCLLLFPRLCG; CLLLFPRLCGM; LLLFPRLCGML; LLFPRLCGMLL; LFPRLCGMLLG; FPRLCGMLLGM; PRLCGMLLGMI; RLCGMLLGMIY; LCGMLLGMIYL; CGMLLGMIYLL; PHRNCREEQKD; HRNCREEQKDF; RNCREEQKDFL; NCREEQKDFLE; CREEQKDFLET; REEQKDFLETP; EEQKDFLETPW; EQKDFLETPWL; QKDFLETPWLD; KDFLETPWLDF; DFLETPWLDFW; FLETPWLDFWR; LETPWLDFWRK; ETPWLDFWRKL; TPWLDFWRKLP; PWLDFWRKLPG; WLDFWRKLPGQ; LDFWRKLPGQL; TFIIIFNNIIL; FIIIFNNIILI; IIIFNNIILIF; IIFNNIILIFP; IFNNIILIFPL; FNNIILIFPLL; NNIILIFPLLG; NIILIFPLLGP; IILIFPLLGPQ; ILIFPLLGPQW; LIFPLLGPQWL; IFPLLGPQWLD; FPLLGPQWLDK; LKGKVPVYILA; KGKVPVYILAI; GKVPVYILAIL; KVPVYILAILI; VPVYILAILIV; EINKVYIQESL; KKLLPQEVLIK; KLLPQEVLIKE; LLPQEVLIKEL; LPQEVLIKELL; PQEVLIKELLL; QEVLIKELLLN; EVLIKELLLNG; VLIKELLLNGC; LIKELLLNGCC; IKELLLNGCCL; KELLLNGCCLY; ELLLNGCCLYF; HLLLKHMKMAP; LLLKHMKMAPT; LLKHMKMAPTK; LKHMKMAPTKR; KHMKMAPTKRK; HMKMAPTKRKG; MKMAPTKRKGE; KMAPTKRKGEC; MAPTKRKGECP; APTKRKGECPG; PTKRKGECPGA; TKRKGECPGAA; KRKGECPGAAP; RKGECPGAAPK; KGECPGAAPKK; GECPGAAPKKP; ECPGAAPKKPK; CPGAAPKKPKE; PGAAPKKPKEP; GAAPKKPKEPV; AAPKKPKEPVQ; APKKPKEPVQV; PKKPKEPVQVP; KKPKEPVQVPK; KPKEPVQVPKL; PKEPVQVPKLL; KEPVQVPKLLI; EPVQVPKLLIK; PVQVPKLLIKG; VQVPKLLIKGG; QVPKLLIKGGV; VPKLLIKGGVE; PKLLIKGGVEV; KLLIKGGVEVL; LLIKGGVEVLE; LIKGGVEVLEV; IKGGVEVLEVK; KGGVEVLEVKT; GGVEVLEVKTG; GVEVLEVKTGV; VEVLEVKTGVD; EVLEVKTGVDA; VLEVKTGVDAI; LEVKTGVDAIT; EVKTGVDAITE; VKTGVDAITEV; KTGVDAITEVE; TGVDAITEVEC; GVDAITEVECF; VDAITEVECFL; DAITEVECFLN; AITEVECFLNP; ITEVECFLNPE; TEVECFLNPEM; EVECFLNPEMG; VECFLNPEMGD; ECFLNPEMGDP; CFLNPEMGDPD; FLNPEMGDPDE; LNPEMGDPDEN; NPEMGDPDENL; PEMGDPDENLR; EMGDPDENLRG; MGDPDENLRGF; GDPDENLRGFS; DPDENLRGFSL; PDENLRGFSLK; DENLRGFSLKL; ENLRGFSLKLS; NLRGFSLKLSA; LRGFSLKLSAE; RGFSLKLSAEN; GFSLKLSAEND; FSLKLSAENDF; SLKLSAENDFS; LKLSAENDFSS; KLSAENDFSSD; LSAENDFSSDS; SAENDFSSDSP; AENDFSSDSPE; ENDFSSDSPER; NDFSSDSPERK; DFSSDSPERKM; FSSDSPERKML; SSDSPERKMLP; SDSPERKMLPC; DSPERKMLPCY; SPERKMLPCYS; PERKMLPCYST; ERKMLPCYSTA; RKMLPCYSTAR; KMLPCYSTARI; MLPCYSTARIP; LPCYSTARIPL; PCYSTARIPLP; CYSTARIPLPN; YSTARIPLPNL; STARIPLPNLN; TARIPLPNLNE; ARIPLPNLNED; RIPLPNLNEDL; IPLPNLNEDLT; PLPNLNEDLTC; LPNLNEDLTCG; PNLNEDLTCGN; NLNEDLTCGNL; LNEDLTCGNLL; NEDLTCGNLLM; EDLTCGNLLMW; DLTCGNLLMWE; LTCGNLLMWEA; TCGNLLMWEAV; CGNLLMWEAVT; GNLLMWEAVTV; NLLMWEAVTVQ; LLMWEAVTVQT; LMWEAVTVQTE; MWEAVTVQTEV; WEAVTVQTEVI; EAVTVQTEVIG; AVTVQTEVIGI; VTVQTEVIGIT; TVQTEVIGITS; VQTEVIGITSM; QTEVIGITSML; TEVIGITSMLN; EVIGITSMLNL; VIGITSMLNLH; IGITSMLNLHA; GITSMLNLHAG; ITSMLNLHAGS; TSMLNLHAGSQ; SMLNLHAGSQK; MLNLHAGSQKV; LNLHAGSQKVH; NLHAGSQKVHE; LHAGSQKVHEH; HAGSQKVHEHG; AGSQKVHEHGG; GSQKVHEHGGG; SQKVHEHGGGK; QKVHEHGGGKP; KVHEHGGGKPI; VHEHGGGKPIQ; HEHGGGKPIQG; EHGGGKPIQGS; HGGGKPIQGSN; GGGKPIQGSNF; GGKPIQGSNFH; GKPIQGSNFHF; KPIQGSNFHFF; PIQGSNFHFFA; IQGSNFHFFAV; QGSNFHFFAVG; GSNFHFFAVGG; SNFHFFAVGGE; NFHFFAVGGEP; FHFFAVGGEPL; HFFAVGGEPLE; FFAVGGEPLEM; FAVGGEPLEMQ; AVGGEPLEMQG; VGGEPLEMQGV; GGEPLEMQGVL; GEPLEMQGVLM; EPLEMQGVLMN; PLEMQGVLMNY; LEMQGVLMNYR; EMQGVLMNYRS; MQGVLMNYRSK; QGVLMNYRSKY; GVLMNYRSKYP; VLMNYRSKYPD; LMNYRSKYPDG; MNYRSKYPDGT; NYRSKYPDGTI; YRSKYPDGTIT; RSKYPDGTITP; SKYPDGTITPK; KYPDGTITPKN; YPDGTITPKNP; PDGTITPKNPT; DGTITPKNPTA; GTITPKNPTAQ; TITPKNPTAQS; ITPKNPTAQSQ; TPKNPTAQSQV; PKNPTAQSQVM; KNPTAQSQVMN; NPTAQSQVMNT; PTAQSQVMNTD; TAQSQVMNTDH; AQSQVMNTDHK; QSQVMNTDHKA; SQVMNTDHKAY; QVMNTDHKAYL; VMNTDHKAYLD; MNTDHKAYLDK; NTDHKAYLDKN; TDHKAYLDKNN; DHKAYLDKNNA; HKAYLDKNNAY; KAYLDKNNAYP; AYLDKNNAYPV; YLDKNNAYPVE; LDKNNAYPVEC; DKNNAYPVECW; KNNAYPVECWV; NNAYPVECWVP; NAYPVECWVPD; AYPVECWVPDP; YPVECWVPDPS; PVECWVPDPSR; VECWVPDPSRN; ECWVPDPSRNE; CWVPDPSRNEN; WVPDPSRNENA; VPDPSRNENAR; PDPSRNENARY; DPSRNENARYF; PSRNENARYFG; SRNENARYFGT; RNENARYFGTF; NENARYFGTFT; ENARYFGTFTG; NARYFGTFTGG; ARYFGTFTGGE; RYFGTFTGGEN; YFGTFTGGENV; FGTFTGGENVP; GTFTGGENVPP; TFTGGENVPPV; FTGGENVPPVL; TGGENVPPVLH; GGENVPPVLHV; GENVPPVLHVT; ENVPPVLHVTN; NVPPVLHVTNT; VPPVLHVTNTA; PPVLHVTNTAT; PVLHVTNTATT; VLHVTNTATTV; LHVTNTATTVL; HVTNTATTVLL; VTNTATTVLLD; TNTATTVLLDE; NTATTVLLDEQ; TATTVLLDEQG; ATTVLLDEQGV; TTVLLDEQGVG; TVLLDEQGVGP; VLLDEQGVGPL; LLDEQGVGPLC; LDEQGVGPLCK; DEQGVGPLCKA; EQGVGPLCKAD; QGVGPLCKADS; GVGPLCKADSL; VGPLCKADSLY; GPLCKADSLYV; PLCKADSLYVS; LCKADSLYVSA; CKADSLYVSAA; KADSLYVSAAD; ADSLYVSAADI; DSLYVSAADIC; SLYVSAADICG; LYVSAADICGL; YVSAADICGLF; VSAADICGLFT; SAADICGLFTN; AADICGLFTNS; ADICGLFTNSS; DICGLFTNSSG; ICGLFTNSSGT; CGLFTNSSGTQ; GLFTNSSGTQQ; LFTNSSGTQQW; FTNSSGTQQWR; TNSSGTQQWRG; NSSGTQQWRGL; SSGTQQWRGLA; SGTQQWRGLAR; GTQQWRGLARY; TQQWRGLARYF; QQWRGLARYFK; QWRGLARYFKI; WRGLARYFKIR; RGLARYFKIRL; GLARYFKIRLR; LARYFKIRLRK; ARYFKIRLRKR; RYFKIRLRKRS; YFKIRLRKRSV; FKIRLRKRSVK; KIRLRKRSVKN; IRLRKRSVKNP; RLRKRSVKNPY; LRKRSVKNPYP; RKRSVKNPYPI; KRSVKNPYPIS; RSVKNPYPISF; SVKNPYPISFL; VKNPYPISFLL; KNPYPISFLLS; NPYPISFLLSD; PYPISFLLSDL; YPISFLLSDLI; PISFLLSDLIN; ISFLLSDLINR; SFLLSDLINRR; FLLSDLINRRT; LLSDLINRRTQ; LSDLINRRTQR; SDLINRRTQRV; DLINRRTQRVD; LINRRTQRVDG; INRRTQRVDGQ; NRRTQRVDGQP; RRTQRVDGQPM; RTQRVDGQPMY; TQRVDGQPMYG; QRVDGQPMYGM; RVDGQPMYGME; VDGQPMYGMES; DGQPMYGMESQ; GQPMYGMESQV; QPMYGMESQVE; PMYGMESQVEE; MYGMESQVEEV; YGMESQVEEVR; GMESQVEEVRV; MESQVEEVRVF; ESQVEEVRVFD; SQVEEVRVFDG; QVEEVRVFDGT; VEEVRVFDGTE; EEVRVFDGTER; EVRVFDGTERL; VRVFDGTERLP; RVFDGTERLPG; VFDGTERLPGD; FDGTERLPGDP; DGTERLPGDPD; GTERLPGDPDM; TERLPGDPDMI; ERLPGDPDMIR; RLPGDPDMIRY; LPGDPDMIRYI; PGDPDMIRYID; GDPDMIRYIDK; DPDMIRYIDKQ; PDMIRYIDKQG; DMIRYIDKQGQ; MIRYIDKQGQL; IRYIDKQGQLQ; RYIDKQGQLQT; YIDKQGQLQTK; IDKQGQLQTKM; DKQGQLQTKML; TGAFIVHIHLI; GAFIVHIHLIN; AFIVHIHLINA; FIVHIHLINAA; IVHIHLINAAF; VHIHLINAAFV; ATFKLVLFWGW; TFKLVLFWGWC; FKLVLFWGWCF; KLVLFWGWCFR; LVLFWGWCFRP; VLFWGWCFRPF; LFWGWCFRPFK; FWGWCFRPFKT; WGWCFRPFKTL; GWCFRPFKTLK; WCFRPFKTLKA; CFRPFKTLKAF; FRPFKTLKAFT; RPFKTLKAFTQ; PFKTLKAFTQM; FKTLKAFTQMQ; KTLKAFTQMQL; TLKAFTQMQLL; LKAFTQMQLLT; KAFTQMQLLTM; AFTQMQLLTMG; FTQMQLLTMGV; ILFSCNIKNTF; LFSCNIKNTFP; FSCNIKNTFPH; SCNIKNTFPHA; CNIKNTFPHAY; NIKNTFPHAYI; IKNTFPHAYII; KNTFPHAYIIF; NTFPHAYIIFH; TFPHAYIIFHP; KSIHTYLRIQP; SIHTYLRIQPF; IHTYLRIQPFL; HTYLRIQPFLP; TYLRIQPFLPF; YLRIQPFLPFN; LRIQPFLPFNN; RIQPFLPFNNS; IQPFLPFNNSR; QPFLPFNNSRL; PFLPFNNSRLY; FLPFNNSRLYI; LPFNNSRLYIS; PFNNSRLYISC; FNNSRLYISCK; NNSRLYISCKI; NSRLYISCKIS; SRLYISCKISY; RLYISCKISYR; LYISCKISYRP; YISCKISYRPK; ISCKISYRPKP; SCKISYRPKPN; IYFGPKIYLSY; YFGPKIYLSYK; FGPKIYLSYKS; GPKIYLSYKSS; PKIYLSYKSSL; KIYLSYKSSLQ; IYLSYKSSLQG; YLSYKSSLQGF; LSYKSSLQGFR; SYKSSLQGFRD; YKSSLQGFRDR; KSSLQGFRDRI; SSLQGFRDRIL; SLQGFRDRILI; LQGFRDRILIH; QGFRDRILIHC; GFRDRILIHCN; FRDRILIHCNQ; RDRILIHCNQA; DRILIHCNQAW; RILIHCNQAWW; ILIHCNQAWWK; LIHCNQAWWKY; IHCNQAWWKYL; HCNQAWWKYLG; CNQAWWKYLGS; NQAWWKYLGSF; QAWWKYLGSFV; FSSCPFYIFKN; SSCPFYIFKNN; SCPFYIFKNNH; CPFYIFKNNHV; PFYIFKNNHVL; FYIFKNNHVLI; YIFKNNHVLIY; IFKNNHVLIYS; FKNNHVLIYSY; KNNHVLIYSYT; CCFSTINGTFK; PVSSFRYIENN; VSSFRYIENNT; SSFRYIENNTV; SFRYIENNTVQ; FRYIENNTVQK; RYIENNTVQKI; YIENNTVQKIK; IENNTVQKIKY; ENNTVQKIKYY; NNTVQKIKYYR; NTVQKIKYYRI; TVQKIKYYRIH; VQKIKYYRIHF; QKIKYYRIHFR; QTVQPSNTCHI; TVQPSNTCHIL; VQPSNTCHILF; HFFPGHMKGIY; FFPGHMKGIYS; FPGHMKGIYSF; PGHMKGIYSFF; GHMKGIYSFFS; NCIYCLLTNTF; CIYCLLTNTFL; IYCLLTNTFLI; YCLLTNTFLIF; CLLTNTFLIFT; LLTNTFLIFTF; LTNTFLIFTFC; TNTFLIFTFCK; NTFLIFTFCKN; TFLIFTFCKNN; FLIFTFCKNNS; LIFTFCKNNSI; IFTFCKNNSIC; FTFCKNNSICK; TFCKNNSICKV; FCKNNSICKVL; CKNNSICKVLF; KNNSICKVLFM; NNSICKVLFMI; NSICKVLFMIL; SICKVLFMILK; ICKVLFMILKV; CKVLFMILKVI; KVLFMILKVIR; VLFMILKVIRL; LFMILKVIRLV; FMILKVIRLVF; MILKVIRLVFF; ILKVIRLVFFL; LKVIRLVFFLT; KVIRLVFFLTL; VIRLVFFLTLF; IRLVFFLTLFT; RLVFFLTLFTL; LVFFLTLFTLL; VFFLTLFTLLY; FFLTLFTLLYI; FLTLFTLLYIV; LTLFTLLYIVL; TLFTLLYIVLK; LFTLLYIVLKF; KHILTLCLYCI; HILTLCLYCIL; ILTLCLYCILS; LTLCLYCILSN; FPRHLLCFFRL; PRHLLCFFRLF; RHLLCFFRLFW; HLLCFFRLFWA; LLCFFRLFWAK; LCFFRLFWAKI; CFFRLFWAKIM; FFRLFWAKIML; FRLFWAKIMLL; APLNAFFYSMV; PLNAFFYSMVW; LNAFFYSMVWI; NAFFYSMVWIS; AFFYSMVWISS; KTKGTQLLTEI; TKGTQLLTEII; KGTQLLTEIIN; GTQLLTEIINC; TQLLTEIINCR; QLLTEIINCRN; LLTEIINCRNS; LTEIINCRNSM; TEIINCRNSMS; EIINCRNSMSM; IINCRNSMSMW; INCRNSMSMWS; KEYNIMPSTHV; EYNIMPSTHVS; YNIMPSTHVST; NIMPSTHVSTN; IMPSTHVSTNK; MPSTHVSTNKS; PSTHVSTNKSY; STHVSTNKSYR; THVSTNKSYRI; HVSTNKSYRIF; VSTNKSYRIFF; STNKSYRIFFH; TNKSYRIFFHK; NKSYRIFFHKF; KSYRIFFHKFF; SYRIFFHKFFI; YRIFFHKFFIQ; RIFFHKFFIQN; IFFHKFFIQNL; FFHKFFIQNLS; FHKFFIQNLSF; HKFFIQNLSFF; KFFIQNLSFFF; FFIQNLSFFFS; FIQNLSFFFSS; IQNLSFFFSSI; QNLSFFFSSIH; NLSFFFSSIHS; LSFFFSSIHSK; SFFFSSIHSKA; FFFSSIHSKAG; FFSSIHSKAGK; FSSIHSKAGKG; SSIHSKAGKGS; SIHSKAGKGSI; IHSKAGKGSIT; HSKAGKGSITK; SKAGKGSITKY; KAGKGSITKYS; AGKGSITKYSL; GKGSITKYSLT; KGSITKYSLTK; GSITKYSLTKK; SITKYSLTKKL; ITKYSLTKKLV; IRGKVFRVFYL; RGKVFRVFYLS; GKVFRVFYLSF; KVFRVFYLSFF; VFRVFYLSFFF; FRVFYLSFFFG; RVFYLSFFFGW; VFYLSFFFGWC; VLRICCCFFIT; LRICCCFFITG; RICCCFFITGK; ICCCFFITGKH; CCCFFITGKHI; CCFFITGKHIF; CFFITGKHIFM; FFITGKHIFMA; FITGKHIFMAK; IFIPFFIKGTP; FIPFFIKGTPP; IPFFIKGTPPG; PFFIKGTPPGL; FFIKGTPPGLP; FIKGTPPGLPL; IKGTPPGLPLF; KGTPPGLPLFC; GTPPGLPLFCS; TPPGLPLFCSI; PPGLPLFCSIG; PGLPLFCSIGW; GLPLFCSIGWH; LPLFCSIGWHL; SFRSLKGVSPI; FRSLKGVSPII; RSLKGVSPIIW; SLKGVSPIIWT; LKGVSPIIWTH; KGVSPIIWTHH; GVSPIIWTHHC; VSPIIWTHHCR; SPIIWTHHCRV; PIIWTHHCRVS; IIWTHHCRVSS; IWTHHCRVSSV; WTHHCRVSSVR; THHCRVSSVRS; HHCRVSSVRSK; HCRVSSVRSKP; CRVSSVRSKPN; RVSSVRSKPNH; VSSVRSKPNHC; SSVRSKPNHCV; SVRSKPNHCVK; VRSKPNHCVKQ; RSKPNHCVKQS; SKPNHCVKQSM; KPNHCVKQSMQ; QSIQTKGSFLK; SIQTKGSFLKN; IQTKGSFLKNF; QTKGSFLKNFL; TKGSFLKNFLF; KGSFLKNFLFK; GSFLKNFLFKC; SFLKNFLFKCL; FLKNFLFKCLN; LKNFLFKCLNL; KNFLFKCLNLS; HSMQGQCTEGF; SMQGQCTEGFL; MQGQCTEGFLE; QGQCTEGFLEQ; GQCTEGFLEQI; QCTEGFLEQIG; CTEGFLEQIGH; TEGFLEQIGHS; EGFLEQIGHSL; GFLEQIGHSLQ; FLEQIGHSLQY; LEQIGHSLQYR; EQIGHSLQYRV; QIGHSLQYRVS; IGHSLQYRVSG; GHSLQYRVSGQ; HSLQYRVSGQR; SLQYRVSGQRG; LQYRVSGQRGK; QYRVSGQRGKS; YRVSGQRGKSA; RVSGQRGKSAQ; VSGQRGKSAQT; SGQRGKSAQTS; GQRGKSAQTSE; QRGKSAQTSEL; RGKSAQTSELL; GKSAQTSELLQ; KSAQTSELLQV; SAQTSELLQVP; AQTSELLQVPK; QTSELLQVPKS; TSELLQVPKSG; ATFTSCSIFLY; TFTSCSIFLYK; FTSCSIFLYKV; TSCSIFLYKVF; SCSIFLYKVFI; CSIFLYKVFIL; SIFLYKVFILF; IFLYKVFILFI; FLYKVFILFIL; LYKVFILFILS; YKVFILFILSS; KVFILFILSSS; VFILFILSSSP; FILFILSSSPP; ILFILSSSPPL; LFILSSSPPLS; FILSSSPPLSG; AFLIKGRFPQA; FLIKGRFPQAA; LIKGRFPQAAL; IKGRFPQAALS; KGRFPQAALSR; GRFPQAALSRP; RFPQAALSRPK; FPQAALSRPKR; PQAALSRPKRS; QAALSRPKRSM; AALSRPKRSMS; ALSRPKRSMSS; LSRPKRSMSSM; SRPKRSMSSMD; RPKRSMSSMDS; PKRSMSSMDSS; KRSMSSMDSSL; RSMSSMDSSLL; SMSSMDSSLLR; MSSMDSSLLRT; SSMDSSLLRTL; SMDSSLLRTLS BK virus reading frame 2 8 mers: GFPQIVLL; FPQIVLLG; PQIVLLGL; QIVLLGLR; IVLLGLRK; VLLGLRKS; LLGLRKSL; LGLRKSLH; GLRKSLHT; LRKSLHTL; RKSLHTLT; KSLHTLTT; EKGWRQRR; KGWRQRRP; GWRQRRPR; WRQRRPRP; RQRRPRPL; QRRPRPLI; RRPRPLIY; RPRPLIYY; PRPLIYYK; RPLIYYKK; PLIYYKKK; LIYYKKKG; IYYKKKGH; YYKKKGHR; YKKKGHRE; KKKGHREE; KKGHREEL; KGHREELL; GHREELLT; HREELLTH; REELLTHG; EELLTHGM; ELLTHGMQ; LLTHGMQP; LTHGMQPN; THGMQPNH; HGMQPNHD; GMQPNHDL; MQPNHDLR; QPNHDLRK; PNHDLRKE; NHDLRKES; HDLRKESA; LTGECSQT; TGECSQTM; GECSQTMT; ECSQTMTS; CSQTMTSG; SQTMTSGR; QTMTSGRK; TMTSGRKV; MTSGRKVH; TSGRKVHD; SGRKVHDS; GRKVHDSQ; RKVHDSQG; KVHDSQGG; VHDSQGGA; HDSQGGAA; DSQGGAAY; SQGGAAYP; QGGAAYPW; GGAAYPWN; GAAYPWNA; AAYPWNAA; AYPWNAAK; YPWNAAKP; PQEGKCMT; QEGKCMTD; EGKCMTDM; GKCMTDMF; KCMTDMFC; CMTDMFCE; MTDMFCEP; TDMFCEPR; DMFCEPRN; MFCEPRNL; FCEPRNLG; CEPRNLGL; EPRNLGLV; PRNLGLVP; RNLGLVPS; TGQRPWFC; GQRPWFCA; QRPWFCAS; RPWFCASC; PWFCASCH; WFCASCHD; FCASCHDK; CASCHDKL; ASCHDKLQ; KLVKPGLE; LVKPGLEQ; VKPGLEQK; KPGLEQKK; PGLEQKKE; GLEQKKEL; LEQKKELR; EQKKELRG; QKKELRGF; KKELRGFL; KELRGFLF; ELRGFLFL; LRGFLFLF; SFCWNFVE; FCWNFVEV; CWNFVEVK; WNFVEVKT; NFVEVKTV; TGKTKVPL; GKTKVPLL; KTKVPLLY; TKVPLLYL; KVPLLYLL; VIPFFLYF; IPFFLYFQ; PFFLYFQV; FFLYFQVH; FLYFQVHG; LYFQVHGC; YFQVHGCC; FQVHGCCS; QVHGCCSS; VHGCCSST; HGCCSSTF; GCCSSTFG; CCSSTFGG; CSSTFGGP; SSTFGGPS; STFGGPSC; TFGGPSCQ; FGGPSCQC; GGPSCQCI; GCCCHRIF; CCCHRIFS; CCHRIFSG; NCCWGGCC; CCWGGCCC; CWGGCCCY; WGGCCCYR; GGCCCYRS; GCCCYRSS; CCCYRSSN; CCYRSSNC; CYRSSNCI; YRSSNCIP; RSSNCIPC; SSNCIPCY; SNCIPCYC; NCIPCYCR; CIPCYCRG; IPCYCRGH; PCYCRGHN; CYCRGHNK; YCRGHNKY; CRGHNKYL; RGHNKYLR; GHNKYLRG; HNKYLRGY; NKYLRGYS; KYLRGYSC; YLRGYSCY; LRGYSCYR; RGYSCYRP; GYSCYRPN; YSCYRPNS; SCYRPNSS; CYRPNSSN; YRPNSSNI; RPNSSNIC; PNSSNICC; NSSNICCN; SSNICCNC; SNICCNCW; NICCNCWC; ICCNCWCS; CCNCWCSW; CNCWCSWG; NCWCSWGY; CWCSWGYC; WCSWGYCW; CSWGYCWV; SWGYCWVC; WGYCWVCC; GYCWVCCF; YCWVCCFN; CWVCCFNS; WVCCFNSN; VCCFNSNC; LGSQSFHC; GSQSFHCR; SQSFHCRP; QSFHCRPL; SFHCRPLS; FHCRPLSA; HCRPLSAI; CRPLSAIR; RPLSAIRH; PLSAIRHG; LSAIRHGF; SAIRHGFG; AIRHGFGI; IRHGFGIV; YSVSWCKY; SVSWCKYF; VSWCKYFC; ALGSFFVC; LGSFFVCY; GSFFVCYY; SFFVCYYF; FFVCYYFP; FVCYYFPG; VCYYFPGF; CYYFPGFV; YYFPGFVA; YFPGFVAC; FPGFVACY; YTFYNLTG; TFYNLTGI; FYNLTGIA; YNLTGIAE; NLTGIAEK; LTGIAEKN; TGIAEKNR; GIAEKNRK; IAEKNRKI; AEKNRKIF; IFGGNYLD; FGGNYLDN; GGNYLDNC; GNYLDNCK; NYLDNCKC; YLDNCKCP; LDNCKCPY; DNCKCPYK; NCKCPYKL; CKCPYKLL; KGRYPCTF; GRYPCTFW; RYPCTFWP; YPCTFWPY; PCTFWPYL; QYRRSYTK; YRRSYTKN; RRSYTKNG; RSYTKNGL; SYTKNGLK; YTKNGLKK; TKNGLKKS; KNGLKKST; NGLKKSTK; GLKKSTKC; LKKSTKCT; KKSTKCTF; KSTKCTFR; STKCTFRR; TKCTFRRV; KCTFRRVY; CTFRRVYR; TFRRVYRK; FRRVYRKN; RRVYRKNY; RVYRKNYC; VYRKNYCP; YRKNYCPR; RKNYCPRR; KNYCPRRC; SKNCSSMD; KNCSSMDV; NCSSMDVA; CSSMDVAF; SSMDVAFT; SMDVAFTS; MDVAFTSR; DVAFTSRP; VAFTSRPV; AFTSRPVR; FTSRPVRD; TSRPVRDC; SRPVRDCN; RPVRDCNT; PVRDCNTC; VRDCNTCS; RWPQPKEK; WPQPKEKE; PQPKEKES; QPKEKESV; PKEKESVQ; KEKESVQG; EKESVQGQ; KESVQGQL; ESVQGQLP; SVQGQLPK; VQGQLPKS; QGQLPKSQ; GQLPKSQR; QLPKSQRN; LPKSQRNP; PKSQRNPC; KSQRNPCK; SQRNPCKC; QRNPCKCQ; RNPCKCQN; NPCKCQNY; TQKWGIQM; QKWGIQMK; KWGIQMKT; WGIQMKTL; GIQMKTLG; IQMKTLGA; QMKTLGAL; MKTLGALV; VLKMTLAV; LKMTLAVI; KMTLAVIA; MTLAVIAQ; TLAVIAQR; LAVIAQRE; AVIAQREK; VIAQREKC; IAQREKCF; AQREKCFP; QREKCFPV; REKCFPVT; EKCFPVTA; KCFPVTAQ; CFPVTAQQ; FPVTAQQE; PVTAQQEF; VTAQQEFP; TAQQEFPS; AQQEFPSP; QQEFPSPI; LYKQRLLE; LACLTFMQ; ACLTFMQG; CLTFMQGH; LTFMQGHK; TFMQGHKK; FMQGHKKC; MQGHKKCM; QGHKKCMS; GHKKCMSM; HKKCMSMV; KKCMSMVE; KCMSMVEE; CMSMVEEN; MSMVEENL; SMVEENLF; MVEENLFK; VEENLFKA; EENLFKAV; ENLFKAVI; NLFKAVIS; LFKAVIST; FKAVISTS; KAVISTSL; AVISTSLL; VENPWKCR; ENPWKCRE; NPWKCREC; ITGQSTLM; TGQSTLMV; GQSTLMVL; PLKTQQPS; LKTQQPSP; KTQQPSPR; ILTIRPIW; LTIRPIWT; TIRPIWTK; IRPIWTKT; RPIWTKTM; PIWTKTML; IWTKTMLI; WTKTMLIQ; TKTMLIQL; KTMLIQLS; TMLIQLSA; MLIQLSAG; LIQLSAGY; IQLSAGYL; QLSAGYLI; LSAGYLIP; SAGYLIPV; AGYLIPVE; GYLIPVEM; YLIPVEMK; LIPVEMKM; IPVEMKML; PVEMKMLG; VEMKMLGI; EMKMLGIL; MKMLGILG; KMLGILGL; MLGILGLS; LGILGLSQ; GILGLSQE; ILGLSQEG; LGLSQEGK; GLSQEGKM; LSQEGKMF; SQEGKMFP; QEGKMFPQ; EGKMFPQY; GKMFPQYF; KMFPQYFM; PTQLPQCC; MNRVWGLF; NRVWGLFV; RVWGLFVK; VWGLFVKL; WGLFVKLI; GLFVKLIA; LFVKLIAC; FVKLIACM; VKLIACMF; KLIACMFQ; LIACMFQL; IACMFQLL; ACMFQLLI; CMFQLLIF; MFQLLIFV; FQLLIFVA; QLLIFVAC; LLIFVACL; LIFVACLL; IFVACLLT; FVACLLTA; VACLLTAL; ACLLTALE; CLLTALEH; LLTALEHN; LTALEHNS; TALEHNSG; ALEHNSGE; LEHNSGEA; EHNSGEAL; HNSGEALQ; NSGEALQD; SGEALQDI; GEALQDIL; EALQDILR; ALQDILRS; LQDILRSA; RILTQFPF; ILTQFPFC; TGEPREWM; GEPREWMG; EPREWMGS; PREWMGSL; REWMGSLC; EWMGSLCM; WMGSLCMV; MGSLCMVW; GSLCMVWN; SLCMVWNP; LCMVWNPR; KRLGCLMA; RLGCLMAQ; LGCLMAQK; GCLMAQKD; CLMAQKDF; LMAQKDFQ; MAQKDFQG; AQKDFQGT; QKDFQGTQ; KDFQGTQI; DILTNRDN; ILTNRDNC; LTNRDNCK; TNRDNCKP; NRDNCKPK; RDNCKPKC; DNCKPKCF; NCKPKCFK; CKPKCFKQ; KPKCFKQV; PKCFKQVL; KCFKQVLL; CFKQVLLL; FKQVLLLY; KQVLLLYI; QVLLLYIY; VLLLYIYI; MLLLYKPL; LLLYKPLL; LLYKPLLS; LYKPLLSL; YKPLLSLC; KPLLSLCY; PLLSLCYF; LLSLCYFG; LSLCYFGG; SLCYFGGG; LCYFGGGV; CYFGGGVL; YFGGGVLG; FGGGVLGL; GGGVLGLL; GGVLGLLK; GVLGLLKH; KPLHKCNS; LWGSDLWE; WGSDLWES; GSDLWESS; SDLWESSA; DLWESSAG; LWESSAGA; WESSAGAE; ESSAGAEV; SSAGAEVS; SAGAEVSE; AGAEVSET; GAEVSETW; AEVSETWE; EVSETWEE; VSETWEEH; SETWEEHC; ETWEEHCD; TWEEHCDW; WEEHCDWD; EEHCDWDS; EHCDWDSV; HCDWDSVL; CDWDSVLD; DWDSVLDP; WDSVLDPC; DSVLDPCP; SVLDPCPE; VLDPCPES; LDPCPESS; DPCPESSV; PCPESSVS; CPESSVSE; PESSVSES; ESSVSESS; SSVSESSS; SVSESSSL; VSESSSLV; SESSSLVI; ESSSLVIS; SSSLVISR; SSLVISRI; SLVISRIH; LVISRIHF; VISRIHFP; ISRIHFPM; SRIHFPMH; RIHFPMHI; IHFPMHIL; HFPMHILY; FPMHILYF; PMHILYFI; MHILYFIL; HILYFILE; ILYFILEK; LYFILEKV; YFILEKVY; FILEKVYI; ILEKVYIL; LEKVYILI; EKVYILIS; KVYILISE; VYILISES; YILISESS; ILISESSL; LISESSLS; ISESSLSF; SESSLSFH; ESSLSFHS; SSLSFHST; SLSFHSTI; LSFHSTIL; SFHSTILD; FHSTILDC; HSTILDCI; STILDCIS; TILDCISV; ILDCISVA; LDCISVAK; DCISVAKS; CISVAKSA; ISVAKSAT; SVAKSATG; VAKSATGL; AKSATGLN; KSATGLNQ; SATGLNQI; ATGLNQIS; TGLNQISS; GLNQISSS; LNQISSSN; NQISSSNK; QISSSNKV; ISSSNKVI; SSSNKVIP; SSNKVIPL; SNKVIPLC; NKVIPLCK; KVIPLCKI; VIPLCKIL; IPLCKILF; PLCKILFS; LCKILFSS; CKILFSSK; KILFSSKN; ILFSSKNS; LFSSKNSE; FSSKNSEF; SSKNSEFC; SKNSEFCK; KNSEFCKD; NSEFCKDF; SEFCKDFL; EFCKDFLK; FCKDFLKY; CKDFLKYI; KDFLKYIL; DFLKYILG; FLKYILGL; LKYILGLK; KYILGLKS; YILGLKSI; ILGLKSIC; LGLKSICL; GLKSICLT; LKSICLTN; KSICLTNL; SICLTNLA; ICLTNLAC; CLTNLACR; LTNLACRV; TNLACRVL; NLACRVLG; LACRVLGT; ACRVLGTG; CRVLGTGY; RVLGTGYS; VLGTGYSF; LGTGYSFI; GTGYSFIV; TGYSFIVT; GYSFIVTK; YSFIVTKP; SFIVTKPG; FIVTKPGG; IVTKPGGN; VTKPGGNI; TKPGGNIW; KPGGNIWV; PGGNIWVL; GGNIWVLL; GNIWVLLF; NIWVLLFK; IWVLLFKC; WVLLFKCF; VLLFKCFF; LLFKCFFS; LFKCFFSK; FKCFFSKF; KCFFSKFT; CFFSKFTL; FFSKFTLT; FSKFTLTL; SKFTLTLP; KFTLTLPS; FTLTLPSK; SLKLSKLF; LKLSKLFI; KLSKLFIP; LSKLFIPC; SKLFIPCP; KLFIPCPE; LFIPCPEG; FIPCPEGK; IPCPEGKS; PCPEGKSF; CPEGKSFD; PEGKSFDS; EGKSFDSA; GKSFDSAP; KSFDSAPV; SFDSAPVP; FDSAPVPF; DSAPVPFT; SAPVPFTS; APVPFTSS; PVPFTSSK; VPFTSSKT; PFTSSKTT; FTSSKTTM; TSSKTTMY; SIATPSSK; IATPSSKV; ATPSSKVS; TPSSKVSL; PSSKVSLS; SSKVSLSM; SKVSLSMG; KVSLSMGR; VSLSMGRF; SLSMGRFT; LSMGRFTF; SMGRFTFK; MGRFTFKA; GRFTFKAL; RFTFKALP; FTFKALPP; TFKALPPH; FKALPPHK; KALPPHKS; ALPPHKSN; LPPHKSNN; PPHKSNNP; PHKSNNPA; HKSNNPAA; KSNNPAAS; SNNPAASV; NNPAASVV; NPAASVVF; PAASVVFP; AASVVFPL; ASVVFPLS; SVVFPLSM; VVFPLSMG; VFPLSMGP; FPLSMGPL; PLSMGPLN; LSMGPLNN; SMGPLNNQ; MGPLNNQY; GPLNNQYL; PLNNQYLL; LNNQYLLL; NNQYLLLG; NQYLLLGT; QYLLLGTL; YLLLGTLK; LLLGTLKT; LLGTLKTI; LGTLKTIQ; GTLKTIQC; TLKTIQCK; LKTIQCKK; KTIQCKKS; TIQCKKSN; IQCKKSNI; QCKKSNIT; CKKSNITE; KKSNITES; KSNITESI; SNITESIL; NITESILG; ITESILGS; TESILGSK; ESILGSKQ; SILGSKQC; ILGSKQCS; LGSKQCSQ; GSKQCSQA; SKQCSQAT; KQCSQATP; QCSQATPA; CSQATPAI; SQATPAIY; QATPAIYC; ATPAIYCS; TPAIYCSS; PAIYCSST; AIYCSSTA; IYCSSTAF; YCSSTAFP; APNIKSIL; PNIKSILS; NIKSILSN; IKSILSNI; LNLSVSIS; NLSVSISS; LSVSISSL; SVSISSLV; VSISSLVI; RVSTLFLA; VSTLFLAK; STLFLAKT; TLFLAKTV; LFLAKTVS; FLAKTVST; LAKTVSTA; AKTVSTAC; FLLSAKII; LLSAKIIA; LSAKIIAF; SAKIIAFA; AKIIAFAK; KIIAFAKC; IIAFAKCF; IAFAKCFS; HFLHSSTL; FLHSSTLY; NSKYIPNN; SKYIPNNK; KYIPNNKN; YIPNNKNT; IPNNKNTS; PNNKNTSS; NNKNTSSH; NKNTSSHF; KNTSSHFV; NTSSHFVS; TSSHFVST; SSHFVSTA; SHFVSTAY; HFVSTAYS; FVSTAYSV; VSTAYSVI; STAYSVIN; TAYSVINF; AYSVINFQ; YSVINFQD; SVINFQDT; VINFQDTC; INFQDTCF; NFQDTCFV; FQDTCFVS; QDTCFVSS; DTCFVSSG; TCFVSSGS; CFVSSGSS; FVSSGSSG; VSSGSSGL; SSGSSGLK; SGSSGLKS; GSSGLKSC; SSGLKSCS; SGLKSCSF; GLKSCSFK; LKSCSFKP; KSCSFKPP; MLSSIVWY; LSSIVWYG; SSIVWYGS; SIVWYGSL; IVWYGSLV; VWYGSLVK; WYGSLVKA; YGSLVKAL; GSLVKALY; SLVKALYS; LVKALYSK; VKALYSKY; KALYSKYS; ALYSKYSL; LYSKYSLL; YSKYSLLT; SKYSLLTP; KYSLLTPL; YSLLTPLQ; SLLTPLQI; LLTPLQIK; LTPLQIKK; TPLQIKKL; PLQIKKLK; LQIKKLKV; QIKKLKVH; IKKLKVHS; KKLKVHSF; QKLLIAET; KLLIAETL; LLIAETLC; LIAETLCL; IAETLCLC; AETLCLCG; ETLCLCGV; TLCLCGVK; LCLCGVKK; CLCGVKKN; LCGVKKNI; CGVKKNII; GVKKNIIL; VKKNIILC; KKNIILCP; KNIILCPA; NIILCPAH; IILCPAHM; ILCPAHMC; LCPAHMCL; CPAHMCLL; PAHMCLLI; AHMCLLIK; HMCLLIKV; MCLLIKVT; CLLIKVTE; LLIKVTEY; LIKVTEYF; IKVTEYFS; KVTEYFSI; VTEYFSIS; TEYFSISF; EYFSISFL; YFSISFLY; FSISFLYR; SISFLYRI; AFSLVVYT; FSLVVYTA; SLVVYTAK; LVVYTAKQ; VVYTAKQA; VYTAKQAR; YTAKQARV; TAKQARVL; AKQARVLL; KQARVLLL; QARVLLLN; ARVLLLNT; RVLLLNTA; LRNWCRSE; RNWCRSEG; NWCRSEGK; WCRSEGKS; CRSEGKSL; RSEGKSLG; SEGKSLGS; EGKSLGSS; GKSLGSST; KSLGSSTF; SLGSSTFL; LGSSTFLF; GSSTFLFF; SSTFLFFL; STFLFFLG; TFLFFLGG; FLFFLGGV; LFFLGGVE; FFLGGVEC; ESAVASSS; SAVASSSL; AVASSSLA; VASSSLAN; ASSSLANI; SSSLANIS; SSLANISS; SLANISSW; LANISSWQ; ANISSWQN; NISSWQNK; ISSWQNKS; SSWQNKSS; SWQNKSSS; WQNKSSSH; QNKSSSHF; NKSSSHFS; KSSSHFSL; SSSHFSLK; SSHFSLKE; SHFSLKEL; HFSLKELH; FSLKELHQ; SLKELHQD; LKELHQDS; KELHQDSH; ELHQDSHS; LHQDSHSS; HQDSHSSV; QDSHSSVP; VGTYKKNN; GTYKKNNY; TYKKNNYL; YKKNNYLG; KKNNYLGP; KNNYLGPF; NNYLGPFN; NYLGPFNI; YLGPFNIL; LGPFNILL; GPFNILLF; PFNILLFI; VSYLKALD; SYLKALDL; REFLQLFG; EFLQLFGP; FLQLFGPT; LQLFGPTI; QLFGPTIA; LFGPTIAE; FGPTIAEF; GPTIAEFL; PTIAEFLQ; TIAEFLQL; IAEFLQLG; AEFLQLGL; EFLQLGLS; FLQLGLSQ; LQLGLSQT; QLGLSQTT; LGLSQTTV; SSQCSSNL; SQCSSNLS; QCSSNLSK; CSSNLSKP; SSNLSKPR; SNLSKPRA; NLSKPRAL; LSKPRALF; SKPRALFL; KPRALFLK; PRALFLKI; RALFLKIF; ALFLKIFY; LFLKIFYL; FLKIFYLN; LKIFYLNA; KIFYLNAL; IFYLNALI; ADIACKGS; DIACKGSA; IACKGSAQ; ACKGSAQK; CKGSAQKA; KGSAQKAF; GSAQKAFW; SAQKAFWN; AQKAFWNK; AIPCSTGY; IPCSTGYL; PCSTGYLG; CSTGYLGK; STGYLGKE; TGYLGKEE; GYLGKEEN; YLGKEENQ; LGKEENQH; GKEENQHK; KEENQHKP; EENQHKPL; ENQHKPLS; NQHKPLSY; QHKPLSYS; HKPLSYSR; KPLSYSRF; PLSYSRFQ; LSYSRFQN; SYSRFQNQ; YSRFQNQA; SRFQNQAD; RFQNQADE; FQNQADEL; QNQADELP; NQADELPL; QADELPLH; ADELPLHP; DELPLHPA; ELPLHPAP; LPLHPAPF; PLHPAPFF; LHPAPFFY; HPAPFFYT; PAPFFYTK; APFFYTKY; PFFYTKYS; FFYTKYSF; FYTKYSFS; YTKYSFSS; TKYSFSSF; KYSFSSFY; YSFSSFYP; SFSSFYPR; FSSFYPRR; SSFYPRRP; SFYPRRPL; FYPRRPLC; YPRRPLCQ; PRRPLCQG; RRPLCQGE; RPLCQGEI; PLCQGEIP; LCQGEIPY; CQGEIPYT; QGEIPYTS; GEIPYTSL; EIPYTSLN; IPYTSLNK; PYTSLNKL; YTSLNKLF; TSLNKLFS; SLNKLFSL; LNKLFSLR; NKLFSLRE; KLFSLRED; LFSLREDF; FSLREDFP; SLREDFPR; LREDFPRQ; REDFPRQL; EDFPRQLF; DFPRQLFQ; FPRQLFQG; PRQLFQGL; RQLFQGLK; QLFQGLKG; LFQGLKGP 9 mers: GFPQIVLLG; FPQIVLLGL; PQIVLLGLR; QIVLLGLRK; IVLLGLRKS; VLLGLRKSL; LLGLRKSLH; LGLRKSLHT; GLRKSLHTL; LRKSLHTLT; RKSLHTLTT; EKGWRQRRP; KGWRQRRPR; GWRQRRPRP; WRQRRPRPL; RQRRPRPLI; QRRPRPLIY; RRPRPLIYY; RPRPLIYYK; PRPLIYYKK; RPLIYYKKK; PLIYYKKKG; LIYYKKKGH; IYYKKKGHR; YYKKKGHRE; YKKKGHREE; KKKGHREEL; KKGHREELL; KGHREELLT; GHREELLTH; HREELLTHG; REELLTHGM; EELLTHGMQ; ELLTHGMQP; LLTHGMQPN; LTHGMQPNH; THGMQPNHD; HGMQPNHDL; GMQPNHDLR; MQPNHDLRK; QPNHDLRKE; PNHDLRKES; NHDLRKESA; LTGECSQTM; TGECSQTMT; GECSQTMTS; ECSQTMTSG; CSQTMTSGR; SQTMTSGRK; QTMTSGRKV; TMTSGRKVH; MTSGRKVHD; TSGRKVHDS; SGRKVHDSQ; GRKVHDSQG; RKVHDSQGG; KVHDSQGGA; VHDSQGGAA; HDSQGGAAY; DSQGGAAYP; SQGGAAYPW; QGGAAYPWN; GGAAYPWNA; GAAYPWNAA; AAYPWNAAK; AYPWNAAKP; PQEGKCMTD; QEGKCMTDM; EGKCMTDMF; GKCMTDMFC; KCMTDMFCE; CMTDMFCEP; MTDMFCEPR; TDMFCEPRN; DMFCEPRNL; MFCEPRNLG; FCEPRNLGL; CEPRNLGLV; EPRNLGLVP; PRNLGLVPS; TGQRPWFCA; GQRPWFCAS; QRPWFCASC; RPWFCASCH; PWFCASCHD; WFCASCHDK; FCASCHDKL; CASCHDKLQ; KLVKPGLEQ; LVKPGLEQK; VKPGLEQKK; KPGLEQKKE; PGLEQKKEL; GLEQKKELR; LEQKKELRG; EQKKELRGF; QKKELRGFL; KKELRGFLF; KELRGFLFL; ELRGFLFLF; SFCWNFVEV; FCWNFVEVK; CWNFVEVKT; WNFVEVKTV; TGKTKVPLL; GKTKVPLLY; KTKVPLLYL; TKVPLLYLL; VIPFFLYFQ; IPFFLYFQV; PFFLYFQVH; FFLYFQVHG; FLYFQVHGC; LYFQVHGCC; YFQVHGCCS; FQVHGCCSS; QVHGCCSST; VHGCCSSTF; HGCCSSTFG; GCCSSTFGG; CCSSTFGGP; CSSTFGGPS; SSTFGGPSC; STFGGPSCQ; TFGGPSCQC; FGGPSCQCI; GCCCHRIFS; CCCHRIFSG; NCCWGGCCC; CCWGGCCCY; CWGGCCCYR; WGGCCCYRS; GGCCCYRSS; GCCCYRSSN; CCCYRSSNC; CCYRSSNCI; CYRSSNCIP; YRSSNCIPC; RSSNCIPCY; SSNCIPCYC; SNCIPCYCR; NCIPCYCRG; CIPCYCRGH; IPCYCRGHN; PCYCRGHNK; CYCRGHNKY; YCRGHNKYL; CRGHNKYLR; RGHNKYLRG; GHNKYLRGY; HNKYLRGYS; NKYLRGYSC; KYLRGYSCY; YLRGYSCYR; LRGYSCYRP; RGYSCYRPN; GYSCYRPNS; YSCYRPNSS; SCYRPNSSN; CYRPNSSNI; YRPNSSNIC; RPNSSNICC; PNSSNICCN; NSSNICCNC; SSNICCNCW; SNICCNCWC; NICCNCWCS; ICCNCWCSW; CCNCWCSWG; CNCWCSWGY; NCWCSWGYC; CWCSWGYCW; WCSWGYCWV; CSWGYCWVC; SWGYCWVCC; WGYCWVCCF; GYCWVCCFN; YCWVCCFNS; CWVCCFNSN; WVCCFNSNC; LGSQSFHCR; GSQSFHCRP; SQSFHCRPL; QSFHCRPLS; SFHCRPLSA; FHCRPLSAI; HCRPLSAIR; CRPLSAIRH; RPLSAIRHG; PLSAIRHGF; LSAIRHGFG; SAIRHGFGI; AIRHGFGIV; YSVSWCKYF; SVSWCKYFC; ALGSFFVCY; LGSFFVCYY; GSFFVCYYF; SFFVCYYFP; FFVCYYFPG; FVCYYFPGF; VCYYFPGFV; CYYFPGFVA; YYFPGFVAC; YFPGFVACY; YTFYNLTGI; TFYNLTGIA; FYNLTGIAE; YNLTGIAEK; NLTGIAEKN; LTGIAEKNR; TGIAEKNRK; GIAEKNRKI; IAEKNRKIF; IFGGNYLDN; FGGNYLDNC; GGNYLDNCK; GNYLDNCKC; NYLDNCKCP; YLDNCKCPY; LDNCKCPYK; DNCKCPYKL; NCKCPYKLL; KGRYPCTFW; GRYPCTFWP; RYPCTFWPY; YPCTFWPYL; QYRRSYTKN; YRRSYTKNG; RRSYTKNGL; RSYTKNGLK; SYTKNGLKK; YTKNGLKKS; TKNGLKKST; KNGLKKSTK; NGLKKSTKC; GLKKSTKCT; LKKSTKCTF; KKSTKCTFR; KSTKCTFRR; STKCTFRRV; TKCTFRRVY; KCTFRRVYR; CTFRRVYRK; TFRRVYRKN; FRRVYRKNY; RRVYRKNYC; RVYRKNYCP; VYRKNYCPR; YRKNYCPRR; RKNYCPRRC; SKNCSSMDV; KNCSSMDVA; NCSSMDVAF; CSSMDVAFT; SSMDVAFTS; SMDVAFTSR; MDVAFTSRP; DVAFTSRPV; VAFTSRPVR; AFTSRPVRD; FTSRPVRDC; TSRPVRDCN; SRPVRDCNT; RPVRDCNTC; PVRDCNTCS; RWPQPKEKE; WPQPKEKES; PQPKEKESV; QPKEKESVQ; PKEKESVQG; KEKESVQGQ; EKESVQGQL; KESVQGQLP; ESVQGQLPK; SVQGQLPKS; VQGQLPKSQ; QGQLPKSQR; GQLPKSQRN; QLPKSQRNP; LPKSQRNPC; PKSQRNPCK; KSQRNPCKC; SQRNPCKCQ; QRNPCKCQN; RNPCKCQNY; TQKWGIQMK; QKWGIQMKT; KWGIQMKTL; WGIQMKTLG; GIQMKTLGA; IQMKTLGAL; QMKTLGALV; VLKMTLAVI; LKMTLAVIA; KMTLAVIAQ; MTLAVIAQR; TLAVIAQRE; LAVIAQREK; AVIAQREKC; VIAQREKCF; IAQREKCFP; AQREKCFPV; QREKCFPVT; REKCFPVTA; EKCFPVTAQ; KCFPVTAQQ; CFPVTAQQE; FPVTAQQEF; PVTAQQEFP; VTAQQEFPS; TAQQEFPSP; AQQEFPSPI; LACLTFMQG; ACLTFMQGH; CLTFMQGHK; LTFMQGHKK; TFMQGHKKC; FMQGHKKCM; MQGHKKCMS; QGHKKCMSM; GHKKCMSMV; HKKCMSMVE; KKCMSMVEE; KCMSMVEEN; CMSMVEENL; MSMVEENLF; SMVEENLFK; MVEENLFKA; VEENLFKAV; EENLFKAVI; ENLFKAVIS; NLFKAVIST; LFKAVISTS; FKAVISTSL; KAVISTSLL; VENPWKCRE; ENPWKCREC; ITGQSTLMV; TGQSTLMVL; PLKTQQPSP; LKTQQPSPR; ILTIRPIWT; LTIRPIWTK; TIRPIWTKT; IRPIWTKTM; RPIWTKTML; PIWTKTMLI; IWTKTMLIQ; WTKTMLIQL; TKTMLIQLS; KTMLIQLSA; TMLIQLSAG; MLIQLSAGY; LIQLSAGYL; IQLSAGYLI; QLSAGYLIP; LSAGYLIPV; SAGYLIPVE; AGYLIPVEM; GYLIPVEMK; YLIPVEMKM; LIPVEMKML; IPVEMKMLG; PVEMKMLGI; VEMKMLGIL; EMKMLGILG; MKMLGILGL; KMLGILGLS; MLGILGLSQ; LGILGLSQE; GILGLSQEG; ILGLSQEGK; LGLSQEGKM; GLSQEGKMF; LSQEGKMFP; SQEGKMFPQ; QEGKMFPQY; EGKMFPQYF; GKMFPQYFM; MNRVWGLFV; NRVWGLFVK; RVWGLFVKL; VWGLFVKLI; WGLFVKLIA; GLFVKLIAC; LFVKLIACM; FVKLIACMF; VKLIACMFQ; KLIACMFQL; LIACMFQLL; IACMFQLLI; ACMFQLLIF; CMFQLLIFV; MFQLLIFVA; FQLLIFVAC; QLLIFVACL; LLIFVACLL; LIFVACLLT; IFVACLLTA; FVACLLTAL; VACLLTALE; ACLLTALEH; CLLTALEHN; LLTALEHNS; LTALEHNSG; TALEHNSGE; ALEHNSGEA; LEHNSGEAL; EHNSGEALQ; HNSGEALQD; NSGEALQDI; SGEALQDIL; GEALQDILR; EALQDILRS; ALQDILRSA; RILTQFPFC; TGEPREWMG; GEPREWMGS; EPREWMGSL; PREWMGSLC; REWMGSLCM; EWMGSLCMV; WMGSLCMVW; MGSLCMVWN; GSLCMVWNP; SLCMVWNPR; KRLGCLMAQ; RLGCLMAQK; LGCLMAQKD; GCLMAQKDF; CLMAQKDFQ; LMAQKDFQG; MAQKDFQGT; AQKDFQGTQ; QKDFQGTQI; DILTNRDNC; ILTNRDNCK; LTNRDNCKP; TNRDNCKPK; NRDNCKPKC; RDNCKPKCF; DNCKPKCFK; NCKPKCFKQ; CKPKCFKQV; KPKCFKQVL; PKCFKQVLL; KCFKQVLLL; CFKQVLLLY; FKQVLLLYI; KQVLLLYIY; QVLLLYIYI; MLLLYKPLL; LLLYKPLLS; LLYKPLLSL; LYKPLLSLC; YKPLLSLCY; KPLLSLCYF; PLLSLCYFG; LLSLCYFGG; LSLCYFGGG; SLCYFGGGV; LCYFGGGVL; CYFGGGVLG; YFGGGVLGL; FGGGVLGLL; GGGVLGLLK; GGVLGLLKH; LWGSDLWES; WGSDLWESS; GSDLWESSA; SDLWESSAG; DLWESSAGA; LWESSAGAE; WESSAGAEV; ESSAGAEVS; SSAGAEVSE; SAGAEVSET; AGAEVSETW; GAEVSETWE; AEVSETWEE; EVSETWEEH; VSETWEEHC; SETWEEHCD; ETWEEHCDW; TWEEHCDWD; WEEHCDWDS; EEHCDWDSV; EHCDWDSVL; HCDWDSVLD; CDWDSVLDP; DWDSVLDPC; WDSVLDPCP; DSVLDPCPE; SVLDPCPES; VLDPCPESS; LDPCPESSV; DPCPESSVS; PCPESSVSE; CPESSVSES; PESSVSESS; ESSVSESSS; SSVSESSSL; SVSESSSLV; VSESSSLVI; SESSSLVIS; ESSSLVISR; SSSLVISRI; SSLVISRIH; SLVISRIHF; LVISRIHFP; VISRIHFPM; ISRIHFPMH; SRIHFPMHI; RIHFPMHIL; IHFPMHILY; HFPMHILYF; FPMHILYFI; PMHILYFIL; MHILYFILE; HILYFILEK; ILYFILEKV; LYFILEKVY; YFILEKVYI; FILEKVYIL; ILEKVYILI; LEKVYILIS; EKVYILISE; KVYILISES; VYILISESS; YILISESSL; ILISESSLS; LISESSLSF; ISESSLSFH; SESSLSFHS; ESSLSFHST; SSLSFHSTI; SLSFHSTIL; LSFHSTILD; SFHSTILDC; FHSTILDCI; HSTILDCIS; STILDCISV; TILDCISVA; ILDCISVAK; LDCISVAKS; DCISVAKSA; CISVAKSAT; ISVAKSATG; SVAKSATGL; VAKSATGLN; AKSATGLNQ; KSATGLNQI; SATGLNQIS; ATGLNQISS; TGLNQISSS; GLNQISSSN; LNQISSSNK; NQISSSNKV; QISSSNKVI; ISSSNKVIP; SSSNKVIPL; SSNKVIPLC; SNKVIPLCK; NKVIPLCKI; KVIPLCKIL; VIPLCKILF; IPLCKILFS; PLCKILFSS; LCKILFSSK; CKILFSSKN; KILFSSKNS; ILFSSKNSE; LFSSKNSEF; FSSKNSEFC; SSKNSEFCK; SKNSEFCKD; KNSEFCKDF; NSEFCKDFL; SEFCKDFLK; EFCKDFLKY; FCKDFLKYI; CKDFLKYIL; KDFLKYILG; DFLKYILGL; FLKYILGLK; LKYILGLKS; KYILGLKSI; YILGLKSIC; ILGLKSICL; LGLKSICLT; GLKSICLTN; LKSICLTNL; KSICLTNLA; SICLTNLAC; ICLTNLACR; CLTNLACRV; LTNLACRVL; TNLACRVLG; NLACRVLGT; LACRVLGTG; ACRVLGTGY; CRVLGTGYS; RVLGTGYSF; VLGTGYSFI; LGTGYSFIV; GTGYSFIVT; TGYSFIVTK; GYSFIVTKP; YSFIVTKPG; SFIVTKPGG; FIVTKPGGN; IVTKPGGNI; VTKPGGNIW; TKPGGNIWV; KPGGNIWVL; PGGNIWVLL; GGNIWVLLF; GNIWVLLFK; NIWVLLFKC; IWVLLFKCF; WVLLFKCFF; VLLFKCFFS; LLFKCFFSK; LFKCFFSKF; FKCFFSKFT; KCFFSKFTL; CFFSKFTLT; FFSKFTLTL; FSKFTLTLP; SKFTLTLPS; KFTLTLPSK; SLKLSKLFI; LKLSKLFIP; KLSKLFIPC; LSKLFIPCP; SKLFIPCPE; KLFIPCPEG; LFIPCPEGK; FIPCPEGKS; IPCPEGKSF; PCPEGKSFD; CPEGKSFDS; PEGKSFDSA; EGKSFDSAP; GKSFDSAPV; KSFDSAPVP; SFDSAPVPF; FDSAPVPFT; DSAPVPFTS; SAPVPFTSS; APVPFTSSK; PVPFTSSKT; VPFTSSKTT; PFTSSKTTM; FTSSKTTMY; SIATPSSKV; IATPSSKVS; ATPSSKVSL; TPSSKVSLS; PSSKVSLSM; SSKVSLSMG; SKVSLSMGR; KVSLSMGRF; VSLSMGRFT; SLSMGRFTF; LSMGRFTFK; SMGRFTFKA; MGRFTFKAL; GRFTFKALP; RFTFKALPP; FTFKALPPH; TFKALPPHK; FKALPPHKS; KALPPHKSN; ALPPHKSNN; LPPHKSNNP; PPHKSNNPA; PHKSNNPAA; HKSNNPAAS; KSNNPAASV; SNNPAASVV; NNPAASVVF; NPAASVVFP; PAASVVFPL; AASVVFPLS; ASVVFPLSM; SVVFPLSMG; VVFPLSMGP; VFPLSMGPL; FPLSMGPLN; PLSMGPLNN; LSMGPLNNQ; SMGPLNNQY; MGPLNNQYL; GPLNNQYLL; PLNNQYLLL; LNNQYLLLG; NNQYLLLGT; NQYLLLGTL; QYLLLGTLK; YLLLGTLKT; LLLGTLKTI; LLGTLKTIQ; LGTLKTIQC; GTLKTIQCK; TLKTIQCKK; LKTIQCKKS; KTIQCKKSN; TIQCKKSNI; IQCKKSNIT; QCKKSNITE; CKKSNITES; KKSNITESI; KSNITESIL; SNITESILG; NITESILGS; ITESILGSK; TESILGSKQ; ESILGSKQC; SILGSKQCS; ILGSKQCSQ; LGSKQCSQA; GSKQCSQAT; SKQCSQATP; KQCSQATPA; QCSQATPAI; CSQATPAIY; SQATPAIYC; QATPAIYCS; ATPAIYCSS; TPAIYCSST; PAIYCSSTA; AIYCSSTAF; IYCSSTAFP; APNIKSILS; PNIKSILSN; NIKSILSNI; LNLSVSISS; NLSVSISSL; LSVSISSLV; SVSISSLVI; RVSTLFLAK; VSTLFLAKT; STLFLAKTV; TLFLAKTVS; LFLAKTVST; FLAKTVSTA; LAKTVSTAC; FLLSAKIIA; LLSAKIIAF; LSAKIIAFA; SAKIIAFAK; AKIIAFAKC; KIIAFAKCF; IIAFAKCFS; HFLHSSTLY; NSKYIPNNK; SKYIPNNKN; KYIPNNKNT; YIPNNKNTS; IPNNKNTSS; PNNKNTSSH; NNKNTSSHF; NKNTSSHFV; KNTSSHFVS; NTSSHFVST; TSSHFVSTA; SSHFVSTAY; SHFVSTAYS; HFVSTAYSV; FVSTAYSVI; VSTAYSVIN; STAYSVINF; TAYSVINFQ; AYSVINFQD; YSVINFQDT; SVINFQDTC; VINFQDTCF; INFQDTCFV; NFQDTCFVS; FQDTCFVSS; QDTCFVSSG; DTCFVSSGS; TCFVSSGSS; CFVSSGSSG; FVSSGSSGL; VSSGSSGLK; SSGSSGLKS; SGSSGLKSC; GSSGLKSCS; SSGLKSCSF; SGLKSCSFK; GLKSCSFKP; LKSCSFKPP; MLSSIVWYG; LSSIVWYGS; SSIVWYGSL; SIVWYGSLV; IVWYGSLVK; VWYGSLVKA; WYGSLVKAL; YGSLVKALY; GSLVKALYS; SLVKALYSK; LVKALYSKY; VKALYSKYS; KALYSKYSL; ALYSKYSLL; LYSKYSLLT; YSKYSLLTP; SKYSLLTPL; KYSLLTPLQ; YSLLTPLQI; SLLTPLQIK; LLTPLQIKK; LTPLQIKKL; TPLQIKKLK; PLQIKKLKV; LQIKKLKVH; QIKKLKVHS; IKKLKVHSF; QKLLIAETL; KLLIAETLC; LLIAETLCL; LIAETLCLC; IAETLCLCG; AETLCLCGV; ETLCLCGVK; TLCLCGVKK; LCLCGVKKN; CLCGVKKNI; LCGVKKNII; CGVKKNIIL; GVKKNIILC; VKKNIILCP; KKNIILCPA; KNIILCPAH; NIILCPAHM; IILCPAHMC; ILCPAHMCL; LCPAHMCLL; CPAHMCLLI; PAHMCLLIK; AHMCLLIKV; HMCLLIKVT; MCLLIKVTE; CLLIKVTEY; LLIKVTEYF; LIKVTEYFS; IKVTEYFSI; KVTEYFSIS; VTEYFSISF; TEYFSISFL; EYFSISFLY; YFSISFLYR; FSISFLYRI; AFSLVVYTA; FSLVVYTAK; SLVVYTAKQ; LVVYTAKQA; VVYTAKQAR; VYTAKQARV; YTAKQARVL; TAKQARVLL; AKQARVLLL; KQARVLLLN; QARVLLLNT; ARVLLLNTA; LRNWCRSEG; RNWCRSEGK; NWCRSEGKS; WCRSEGKSL; CRSEGKSLG; RSEGKSLGS; SEGKSLGSS; EGKSLGSST; GKSLGSSTF; KSLGSSTFL; SLGSSTFLF; LGSSTFLFF; GSSTFLFFL; SSTFLFFLG; STFLFFLGG; TFLFFLGGV; FLFFLGGVE; LFFLGGVEC; ESAVASSSL; SAVASSSLA; AVASSSLAN; VASSSLANI; ASSSLANIS; SSSLANISS; SSLANISSW; SLANISSWQ; LANISSWQN; ANISSWQNK; NISSWQNKS; ISSWQNKSS; SSWQNKSSS; SWQNKSSSH; WQNKSSSHF; QNKSSSHFS; NKSSSHFSL; KSSSHFSLK; SSSHFSLKE; SSHFSLKEL; SHFSLKELH; HFSLKELHQ; FSLKELHQD; SLKELHQDS; LKELHQDSH; KELHQDSHS; ELHQDSHSS; LHQDSHSSV; HQDSHSSVP; VGTYKKNNY; GTYKKNNYL; TYKKNNYLG; YKKNNYLGP; KKNNYLGPF; KNNYLGPFN; NNYLGPFNI; NYLGPFNIL; YLGPFNILL; LGPFNILLF; GPFNILLFI; VSYLKALDL; REFLQLFGP; EFLQLFGPT; FLQLFGPTI; LQLFGPTIA; QLFGPTIAE; LFGPTIAEF; FGPTIAEFL; GPTIAEFLQ; PTIAEFLQL; TIAEFLQLG; IAEFLQLGL; AEFLQLGLS; EFLQLGLSQ; FLQLGLSQT; LQLGLSQTT; QLGLSQTTV; SSQCSSNLS; SQCSSNLSK; QCSSNLSKP; CSSNLSKPR; SSNLSKPRA; SNLSKPRAL; NLSKPRALF; LSKPRALFL; SKPRALFLK; KPRALFLKI; PRALFLKIF; RALFLKIFY; ALFLKIFYL; LFLKIFYLN; FLKIFYLNA; LKIFYLNAL; KIFYLNALI; ADIACKGSA; DIACKGSAQ; IACKGSAQK; ACKGSAQKA; CKGSAQKAF; KGSAQKAFW; GSAQKAFWN; SAQKAFWNK; AIPCSTGYL; IPCSTGYLG; PCSTGYLGK; CSTGYLGKE; STGYLGKEE; TGYLGKEEN; GYLGKEENQ; YLGKEENQH; LGKEENQHK; GKEENQHKP; KEENQHKPL; EENQHKPLS; ENQHKPLSY; NQHKPLSYS; QHKPLSYSR; HKPLSYSRF; KPLSYSRFQ; PLSYSRFQN; LSYSRFQNQ; SYSRFQNQA; YSRFQNQAD; SRFQNQADE; RFQNQADEL; FQNQADELP; QNQADELPL; NQADELPLH; QADELPLHP; ADELPLHPA; DELPLHPAP; ELPLHPAPF; LPLHPAPFF; PLHPAPFFY; LHPAPFFYT; HPAPFFYTK; PAPFFYTKY; APFFYTKYS; PFFYTKYSF; FFYTKYSFS; FYTKYSFSS; YTKYSFSSF; TKYSFSSFY; KYSFSSFYP; YSFSSFYPR; SFSSFYPRR; FSSFYPRRP; SSFYPRRPL; SFYPRRPLC; FYPRRPLCQ; YPRRPLCQG; PRRPLCQGE; RRPLCQGEI; RPLCQGEIP; PLCQGEIPY; LCQGEIPYT; CQGEIPYTS; QGEIPYTSL; GEIPYTSLN; EIPYTSLNK; IPYTSLNKL; PYTSLNKLF; YTSLNKLFS; TSLNKLFSL; SLNKLFSLR; LNKLFSLRE; NKLFSLRED; KLFSLREDF; LFSLREDFP; FSLREDFPR; SLREDFPRQ; LREDFPRQL; REDFPRQLF; EDFPRQLFQ; DFPRQLFQG; FPRQLFQGL; PRQLFQGLK; RQLFQGLKG; QLFQGLKGP 10 mers: GFPQIVLLGL; FPQIVLLGLR; PQIVLLGLRK; QIVLLGLRKS; IVLLGLRKSL; VLLGLRKSLH; LLGLRKSLHT; LGLRKSLHTL; GLRKSLHTLT; LRKSLHTLTT; EKGWRQRRPR; KGWRQRRPRP; GWRQRRPRPL; WRQRRPRPLI; RQRRPRPLIY; QRRPRPLIYY; RRPRPLIYYK; RPRPLIYYKK; PRPLIYYKKK; RPLIYYKKKG; PLIYYKKKGH; LIYYKKKGHR; IYYKKKGHRE; YYKKKGHREE; YKKKGHREEL; KKKGHREELL; KKGHREELLT; KGHREELLTH; GHREELLTHG; HREELLTHGM; REELLTHGMQ; EELLTHGMQP; ELLTHGMQPN; LLTHGMQPNH; LTHGMQPNHD; THGMQPNHDL; HGMQPNHDLR; GMQPNHDLRK; MQPNHDLRKE; QPNHDLRKES; PNHDLRKESA; LTGECSQTMT; TGECSQTMTS; GECSQTMTSG; ECSQTMTSGR; CSQTMTSGRK; SQTMTSGRKV; QTMTSGRKVH; TMTSGRKVHD; MTSGRKVHDS; TSGRKVHDSQ; SGRKVHDSQG; GRKVHDSQGG; RKVHDSQGGA; KVHDSQGGAA; VHDSQGGAAY; HDSQGGAAYP; DSQGGAAYPW; SQGGAAYPWN; QGGAAYPWNA; GGAAYPWNAA; GAAYPWNAAK; AAYPWNAAKP; PQEGKCMTDM; QEGKCMTDMF; EGKCMTDMFC; GKCMTDMFCE; KCMTDMFCEP; CMTDMFCEPR; MTDMFCEPRN; TDMFCEPRNL; DMFCEPRNLG; MFCEPRNLGL; FCEPRNLGLV; CEPRNLGLVP; EPRNLGLVPS; TGQRPWFCAS; GQRPWFCASC; QRPWFCASCH; RPWFCASCHD; PWFCASCHDK; WFCASCHDKL; FCASCHDKLQ; KLVKPGLEQK; LVKPGLEQKK; VKPGLEQKKE; KPGLEQKKEL; PGLEQKKELR; GLEQKKELRG; LEQKKELRGF; EQKKELRGFL; QKKELRGFLF; KKELRGFLFL; KELRGFLFLF; SFCWNFVEVK; FCWNFVEVKT; CWNFVEVKTV; TGKTKVPLLY; GKTKVPLLYL; KTKVPLLYLL; VIPFFLYFQV; IPFFLYFQVH; PFFLYFQVHG; FFLYFQVHGC; FLYFQVHGCC; LYFQVHGCCS; YFQVHGCCSS; FQVHGCCSST; QVHGCCSSTF; VHGCCSSTFG; HGCCSSTFGG; GCCSSTFGGP; CCSSTFGGPS; CSSTFGGPSC; SSTFGGPSCQ; STFGGPSCQC; TFGGPSCQCI; GCCCHRIFSG; NCCWGGCCCY; CCWGGCCCYR; CWGGCCCYRS; WGGCCCYRSS; GGCCCYRSSN; GCCCYRSSNC; CCCYRSSNCI; CCYRSSNCIP; CYRSSNCIPC; YRSSNCIPCY; RSSNCIPCYC; SSNCIPCYCR; SNCIPCYCRG; NCIPCYCRGH; CIPCYCRGHN; IPCYCRGHNK; PCYCRGHNKY; CYCRGHNKYL; YCRGHNKYLR; CRGHNKYLRG; RGHNKYLRGY; GHNKYLRGYS; HNKYLRGYSC; NKYLRGYSCY; KYLRGYSCYR; YLRGYSCYRP; LRGYSCYRPN; RGYSCYRPNS; GYSCYRPNSS; YSCYRPNSSN; SCYRPNSSNI; CYRPNSSNIC; YRPNSSNICC; RPNSSNICCN; PNSSNICCNC; NSSNICCNCW; SSNICCNCWC; SNICCNCWCS; NICCNCWCSW; ICCNCWCSWG; CCNCWCSWGY; CNCWCSWGYC; NCWCSWGYCW; CWCSWGYCWV; WCSWGYCWVC; CSWGYCWVCC; SWGYCWVCCF; WGYCWVCCFN; GYCWVCCFNS; YCWVCCFNSN; CWVCCFNSNC; LGSQSFHCRP; GSQSFHCRPL; SQSFHCRPLS; QSFHCRPLSA; SFHCRPLSAI; FHCRPLSAIR; HCRPLSAIRH; CRPLSAIRHG; RPLSAIRHGF; PLSAIRHGFG; LSAIRHGFGI; SAIRHGFGIV; YSVSWCKYFC; ALGSFFVCYY; LGSFFVCYYF; GSFFVCYYFP; SFFVCYYFPG; FFVCYYFPGF; FVCYYFPGFV; VCYYFPGFVA; CYYFPGFVAC; YYFPGFVACY; YTFYNLTGIA; TFYNLTGIAE; FYNLTGIAEK; YNLTGIAEKN; NLTGIAEKNR; LTGIAEKNRK; TGIAEKNRKI; GIAEKNRKIF; IFGGNYLDNC; FGGNYLDNCK; GGNYLDNCKC; GNYLDNCKCP; NYLDNCKCPY; YLDNCKCPYK; LDNCKCPYKL; DNCKCPYKLL; KGRYPCTFWP; GRYPCTFWPY; RYPCTFWPYL; QYRRSYTKNG; YRRSYTKNGL; RRSYTKNGLK; RSYTKNGLKK; SYTKNGLKKS; YTKNGLKKST; TKNGLKKSTK; KNGLKKSTKC; NGLKKSTKCT; GLKKSTKCTF; LKKSTKCTFR; KKSTKCTFRR; KSTKCTFRRV; STKCTFRRVY; TKCTFRRVYR; KCTFRRVYRK; CTFRRVYRKN; TFRRVYRKNY; FRRVYRKNYC; RRVYRKNYCP; RVYRKNYCPR; VYRKNYCPRR; YRKNYCPRRC; SKNCSSMDVA; KNCSSMDVAF; NCSSMDVAFT; CSSMDVAFTS; SSMDVAFTSR; SMDVAFTSRP; MDVAFTSRPV; DVAFTSRPVR; VAFTSRPVRD; AFTSRPVRDC; FTSRPVRDCN; TSRPVRDCNT; SRPVRDCNTC; RPVRDCNTCS; RWPQPKEKES; WPQPKEKESV; PQPKEKESVQ; QPKEKESVQG; PKEKESVQGQ; KEKESVQGQL; EKESVQGQLP; KESVQGQLPK; ESVQGQLPKS; SVQGQLPKSQ; VQGQLPKSQR; QGQLPKSQRN; GQLPKSQRNP; QLPKSQRNPC; LPKSQRNPCK; PKSQRNPCKC; KSQRNPCKCQ; SQRNPCKCQN; QRNPCKCQNY; TQKWGIQMKT; QKWGIQMKTL; KWGIQMKTLG; WGIQMKTLGA; GIQMKTLGAL; IQMKTLGALV; VLKMTLAVIA; LKMTLAVIAQ; KMTLAVIAQR; MTLAVIAQRE; TLAVIAQREK; LAVIAQREKC; AVIAQREKCF; VIAQREKCFP; IAQREKCFPV; AQREKCFPVT; QREKCFPVTA; REKCFPVTAQ; EKCFPVTAQQ; KCFPVTAQQE; CFPVTAQQEF; FPVTAQQEFP; PVTAQQEFPS; VTAQQEFPSP; TAQQEFPSPI; LACLTFMQGH; ACLTFMQGHK; CLTFMQGHKK; LTFMQGHKKC; TFMQGHKKCM; FMQGHKKCMS; MQGHKKCMSM; QGHKKCMSMV; GHKKCMSMVE; HKKCMSMVEE; KKCMSMVEEN; KCMSMVEENL; CMSMVEENLF; MSMVEENLFK; SMVEENLFKA; MVEENLFKAV; VEENLFKAVI; EENLFKAVIS; ENLFKAVIST; NLFKAVISTS; LFKAVISTSL; FKAVISTSLL; VENPWKCREC; ITGQSTLMVL; PLKTQQPSPR; ILTIRPIWTK; LTIRPIWTKT; TIRPIWTKTM; IRPIWTKTML; RPIWTKTMLI; PIWTKTMLIQ; IWTKTMLIQL; WTKTMLIQLS; TKTMLIQLSA; KTMLIQLSAG; TMLIQLSAGY; MLIQLSAGYL; LIQLSAGYLI; IQLSAGYLIP; QLSAGYLIPV; LSAGYLIPVE; SAGYLIPVEM; AGYLIPVEMK; GYLIPVEMKM; YLIPVEMKML; LIPVEMKMLG; IPVEMKMLGI; PVEMKMLGIL; VEMKMLGILG; EMKMLGILGL; MKMLGILGLS; KMLGILGLSQ; MLGILGLSQE; LGILGLSQEG; GILGLSQEGK; ILGLSQEGKM; LGLSQEGKMF; GLSQEGKMFP; LSQEGKMFPQ; SQEGKMFPQY; QEGKMFPQYF; EGKMFPQYFM; MNRVWGLFVK; NRVWGLFVKL; RVWGLFVKLI; VWGLFVKLIA; WGLFVKLIAC; GLFVKLIACM; LFVKLIACMF; FVKLIACMFQ; VKLIACMFQL; KLIACMFQLL; LIACMFQLLI; IACMFQLLIF; ACMFQLLIFV; CMFQLLIFVA; MFQLLIFVAC; FQLLIFVACL; QLLIFVACLL; LLIFVACLLT; LIFVACLLTA; IFVACLLTAL; FVACLLTALE; VACLLTALEH; ACLLTALEHN; CLLTALEHNS; LLTALEHNSG; LTALEHNSGE; TALEHNSGEA; ALEHNSGEAL; LEHNSGEALQ; EHNSGEALQD; HNSGEALQDI; NSGEALQDIL; SGEALQDILR; GEALQDILRS; EALQDILRSA; TGEPREWMGS; GEPREWMGSL; EPREWMGSLC; PREWMGSLCM; REWMGSLCMV; EWMGSLCMVW; WMGSLCMVWN; MGSLCMVWNP; GSLCMVWNPR; KRLGCLMAQK; RLGCLMAQKD; LGCLMAQKDF; GCLMAQKDFQ; CLMAQKDFQG; LMAQKDFQGT; MAQKDFQGTQ; AQKDFQGTQI; DILTNRDNCK; ILTNRDNCKP; LTNRDNCKPK; TNRDNCKPKC; NRDNCKPKCF; RDNCKPKCFK; DNCKPKCFKQ; NCKPKCFKQV; CKPKCFKQVL; KPKCFKQVLL; PKCFKQVLLL; KCFKQVLLLY; CFKQVLLLYI; FKQVLLLYIY; KQVLLLYIYI; MLLLYKPLLS; LLLYKPLLSL; LLYKPLLSLC; LYKPLLSLCY; YKPLLSLCYF; KPLLSLCYFG; PLLSLCYFGG; LLSLCYFGGG; LSLCYFGGGV; SLCYFGGGVL; LCYFGGGVLG; CYFGGGVLGL; YFGGGVLGLL; FGGGVLGLLK; GGGVLGLLKH; LWGSDLWESS; WGSDLWESSA; GSDLWESSAG; SDLWESSAGA; DLWESSAGAE; LWESSAGAEV; WESSAGAEVS; ESSAGAEVSE; SSAGAEVSET; SAGAEVSETW; AGAEVSETWE; GAEVSETWEE; AEVSETWEEH; EVSETWEEHC; VSETWEEHCD; SETWEEHCDW; ETWEEHCDWD; TWEEHCDWDS; WEEHCDWDSV; EEHCDWDSVL; EHCDWDSVLD; HCDWDSVLDP; CDWDSVLDPC; DWDSVLDPCP; WDSVLDPCPE; DSVLDPCPES; SVLDPCPESS; VLDPCPESSV; LDPCPESSVS; DPCPESSVSE; PCPESSVSES; CPESSVSESS; PESSVSESSS; ESSVSESSSL; SSVSESSSLV; SVSESSSLVI; VSESSSLVIS; SESSSLVISR; ESSSLVISRI; SSSLVISRIH; SSLVISRIHF; SLVISRIHFP; LVISRIHFPM; VISRIHFPMH; ISRIHFPMHI; SRIHFPMHIL; RIHFPMHILY; IHFPMHILYF; HFPMHILYFI; FPMHILYFIL; PMHILYFILE; MHILYFILEK; HILYFILEKV; ILYFILEKVY; LYFILEKVYI; YFILEKVYIL; FILEKVYILI; ILEKVYILIS; LEKVYILISE; EKVYILISES; KVYILISESS; VYILISESSL; YILISESSLS; ILISESSLSF; LISESSLSFH; ISESSLSFHS; SESSLSFHST; ESSLSFHSTI; SSLSFHSTIL; SLSFHSTILD; LSFHSTILDC; SFHSTILDCI; FHSTILDCIS; HSTILDCISV; STILDCISVA; TILDCISVAK; ILDCISVAKS; LDCISVAKSA; DCISVAKSAT; CISVAKSATG; ISVAKSATGL; SVAKSATGLN; VAKSATGLNQ; AKSATGLNQI; KSATGLNQIS; SATGLNQISS; ATGLNQISSS; TGLNQISSSN; GLNQISSSNK; LNQISSSNKV; NQISSSNKVI; QISSSNKVIP; ISSSNKVIPL; SSSNKVIPLC; SSNKVIPLCK; SNKVIPLCKI; NKVIPLCKIL; KVIPLCKILF; VIPLCKILFS; IPLCKILFSS; PLCKILFSSK; LCKILFSSKN; CKILFSSKNS; KILFSSKNSE; ILFSSKNSEF; LFSSKNSEFC; FSSKNSEFCK; SSKNSEFCKD; SKNSEFCKDF; KNSEFCKDFL; NSEFCKDFLK; SEFCKDFLKY; EFCKDFLKYI; FCKDFLKYIL; CKDFLKYILG; KDFLKYILGL; DFLKYILGLK; FLKYILGLKS; LKYILGLKSI; KYILGLKSIC; YILGLKSICL; ILGLKSICLT; LGLKSICLTN; GLKSICLTNL; LKSICLTNLA; KSICLTNLAC; SICLTNLACR; ICLTNLACRV; CLTNLACRVL; LTNLACRVLG; TNLACRVLGT; NLACRVLGTG; LACRVLGTGY; ACRVLGTGYS; CRVLGTGYSF; RVLGTGYSFI; VLGTGYSFIV; LGTGYSFIVT; GTGYSFIVTK; TGYSFIVTKP; GYSFIVTKPG; YSFIVTKPGG; SFIVTKPGGN; FIVTKPGGNI; IVTKPGGNIW; VTKPGGNIWV; TKPGGNIWVL; KPGGNIWVLL; PGGNIWVLLF; GGNIWVLLFK; GNIWVLLFKC; NIWVLLFKCF; IWVLLFKCFF; WVLLFKCFFS; VLLFKCFFSK; LLFKCFFSKF; LFKCFFSKFT; FKCFFSKFTL; KCFFSKFTLT; CFFSKFTLTL; FFSKFTLTLP; FSKFTLTLPS; SKFTLTLPSK; SLKLSKLFIP; LKLSKLFIPC; KLSKLFIPCP; LSKLFIPCPE; SKLFIPCPEG; KLFIPCPEGK; LFIPCPEGKS; FIPCPEGKSF; IPCPEGKSFD; PCPEGKSFDS; CPEGKSFDSA; PEGKSFDSAP; EGKSFDSAPV; GKSFDSAPVP; KSFDSAPVPF; SFDSAPVPFT; FDSAPVPFTS; DSAPVPFTSS; SAPVPFTSSK; APVPFTSSKT; PVPFTSSKTT; VPFTSSKTTM; PFTSSKTTMY; SIATPSSKVS; IATPSSKVSL; ATPSSKVSLS; TPSSKVSLSM; PSSKVSLSMG; SSKVSLSMGR; SKVSLSMGRF; KVSLSMGRFT; VSLSMGRFTF; SLSMGRFTFK; LSMGRFTFKA; SMGRFTFKAL; MGRFTFKALP; GRFTFKALPP; RFTFKALPPH; FTFKALPPHK; TFKALPPHKS; FKALPPHKSN; KALPPHKSNN; ALPPHKSNNP; LPPHKSNNPA; PPHKSNNPAA; PHKSNNPAAS; HKSNNPAASV; KSNNPAASVV; SNNPAASVVF; NNPAASVVFP; NPAASVVFPL; PAASVVFPLS; AASVVFPLSM; ASVVFPLSMG; SVVFPLSMGP; VVFPLSMGPL; VFPLSMGPLN; FPLSMGPLNN; PLSMGPLNNQ; LSMGPLNNQY; SMGPLNNQYL; MGPLNNQYLL; GPLNNQYLLL; PLNNQYLLLG; LNNQYLLLGT; NNQYLLLGTL; NQYLLLGTLK; QYLLLGTLKT; YLLLGTLKTI; LLLGTLKTIQ; LLGTLKTIQC; LGTLKTIQCK; GTLKTIQCKK; TLKTIQCKKS; LKTIQCKKSN; KTIQCKKSNI; TIQCKKSNIT; IQCKKSNITE; QCKKSNITES; CKKSNITESI; KKSNITESIL; KSNITESILG; SNITESILGS; NITESILGSK; ITESILGSKQ; TESILGSKQC; ESILGSKQCS; SILGSKQCSQ; ILGSKQCSQA; LGSKQCSQAT; GSKQCSQATP; SKQCSQATPA; KQCSQATPAI; QCSQATPAIY; CSQATPAIYC; SQATPAIYCS; QATPAIYCSS; ATPAIYCSST; TPAIYCSSTA; PAIYCSSTAF; AIYCSSTAFP; APNIKSILSN; PNIKSILSNI; LNLSVSISSL; NLSVSISSLV; LSVSISSLVI; RVSTLFLAKT; VSTLFLAKTV; STLFLAKTVS; TLFLAKTVST; LFLAKTVSTA; FLAKTVSTAC; FLLSAKIIAF; LLSAKIIAFA; LSAKIIAFAK; SAKIIAFAKC; AKIIAFAKCF; KIIAFAKCFS; NSKYIPNNKN; SKYIPNNKNT; KYIPNNKNTS; YIPNNKNTSS; IPNNKNTSSH; PNNKNTSSHF; NNKNTSSHFV; NKNTSSHFVS; KNTSSHFVST; NTSSHFVSTA; TSSHFVSTAY; SSHFVSTAYS; SHFVSTAYSV; HFVSTAYSVI; FVSTAYSVIN; VSTAYSVINF; STAYSVINFQ; TAYSVINFQD; AYSVINFQDT; YSVINFQDTC; SVINFQDTCF; VINFQDTCFV; INFQDTCFVS; NFQDTCFVSS; FQDTCFVSSG; QDTCFVSSGS; DTCFVSSGSS; TCFVSSGSSG; CFVSSGSSGL; FVSSGSSGLK; VSSGSSGLKS; SSGSSGLKSC; SGSSGLKSCS; GSSGLKSCSF; SSGLKSCSFK; SGLKSCSFKP; GLKSCSFKPP; MLSSIVWYGS; LSSIVWYGSL; SSIVWYGSLV; SIVWYGSLVK; IVWYGSLVKA; VWYGSLVKAL; WYGSLVKALY; YGSLVKALYS; GSLVKALYSK; SLVKALYSKY; LVKALYSKYS; VKALYSKYSL; KALYSKYSLL; ALYSKYSLLT; LYSKYSLLTP; YSKYSLLTPL; SKYSLLTPLQ; KYSLLTPLQI; YSLLTPLQIK; SLLTPLQIKK; LLTPLQIKKL; LTPLQIKKLK; TPLQIKKLKV; PLQIKKLKVH; LQIKKLKVHS; QIKKLKVHSF; QKLLIAETLC; KLLIAETLCL; LLIAETLCLC; LIAETLCLCG; IAETLCLCGV; AETLCLCGVK; ETLCLCGVKK; TLCLCGVKKN; LCLCGVKKNI; CLCGVKKNII; LCGVKKNIIL; CGVKKNIILC; GVKKNIILCP; VKKNIILCPA; KKNIILCPAH; KNIILCPAHM; NIILCPAHMC; IILCPAHMCL; ILCPAHMCLL; LCPAHMCLLI; CPAHMCLLIK; PAHMCLLIKV; AHMCLLIKVT; HMCLLIKVTE; MCLLIKVTEY; CLLIKVTEYF; LLIKVTEYFS; LIKVTEYFSI; IKVTEYFSIS; KVTEYFSISF; VTEYFSISFL; TEYFSISFLY; EYFSISFLYR; YFSISFLYRI; AFSLVVYTAK; FSLVVYTAKQ; SLVVYTAKQA; LVVYTAKQAR; VVYTAKQARV; VYTAKQARVL; YTAKQARVLL; TAKQARVLLL; AKQARVLLLN; KQARVLLLNT; QARVLLLNTA; LRNWCRSEGK; RNWCRSEGKS; NWCRSEGKSL; WCRSEGKSLG; CRSEGKSLGS; RSEGKSLGSS; SEGKSLGSST; EGKSLGSSTF; GKSLGSSTFL; KSLGSSTFLF; SLGSSTFLFF; LGSSTFLFFL; GSSTFLFFLG; SSTFLFFLGG; STFLFFLGGV; TFLFFLGGVE; FLFFLGGVEC; ESAVASSSLA; SAVASSSLAN; AVASSSLANI; VASSSLANIS; ASSSLANISS; SSSLANISSW; SSLANISSWQ; SLANISSWQN; LANISSWQNK; ANISSWQNKS; NISSWQNKSS; ISSWQNKSSS; SSWQNKSSSH; SWQNKSSSHF; WQNKSSSHFS; QNKSSSHFSL; NKSSSHFSLK; KSSSHFSLKE; SSSHFSLKEL; SSHFSLKELH; SHFSLKELHQ; HFSLKELHQD; FSLKELHQDS; SLKELHQDSH; LKELHQDSHS; KELHQDSHSS; ELHQDSHSSV; LHQDSHSSVP; VGTYKKNNYL; GTYKKNNYLG; TYKKNNYLGP; YKKNNYLGPF; KKNNYLGPFN; KNNYLGPFNI; NNYLGPFNIL; NYLGPFNILL; YLGPFNILLF; LGPFNILLFI; REFLQLFGPT; EFLQLFGPTI; FLQLFGPTIA; LQLFGPTIAE; QLFGPTIAEF; LFGPTIAEFL; FGPTIAEFLQ; GPTIAEFLQL; PTIAEFLQLG; TIAEFLQLGL; IAEFLQLGLS; AEFLQLGLSQ; EFLQLGLSQT; FLQLGLSQTT; LQLGLSQTTV; SSQCSSNLSK; SQCSSNLSKP; QCSSNLSKPR; CSSNLSKPRA; SSNLSKPRAL; SNLSKPRALF; NLSKPRALFL; LSKPRALFLK; SKPRALFLKI; KPRALFLKIF; PRALFLKIFY; RALFLKIFYL; ALFLKIFYLN; LFLKIFYLNA; FLKIFYLNAL; LKIFYLNALI; ADIACKGSAQ; DIACKGSAQK; IACKGSAQKA; ACKGSAQKAF; CKGSAQKAFW; KGSAQKAFWN; GSAQKAFWNK; AIPCSTGYLG; IPCSTGYLGK; PCSTGYLGKE; CSTGYLGKEE; STGYLGKEEN; TGYLGKEENQ; GYLGKEENQH; YLGKEENQHK; LGKEENQHKP; GKEENQHKPL; KEENQHKPLS; EENQHKPLSY; ENQHKPLSYS; NQHKPLSYSR; QHKPLSYSRF; HKPLSYSRFQ; KPLSYSRFQN; PLSYSRFQNQ; LSYSRFQNQA; SYSRFQNQAD; YSRFQNQADE; SRFQNQADEL; RFQNQADELP; FQNQADELPL; QNQADELPLH; NQADELPLHP; QADELPLHPA; ADELPLHPAP; DELPLHPAPF; ELPLHPAPFF; LPLHPAPFFY; PLHPAPFFYT; LHPAPFFYTK; HPAPFFYTKY; PAPFFYTKYS; APFFYTKYSF; PFFYTKYSFS; FFYTKYSFSS; FYTKYSFSSF; YTKYSFSSFY; TKYSFSSFYP; KYSFSSFYPR; YSFSSFYPRR; SFSSFYPRRP; FSSFYPRRPL; SSFYPRRPLC; SFYPRRPLCQ; FYPRRPLCQG; YPRRPLCQGE; PRRPLCQGEI; RRPLCQGEIP; RPLCQGEIPY; PLCQGEIPYT; LCQGEIPYTS; CQGEIPYTSL; QGEIPYTSLN; GEIPYTSLNK; EIPYTSLNKL; IPYTSLNKLF; PYTSLNKLFS; YTSLNKLFSL; TSLNKLFSLR; SLNKLFSLRE; LNKLFSLRED; NKLFSLREDF; KLFSLREDFP; LFSLREDFPR; FSLREDFPRQ; SLREDFPRQL; LREDFPRQLF; REDFPRQLFQ; EDFPRQLFQG; DFPRQLFQGL; FPRQLFQGLK; PRQLFQGLKG; RQLFQGLKGP 11 mers: GFPQIVLLGLR; FPQIVLLGLRK; PQIVLLGLRKS; QIVLLGLRKSL; IVLLGLRKSLH; VLLGLRKSLHT; LLGLRKSLHTL; LGLRKSLHTLT; GLRKSLHTLTT; EKGWRQRRPRP; KGWRQRRPRPL; GWRQRRPRPLI; WRQRRPRPLIY; RQRRPRPLIYY; QRRPRPLIYYK; RRPRPLIYYKK; RPRPLIYYKKK; PRPLIYYKKKG; RPLIYYKKKGH; PLIYYKKKGHR; LIYYKKKGHRE; IYYKKKGHREE; YYKKKGHREEL; YKKKGHREELL; KKKGHREELLT; KKGHREELLTH; KGHREELLTHG; GHREELLTHGM; HREELLTHGMQ; REELLTHGMQP; EELLTHGMQPN; ELLTHGMQPNH; LLTHGMQPNHD; LTHGMQPNHDL; THGMQPNHDLR; HGMQPNHDLRK; GMQPNHDLRKE; MQPNHDLRKES; QPNHDLRKESA; LTGECSQTMTS; TGECSQTMTSG; GECSQTMTSGR; ECSQTMTSGRK; CSQTMTSGRKV; SQTMTSGRKVH; QTMTSGRKVHD; TMTSGRKVHDS; MTSGRKVHDSQ; TSGRKVHDSQG; SGRKVHDSQGG; GRKVHDSQGGA; RKVHDSQGGAA; KVHDSQGGAAY; VHDSQGGAAYP; HDSQGGAAYPW; DSQGGAAYPWN; SQGGAAYPWNA; QGGAAYPWNAA; GGAAYPWNAAK; GAAYPWNAAKP; PQEGKCMTDMF; QEGKCMTDMFC; EGKCMTDMFCE; GKCMTDMFCEP; KCMTDMFCEPR; CMTDMFCEPRN; MTDMFCEPRNL; TDMFCEPRNLG; DMFCEPRNLGL; MFCEPRNLGLV; FCEPRNLGLVP; CEPRNLGLVPS; TGQRPWFCASC; GQRPWFCASCH; QRPWFCASCHD; RPWFCASCHDK; PWFCASCHDKL; WFCASCHDKLQ; KLVKPGLEQKK; LVKPGLEQKKE; VKPGLEQKKEL; KPGLEQKKELR; PGLEQKKELRG; GLEQKKELRGF; LEQKKELRGFL; EQKKELRGFLF; QKKELRGFLFL; KKELRGFLFLF; SFCWNFVEVKT; FCWNFVEVKTV; TGKTKVPLLYL; GKTKVPLLYLL; VIPFFLYFQVH; IPFFLYFQVHG; PFFLYFQVHGC; FFLYFQVHGCC; FLYFQVHGCCS; LYFQVHGCCSS; YFQVHGCCSST; FQVHGCCSSTF; QVHGCCSSTFG; VHGCCSSTFGG; HGCCSSTFGGP; GCCSSTFGGPS; CCSSTFGGPSC; CSSTFGGPSCQ; SSTFGGPSCQC; STFGGPSCQCI; NCCWGGCCCYR; CCWGGCCCYRS; CWGGCCCYRSS; WGGCCCYRSSN; GGCCCYRSSNC; GCCCYRSSNCI; CCCYRSSNCIP; CCYRSSNCIPC; CYRSSNCIPCY; YRSSNCIPCYC; RSSNCIPCYCR; SSNCIPCYCRG; SNCIPCYCRGH; NCIPCYCRGHN; CIPCYCRGHNK; IPCYCRGHNKY; PCYCRGHNKYL; CYCRGHNKYLR; YCRGHNKYLRG; CRGHNKYLRGY; RGHNKYLRGYS; GHNKYLRGYSC; HNKYLRGYSCY; NKYLRGYSCYR; KYLRGYSCYRP; YLRGYSCYRPN; LRGYSCYRPNS; RGYSCYRPNSS; GYSCYRPNSSN; YSCYRPNSSNI; SCYRPNSSNIC; CYRPNSSNICC; YRPNSSNICCN; RPNSSNICCNC; PNSSNICCNCW; NSSNICCNCWC; SSNICCNCWCS; SNICCNCWCSW; NICCNCWCSWG; ICCNCWCSWGY; CCNCWCSWGYC; CNCWCSWGYCW; NCWCSWGYCWV; CWCSWGYCWVC; WCSWGYCWVCC; CSWGYCWVCCF; SWGYCWVCCFN; WGYCWVCCFNS; GYCWVCCFNSN; YCWVCCFNSNC; LGSQSFHCRPL; GSQSFHCRPLS; SQSFHCRPLSA; QSFHCRPLSAI; SFHCRPLSAIR; FHCRPLSAIRH; HCRPLSAIRHG; CRPLSAIRHGF; RPLSAIRHGFG; PLSAIRHGFGI; LSAIRHGFGIV; ALGSFFVCYYF; LGSFFVCYYFP; GSFFVCYYFPG; SFFVCYYFPGF; FFVCYYFPGFV; FVCYYFPGFVA; VCYYFPGFVAC; CYYFPGFVACY; YTFYNLTGIAE; TFYNLTGIAEK; FYNLTGIAEKN; YNLTGIAEKNR; NLTGIAEKNRK; LTGIAEKNRKI; TGIAEKNRKIF; IFGGNYLDNCK; FGGNYLDNCKC; GGNYLDNCKCP; GNYLDNCKCPY; NYLDNCKCPYK; YLDNCKCPYKL; LDNCKCPYKLL; KGRYPCTFWPY; GRYPCTFWPYL; QYRRSYTKNGL; YRRSYTKNGLK; RRSYTKNGLKK; RSYTKNGLKKS; SYTKNGLKKST; YTKNGLKKSTK; TKNGLKKSTKC; KNGLKKSTKCT; NGLKKSTKCTF; GLKKSTKCTFR; LKKSTKCTFRR; KKSTKCTFRRV; KSTKCTFRRVY; STKCTFRRVYR; TKCTFRRVYRK; KCTFRRVYRKN; CTFRRVYRKNY; TFRRVYRKNYC; FRRVYRKNYCP; RRVYRKNYCPR; RVYRKNYCPRR; VYRKNYCPRRC; SKNCSSMDVAF; KNCSSMDVAFT; NCSSMDVAFTS; CSSMDVAFTSR; SSMDVAFTSRP; SMDVAFTSRPV; MDVAFTSRPVR; DVAFTSRPVRD; VAFTSRPVRDC; AFTSRPVRDCN; FTSRPVRDCNT; TSRPVRDCNTC; SRPVRDCNTCS; RWPQPKEKESV; WPQPKEKESVQ; PQPKEKESVQG; QPKEKESVQGQ; PKEKESVQGQL; KEKESVQGQLP; EKESVQGQLPK; KESVQGQLPKS; ESVQGQLPKSQ; SVQGQLPKSQR; VQGQLPKSQRN; QGQLPKSQRNP; GQLPKSQRNPC; QLPKSQRNPCK; LPKSQRNPCKC; PKSQRNPCKCQ; KSQRNPCKCQN; SQRNPCKCQNY; TQKWGIQMKTL; QKWGIQMKTLG; KWGIQMKTLGA; WGIQMKTLGAL; GIQMKTLGALV; VLKMTLAVIAQ; LKMTLAVIAQR; KMTLAVIAQRE; MTLAVIAQREK; TLAVIAQREKC; LAVIAQREKCF; AVIAQREKCFP; VIAQREKCFPV; IAQREKCFPVT; AQREKCFPVTA; QREKCFPVTAQ; REKCFPVTAQQ; EKCFPVTAQQE; KCFPVTAQQEF; CFPVTAQQEFP; FPVTAQQEFPS; PVTAQQEFPSP; VTAQQEFPSPI; LACLTFMQGHK; ACLTFMQGHKK; CLTFMQGHKKC; LTFMQGHKKCM; TFMQGHKKCMS; FMQGHKKCMSM; MQGHKKCMSMV; QGHKKCMSMVE; GHKKCMSMVEE; HKKCMSMVEEN; KKCMSMVEENL; KCMSMVEENLF; CMSMVEENLFK; MSMVEENLFKA; SMVEENLFKAV; MVEENLFKAVI; VEENLFKAVIS; EENLFKAVIST; ENLFKAVISTS; NLFKAVISTSL; LFKAVISTSLL; ILTIRPIWTKT; LTIRPIWTKTM; TIRPIWTKTML; IRPIWTKTMLI; RPIWTKTMLIQ; PIWTKTMLIQL; IWTKTMLIQLS; WTKTMLIQLSA; TKTMLIQLSAG; KTMLIQLSAGY; TMLIQLSAGYL; MLIQLSAGYLI; LIQLSAGYLIP; IQLSAGYLIPV; QLSAGYLIPVE; LSAGYLIPVEM; SAGYLIPVEMK; AGYLIPVEMKM; GYLIPVEMKML; YLIPVEMKMLG; LIPVEMKMLGI; IPVEMKMLGIL; PVEMKMLGILG; VEMKMLGILGL; EMKMLGILGLS; MKMLGILGLSQ; KMLGILGLSQE; MLGILGLSQEG; LGILGLSQEGK; GILGLSQEGKM; ILGLSQEGKMF; LGLSQEGKMFP; GLSQEGKMFPQ; LSQEGKMFPQY; SQEGKMFPQYF; QEGKMFPQYFM; MNRVWGLFVKL; NRVWGLFVKLI; RVWGLFVKLIA; VWGLFVKLIAC; WGLFVKLIACM; GLFVKLIACMF; LFVKLIACMFQ; FVKLIACMFQL; VKLIACMFQLL; KLIACMFQLLI; LIACMFQLLIF; IACMFQLLIFV; ACMFQLLIFVA; CMFQLLIFVAC; MFQLLIFVACL; FQLLIFVACLL; QLLIFVACLLT; LLIFVACLLTA; LIFVACLLTAL; IFVACLLTALE; FVACLLTALEH; VACLLTALEHN; ACLLTALEHNS; CLLTALEHNSG; LLTALEHNSGE; LTALEHNSGEA; TALEHNSGEAL; ALEHNSGEALQ; LEHNSGEALQD; EHNSGEALQDI; HNSGEALQDIL; NSGEALQDILR; SGEALQDILRS; GEALQDILRSA; TGEPREWMGSL; GEPREWMGSLC; EPREWMGSLCM; PREWMGSLCMV; REWMGSLCMVW; EWMGSLCMVWN; WMGSLCMVWNP; MGSLCMVWNPR; KRLGCLMAQKD; RLGCLMAQKDF; LGCLMAQKDFQ; GCLMAQKDFQG; CLMAQKDFQGT; LMAQKDFQGTQ; MAQKDFQGTQI; DILTNRDNCKP; ILTNRDNCKPK; LTNRDNCKPKC; TNRDNCKPKCF; NRDNCKPKCFK; RDNCKPKCFKQ; DNCKPKCFKQV; NCKPKCFKQVL; CKPKCFKQVLL; KPKCFKQVLLL; PKCFKQVLLLY; KCFKQVLLLYI; CFKQVLLLYIY; FKQVLLLYIYI; MLLLYKPLLSL; LLLYKPLLSLC; LLYKPLLSLCY; LYKPLLSLCYF; YKPLLSLCYFG; KPLLSLCYFGG; PLLSLCYFGGG; LLSLCYFGGGV; LSLCYFGGGVL; SLCYFGGGVLG; LCYFGGGVLGL; CYFGGGVLGLL; YFGGGVLGLLK; FGGGVLGLLKH; LWGSDLWESSA; WGSDLWESSAG; GSDLWESSAGA; SDLWESSAGAE; DLWESSAGAEV; LWESSAGAEVS; WESSAGAEVSE; ESSAGAEVSET; SSAGAEVSETW; SAGAEVSETWE; AGAEVSETWEE; GAEVSETWEEH; AEVSETWEEHC; EVSETWEEHCD; VSETWEEHCDW; SETWEEHCDWD; ETWEEHCDWDS; TWEEHCDWDSV; WEEHCDWDSVL; EEHCDWDSVLD; EHCDWDSVLDP; HCDWDSVLDPC; CDWDSVLDPCP; DWDSVLDPCPE; WDSVLDPCPES; DSVLDPCPESS; SVLDPCPESSV; VLDPCPESSVS; LDPCPESSVSE; DPCPESSVSES; PCPESSVSESS; CPESSVSESSS; PESSVSESSSL; ESSVSESSSLV; SSVSESSSLVI; SVSESSSLVIS; VSESSSLVISR; SESSSLVISRI; ESSSLVISRIH; SSSLVISRIHF; SSLVISRIHFP; SLVISRIHFPM; LVISRIHFPMH; VISRIHFPMHI; ISRIHFPMHIL; SRIHFPMHILY; RIHFPMHILYF; IHFPMHILYFI; HFPMHILYFIL; FPMHILYFILE; PMHILYFILEK; MHILYFILEKV; HILYFILEKVY; ILYFILEKVYI; LYFILEKVYIL; YFILEKVYILI; FILEKVYILIS; ILEKVYILISE; LEKVYILISES; EKVYILISESS; KVYILISESSL; VYILISESSLS; YILISESSLSF; ILISESSLSFH; LISESSLSFHS; ISESSLSFHST; SESSLSFHSTI; ESSLSFHSTIL; SSLSFHSTILD; SLSFHSTILDC; LSFHSTILDCI; SFHSTILDCIS; FHSTILDCISV; HSTILDCISVA; STILDCISVAK; TILDCISVAKS; ILDCISVAKSA; LDCISVAKSAT; DCISVAKSATG; CISVAKSATGL; ISVAKSATGLN; SVAKSATGLNQ; VAKSATGLNQI; AKSATGLNQIS; KSATGLNQISS; SATGLNQISSS; ATGLNQISSSN; TGLNQISSSNK; GLNQISSSNKV; LNQISSSNKVI; NQISSSNKVIP; QISSSNKVIPL; ISSSNKVIPLC; SSSNKVIPLCK; SSNKVIPLCKI; SNKVIPLCKIL; NKVIPLCKILF; KVIPLCKILFS; VIPLCKILFSS; IPLCKILFSSK; PLCKILFSSKN; LCKILFSSKNS; CKILFSSKNSE; KILFSSKNSEF; ILFSSKNSEFC; LFSSKNSEFCK; FSSKNSEFCKD; SSKNSEFCKDF; SKNSEFCKDFL; KNSEFCKDFLK; NSEFCKDFLKY; SEFCKDFLKYI; EFCKDFLKYIL; FCKDFLKYILG; CKDFLKYILGL; KDFLKYILGLK; DFLKYILGLKS; FLKYILGLKSI; LKYILGLKSIC; KYILGLKSICL; YILGLKSICLT; ILGLKSICLTN; LGLKSICLTNL; GLKSICLTNLA; LKSICLTNLAC; KSICLTNLACR; SICLTNLACRV; ICLTNLACRVL; CLTNLACRVLG; LTNLACRVLGT; TNLACRVLGTG; NLACRVLGTGY; LACRVLGTGYS; ACRVLGTGYSF; CRVLGTGYSFI; RVLGTGYSFIV; VLGTGYSFIVT; LGTGYSFIVTK; GTGYSFIVTKP; TGYSFIVTKPG; GYSFIVTKPGG; YSFIVTKPGGN; SFIVTKPGGNI; FIVTKPGGNIW; IVTKPGGNIWV; VTKPGGNIWVL; TKPGGNIWVLL; KPGGNIWVLLF; PGGNIWVLLFK; GGNIWVLLFKC; GNIWVLLFKCF; NIWVLLFKCFF; IWVLLFKCFFS; WVLLFKCFFSK; VLLFKCFFSKF; LLFKCFFSKFT; LFKCFFSKFTL; FKCFFSKFTLT; KCFFSKFTLTL; CFFSKFTLTLP; FFSKFTLTLPS; FSKFTLTLPSK; SLKLSKLFIPC; LKLSKLFIPCP; KLSKLFIPCPE; LSKLFIPCPEG; SKLFIPCPEGK; KLFIPCPEGKS; LFIPCPEGKSF; FIPCPEGKSFD; IPCPEGKSFDS; PCPEGKSFDSA; CPEGKSFDSAP; PEGKSFDSAPV; EGKSFDSAPVP; GKSFDSAPVPF; KSFDSAPVPFT; SFDSAPVPFTS; FDSAPVPFTSS; DSAPVPFTSSK; SAPVPFTSSKT; APVPFTSSKTT; PVPFTSSKTTM; VPFTSSKTTMY; SIATPSSKVSL; IATPSSKVSLS; ATPSSKVSLSM; TPSSKVSLSMG; PSSKVSLSMGR; SSKVSLSMGRF; SKVSLSMGRFT; KVSLSMGRFTF; VSLSMGRFTFK; SLSMGRFTFKA; LSMGRFTFKAL; SMGRFTFKALP; MGRFTFKALPP; GRFTFKALPPH; RFTFKALPPHK; FTFKALPPHKS; TFKALPPHKSN; FKALPPHKSNN; KALPPHKSNNP; ALPPHKSNNPA; LPPHKSNNPAA; PPHKSNNPAAS; PHKSNNPAASV; HKSNNPAASVV; KSNNPAASVVF; SNNPAASVVFP; NNPAASVVFPL; NPAASVVFPLS; PAASVVFPLSM; AASVVFPLSMG; ASVVFPLSMGP; SVVFPLSMGPL; VVFPLSMGPLN; VFPLSMGPLNN; FPLSMGPLNNQ; PLSMGPLNNQY; LSMGPLNNQYL; SMGPLNNQYLL; MGPLNNQYLLL; GPLNNQYLLLG; PLNNQYLLLGT; LNNQYLLLGTL; NNQYLLLGTLK; NQYLLLGTLKT; QYLLLGTLKTI; YLLLGTLKTIQ; LLLGTLKTIQC; LLGTLKTIQCK; LGTLKTIQCKK; GTLKTIQCKKS; TLKTIQCKKSN; LKTIQCKKSNI; KTIQCKKSNIT; TIQCKKSNITE; IQCKKSNITES; QCKKSNITESI; CKKSNITESIL; KKSNITESILG; KSNITESILGS; SNITESILGSK; NITESILGSKQ; ITESILGSKQC; TESILGSKQCS; ESILGSKQCSQ; SILGSKQCSQA; ILGSKQCSQAT; LGSKQCSQATP; GSKQCSQATPA; SKQCSQATPAI; KQCSQATPAIY; QCSQATPAIYC; CSQATPAIYCS; SQATPAIYCSS; QATPAIYCSST; ATPAIYCSSTA; TPAIYCSSTAF; PAIYCSSTAFP; APNIKSILSNI; LNLSVSISSLV; NLSVSISSLVI; RVSTLFLAKTV; VSTLFLAKTVS; STLFLAKTVST; TLFLAKTVSTA; LFLAKTVSTAC; FLLSAKIIAFA; LLSAKIIAFAK; LSAKIIAFAKC; SAKIIAFAKCF; AKIIAFAKCFS; NSKYIPNNKNT; SKYIPNNKNTS; KYIPNNKNTSS; YIPNNKNTSSH; IPNNKNTSSHF; PNNKNTSSHFV; NNKNTSSHFVS; NKNTSSHFVST; KNTSSHFVSTA; NTSSHFVSTAY; TSSHFVSTAYS; SSHFVSTAYSV; SHFVSTAYSVI; HFVSTAYSVIN; FVSTAYSVINF; VSTAYSVINFQ; STAYSVINFQD; TAYSVINFQDT; AYSVINFQDTC; YSVINFQDTCF; SVINFQDTCFV; VINFQDTCFVS; INFQDTCFVSS; NFQDTCFVSSG; FQDTCFVSSGS; QDTCFVSSGSS; DTCFVSSGSSG; TCFVSSGSSGL; CFVSSGSSGLK; FVSSGSSGLKS; VSSGSSGLKSC; SSGSSGLKSCS; SGSSGLKSCSF; GSSGLKSCSFK; SSGLKSCSFKP; SGLKSCSFKPP; MLSSIVWYGSL; LSSIVWYGSLV; SSIVWYGSLVK; SIVWYGSLVKA; IVWYGSLVKAL; VWYGSLVKALY; WYGSLVKALYS; YGSLVKALYSK; GSLVKALYSKY; SLVKALYSKYS; LVKALYSKYSL; VKALYSKYSLL; KALYSKYSLLT; ALYSKYSLLTP; LYSKYSLLTPL; YSKYSLLTPLQ; SKYSLLTPLQI; KYSLLTPLQIK; YSLLTPLQIKK; SLLTPLQIKKL; LLTPLQIKKLK; LTPLQIKKLKV; TPLQIKKLKVH; PLQIKKLKVHS; LQIKKLKVHSF; QKLLIAETLCL; KLLIAETLCLC; LLIAETLCLCG; LIAETLCLCGV; IAETLCLCGVK; AETLCLCGVKK; ETLCLCGVKKN; TLCLCGVKKNI; LCLCGVKKNII; CLCGVKKNIIL; LCGVKKNIILC; CGVKKNIILCP; GVKKNIILCPA; VKKNIILCPAH; KKNIILCPAHM; KNIILCPAHMC; NIILCPAHMCL; IILCPAHMCLL; ILCPAHMCLLI; LCPAHMCLLIK; CPAHMCLLIKV; PAHMCLLIKVT; AHMCLLIKVTE; HMCLLIKVTEY; MCLLIKVTEYF; CLLIKVTEYFS; LLIKVTEYFSI; LIKVTEYFSIS; IKVTEYFSISF; KVTEYFSISFL; VTEYFSISFLY; TEYFSISFLYR; EYFSISFLYRI; AFSLVVYTAKQ; FSLVVYTAKQA; SLVVYTAKQAR; LVVYTAKQARV; VVYTAKQARVL; VYTAKQARVLL; YTAKQARVLLL; TAKQARVLLLN; AKQARVLLLNT; KQARVLLLNTA; LRNWCRSEGKS; RNWCRSEGKSL; NWCRSEGKSLG; WCRSEGKSLGS; CRSEGKSLGSS; RSEGKSLGSST; SEGKSLGSSTF; EGKSLGSSTFL; GKSLGSSTFLF; KSLGSSTFLFF; SLGSSTFLFFL; LGSSTFLFFLG; GSSTFLFFLGG; SSTFLFFLGGV; STFLFFLGGVE; TFLFFLGGVEC; ESAVASSSLAN; SAVASSSLANI; AVASSSLANIS; VASSSLANISS; ASSSLANISSW; SSSLANISSWQ; SSLANISSWQN; SLANISSWQNK; LANISSWQNKS; ANISSWQNKSS; NISSWQNKSSS; ISSWQNKSSSH; SSWQNKSSSHF; SWQNKSSSHFS; WQNKSSSHFSL; QNKSSSHFSLK; NKSSSHFSLKE; KSSSHFSLKEL; SSSHFSLKELH; SSHFSLKELHQ; SHFSLKELHQD; HFSLKELHQDS; FSLKELHQDSH; SLKELHQDSHS; LKELHQDSHSS; KELHQDSHSSV; ELHQDSHSSVP; VGTYKKNNYLG; GTYKKNNYLGP; TYKKNNYLGPF; YKKNNYLGPFN; KKNNYLGPFNI; KNNYLGPFNIL; NNYLGPFNILL; NYLGPFNILLF; YLGPFNILLFI; REFLQLFGPTI; EFLQLFGPTIA; FLQLFGPTIAE; LQLFGPTIAEF; QLFGPTIAEFL; LFGPTIAEFLQ; FGPTIAEFLQL; GPTIAEFLQLG; PTIAEFLQLGL; TIAEFLQLGLS; IAEFLQLGLSQ; AEFLQLGLSQT; EFLQLGLSQTT; FLQLGLSQTTV; SSQCSSNLSKP; SQCSSNLSKPR; QCSSNLSKPRA; CSSNLSKPRAL; SSNLSKPRALF; SNLSKPRALFL; NLSKPRALFLK; LSKPRALFLKI; SKPRALFLKIF; KPRALFLKIFY; PRALFLKIFYL; RALFLKIFYLN; ALFLKIFYLNA; LFLKIFYLNAL; FLKIFYLNALI; ADIACKGSAQK; DIACKGSAQKA; IACKGSAQKAF; ACKGSAQKAFW; CKGSAQKAFWN; KGSAQKAFWNK; AIPCSTGYLGK; IPCSTGYLGKE; PCSTGYLGKEE; CSTGYLGKEEN; STGYLGKEENQ; TGYLGKEENQH; GYLGKEENQHK; YLGKEENQHKP; LGKEENQHKPL; GKEENQHKPLS; KEENQHKPLSY; EENQHKPLSYS; ENQHKPLSYSR; NQHKPLSYSRF; QHKPLSYSRFQ; HKPLSYSRFQN; KPLSYSRFQNQ; PLSYSRFQNQA; LSYSRFQNQAD; SYSRFQNQADE; YSRFQNQADEL; SRFQNQADELP; RFQNQADELPL; FQNQADELPLH; QNQADELPLHP; NQADELPLHPA; QADELPLHPAP; ADELPLHPAPF; DELPLHPAPFF; ELPLHPAPFFY; LPLHPAPFFYT; PLHPAPFFYTK; LHPAPFFYTKY; HPAPFFYTKYS; PAPFFYTKYSF; APFFYTKYSFS; PFFYTKYSFSS; FFYTKYSFSSF; FYTKYSFSSFY; YTKYSFSSFYP; TKYSFSSFYPR; KYSFSSFYPRR; YSFSSFYPRRP; SFSSFYPRRPL; FSSFYPRRPLC; SSFYPRRPLCQ; SFYPRRPLCQG; FYPRRPLCQGE; YPRRPLCQGEI; PRRPLCQGEIP; RRPLCQGEIPY; RPLCQGEIPYT; PLCQGEIPYTS; LCQGEIPYTSL; CQGEIPYTSLN; QGEIPYTSLNK; GEIPYTSLNKL; EIPYTSLNKLF; IPYTSLNKLFS; PYTSLNKLFSL; YTSLNKLFSLR; TSLNKLFSLRE; SLNKLFSLRED; LNKLFSLREDF; NKLFSLREDFP; KLFSLREDFPR; LFSLREDFPRQ; FSLREDFPRQL; SLREDFPRQLF; LREDFPRQLFQ; REDFPRQLFQG; EDFPRQLFQGL; DFPRQLFQGLK; FPRQLFQGLKG; PRQLFQGLKGP BK reading frame 3 8 mers: LQKLQKNR; QKLQKNRD; KLQKNRDF; LQKNRDFP; QKNRDFPK; ASEKASTP; SEKASTPL; EKASTPLL; KASTPLLL; ASTPLLLE; STPLLLER; TPLLLERK; PLLLERKG; LLLERKGG; LLERKGGG; LERKGGGR; ERKGGGRG; RKGGGRGG; KGGGRGGL; GGGRGGLG; GGRGGLGL; GRGGLGLL; RGGLGLLY; GGLGLLYI; GLGLLYII; LGLLYIIK; GLLYIIKK; LLYIIKKK; LYIIKKKA; YIIKKKAT; IIKKKATG; IKKKATGR; KKKATGRS; KKATGRSC; KATGRSCL; ATGRSCLP; TGRSCLPM; GRSCLPME; RSCLPMEC; SCLPMECS; CLPMECSQ; LPMECSQT; PMECSQTM; MECSQTMT; ECSQTMTS; CSQTMTSG; SQTMTSGR; QTMTSGRK; TMTSGRKV; MTSGRKVH; TSGRKVHD; SGRKVHDS; GRKVHDSQ; RKVHDSQG; KVHDSQGN; VHDSQGNA; HDSQGNAA; DSQGNAAK; SQGNAAKP; PQEGKCMT; QEGKCMTH; EGKCMTHR; GKCMTHRE; KCMTHREE; CMTHREEL; MTHREELL; THREELLT; HREELLTH; REELLTHG; EELLTHGM; ELLTHGMQ; LLTHGMQP; LTHGMQPN; THGMQPNH; HGMQPNHD; GMQPNHDL; MQPNHDLR; QPNHDLRK; PNHDLRKE; NHDLRKES; HDLRKESA; QTCFASLG; TCFASLGI; CFASLGIL; FASLGILA; ASLGILAL; SLGILALS; LGILALSP; GILALSPV; ILALSPVK; LALSPVKL; ALSPVKLD; LSPVKLDK; SPVKLDKG; PVKLDKGH; VKLDKGHG; KLDKGHGS; LDKGHGSA; DKGHGSAP; KGHGSAPA; GHGSAPAV; HGSAPAVT; GSAPAVTT; SAPAVTTS; APAVTTSF; PAVTTSFS; AVTTSFSE; VTTSFSES; TTSFSESW; NLDWNKKK; LDWNKKKS; DWNKKKSS; WNKKKSSE; NKKKSSED; KKKSSEDF; KKSSEDFY; KSSEDFYF; SSEDFYFY; SEDFYFYF; EDFYFYFR; DFYFYFRA; FYFYFRAF; YFYFRAFA; FYFRAFAG; YFRAFAGI; FRAFAGIL; RQCRREKQ; QCRREKQK; CRREKQKY; RREKQKYH; REKQKYHC; EKQKYHCF; KQKYHCFT; QKYHCFTC; KYHCFTCC; YHCFTCCK; HCFTCCKR; CFTCCKRL; FTCCKRLC; TCCKRLCK; CCKRLCKR; CKRLCKRL; KRLCKRLL; RLCKRLLG; LCKRLLGK; SLFFCISR; LFFCISRF; FFCISRFM; FCISRFMG; CISRFMGA; ISRFMGAA; SRFMGAAL; RFMGAALA; FMGAALAL; MGAALALL; GAALALLG; AALALLGD; ALALLGDL; LALLGDLV; ALLGDLVA; LLGDLVAS; LGDLVASV; GDLVASVS; DLVASVSE; LVASVSEA; VASVSEAA; ASVSEAAA; SVSEAAAA; VSEAAAAT; SEAAAATG; EAAAATGF; AAAATGFS; AAATGFSV; AATGFSVA; ATGFSVAE; TGFSVAEI; GFSVAEIA; FSVAEIAA; SVAEIAAG; VAEIAAGE; AEIAAGEA; EIAAGEAA; IAAGEAAA; AAGEAAAA; AGEAAAAI; GEAAAAIE; EAAAAIEV; AAAAIEVQ; AAAIEVQI; AAIEVQIA; AIEVQIAS; IEVQIASL; EVQIASLA; VQIASLAT; QIASLATV; IASLATVE; ASLATVEG; SLATVEGI; LATVEGIT; ATVEGITS; TVEGITST; VEGITSTS; EGITSTSE; GITSTSEA; ITSTSEAI; TSTSEAIA; STSEAIAA; TSEAIAAI; SEAIAAIG; EAIAAIGL; AIAAIGLT; IAAIGLTP; AAIGLTPQ; AIGLTPQT; IGLTPQTY; GLTPQTYA; LTPQTYAV; TPQTYAVI; PQTYAVIA; QTYAVIAG; TYAVIAGA; YAVIAGAP; AVIAGAPG; VIAGAPGA; IAGAPGAI; AGAPGAIA; GAPGAIAG; APGAIAGF; PGAIAGFA; GAIAGFAA; AIAGFAAL; IAGFAALI; AGFAALIQ; GFAALIQT; FAALIQTV; AALIQTVS; ALIQTVSG; LIQTVSGI; IQTVSGIS; QTVSGISS; TVSGISSL; VSGISSLA; SGISSLAQ; GISSLAQV; ISSLAQVG; SSLAQVGY; SLAQVGYK; LAQVGYKF; AQVGYKFF; QVGYKFFD; VGYKFFDD; GYKFFDDW; YKFFDDWD; KFFDDWDH; FFDDWDHK; FDDWDHKV; DDWDHKVS; DWDHKVST; WDHKVSTV; DHKVSTVG; HKVSTVGL; KVSTVGLY; VSTVGLYQ; STVGLYQQ; TVGLYQQS; VGLYQQSG; GLYQQSGM; LYQQSGMA; YQQSGMAL; QQSGMALE; QSGMALEL; SGMALELF; GMALELFN; MALELFNP; ALELFNPD; LELFNPDE; ELFNPDEY; LFNPDEYY; FNPDEYYD; NPDEYYDI; PDEYYDIL; DEYYDILF; EYYDILFP; YYDILFPG; YDILFPGV; DILFPGVN; ILFPGVNT; LFPGVNTF; FPGVNTFV; PGVNTFVN; GVNTFVNN; VNTFVNNI; NTFVNNIQ; TFVNNIQY; FVNNIQYL; VNNIQYLD; NNIQYLDP; NIQYLDPR; IQYLDPRH; QYLDPRHW; YLDPRHWG; LDPRHWGP; DPRHWGPS; PRHWGPSL; RHWGPSLF; HWGPSLFA; WGPSLFAT; GPSLFATI; PSLFATIS; SLFATISQ; LFATISQA; FATISQAL; ATISQALW; TISQALWH; ISQALWHV; SQALWHVI; QALWHVIR; ALWHVIRD; LWHVIRDD; WHVIRDDI; HVIRDDIP; VIRDDIPS; IRDDIPSI; RDDIPSIT; DDIPSITS; DIPSITSQ; IPSITSQE; PSITSQEL; SITSQELQ; ITSQELQR; TSQELQRR; SQELQRRT; QELQRRTE; ELQRRTER; LQRRTERF; QRRTERFF; RRTERFFR; RTERFFRD; TERFFRDS; ERFFRDSL; RFFRDSLA; FFRDSLAR; FRDSLARF; RDSLARFL; DSLARFLE; SLARFLEE; LARFLEET; ARFLEETT; RFLEETTW; FLEETTWT; LEETTWTI; EETTWTIV; ETTWTIVN; TTWTIVNA; TWTIVNAP; WTIVNAPI; TIVNAPIN; IVNAPINF; VNAPINFY; NAPINFYN; APINFYNY; PINFYNYI; INFYNYIQ; NFYNYIQQ; FYNYIQQY; YNYIQQYY; NYIQQYYS; YIQQYYSD; IQQYYSDL; QQYYSDLS; QYYSDLSP; YYSDLSPI; YSDLSPIR; SDLSPIRP; DLSPIRPS; LSPIRPSM; SPIRPSMV; PIRPSMVR; IRPSMVRQ; RPSMVRQV; PSMVRQVA; SMVRQVAE; MVRQVAER; VRQVAERE; RQVAEREG; QVAEREGT; VAEREGTR; AEREGTRV; EREGTRVH; REGTRVHF; EGTRVHFG; GTRVHFGH; TRVHFGHT; RVHFGHTY; VHFGHTYS; HFGHTYSI; FGHTYSID; GHTYSIDD; HTYSIDDA; TYSIDDAD; YSIDDADS; SIDDADSI; IDDADSIE; DDADSIEE; DADSIEEV; ADSIEEVT; DSIEEVTQ; SIEEVTQR; IEEVTQRM; EEVTQRMD; EVTQRMDL; VTQRMDLR; TQRMDLRN; QRMDLRNQ; RMDLRNQQ; MDLRNQQS; DLRNQQSV; LRNQQSVH; RNQQSVHS; NQQSVHSG; QQSVHSGE; QSVHSGEF; SVHSGEFI; VHSGEFIE; HSGEFIEK; SGEFIEKT; GEFIEKTI; EFIEKTIA; FIEKTIAP; IEKTIAPG; EKTIAPGG; KTIAPGGA; TIAPGGAN; IAPGGANQ; APGGANQR; PGGANQRT; GGANQRTA; GANQRTAP; ANQRTAPQ; NQRTAPQW; QRTAPQWM; RTAPQWML; TAPQWMLP; APQWMLPL; PQWMLPLL; QWMLPLLL; WMLPLLLG; MLPLLLGL; LPLLLGLY; PLLLGLYG; LLLGLYGT; LLGLYGTV; LGLYGTVT; GLYGTVTP; LYGTVTPA; YGTVTPAL; GTVTPALE; TVTPALEA; VTPALEAY; TPALEAYE; PALEAYED; ALEAYEDG; LEAYEDGP; EAYEDGPN; AYEDGPNQ; YEDGPNQK; EDGPNQKK; DGPNQKKR; GPNQKKRR; PNQKKRRV; NQKKRRVS; QKKRRVSR; KKRRVSRG; KRRVSRGS; RRVSRGSS; RVSRGSSQ; VSRGSSQK; SRGSSQKA; RGSSQKAK; GSSQKAKG; SSQKAKGT; SQKAKGTR; QKAKGTRA; KAKGTRAS; AKGTRASA; KGTRASAK; GTRASAKT; TRASAKTT; RASAKTTN; ASAKTTNK; SAKTTNKR; AKTTNKRR; KTTNKRRS; TTNKRRSR; TNKRRSRS; NKRRSRSS; KRRSRSSR; RRSRSSRS; NWGRCYYR; WGRCYYRG; GRCYYRGR; RCYYRGRM; CYYRGRML; YYRGRMLP; YRGRMLPK; RGRMLPKP; GRMLPKPR; RMLPKPRN; MLPKPRNG; LPKPRNGG; PKPRNGGS; KPRNGGSR; PREKNASL; REKNASLL; EKNASLLQ; KNASLLQH; NASLLQHS; ASLLQHSK; SLLQHSKN; LLQHSKNS; LQHSKNSP; QHSKNSPP; HSKNSPPQ; SKNSPPQF; KNSPPQFK; GPNLWKST; PNLWKSTD; NLWKSTDV; LWKSTDVG; WKSTDVGG; KSTDVGGC; STDVGGCN; TDVGGCNC; DVGGCNCT; VGGCNCTN; GGCNCTNR; GCNCTNRG; CNCTNRGY; NCTNRGYW; CTNRGYWN; TNRGYWNN; PSCRVTKS; SCRVTKSA; AWWRKTYS; WWRKTYSR; WRKTYSRQ; FPLLCCRW; PLLCCRWR; LLCCRWRT; LCCRWRTL; CCRWRTLG; CRWRTLGN; RWRTLGNA; WRTLGNAG; RTLGNAGS; TLGNAGSA; LGNAGSAN; GNAGSANE; NAGSANEL; AGSANELQ; GSANELQV; SANELQVK; ANELQVKV; NELQVKVP; KPNSPVPG; PNSPVPGN; NSPVPGNE; SPVPGNEY; GLFGQKQC; LFGQKQCL; FGQKQCLS; GQKQCLSS; VFWDFHRR; FWDFHRRG; WDFHRRGK; DFHRRGKC; FHRRGKCS; HRRGKCSP; RRGKCSPS; RGKCSPST; GKCSPSTS; KCSPSTSC; CSPSTSCD; SPSTSCDQ; PSTSCDQH; STSCDQHS; TSCDQHSY; SCDQHSYH; CDQHSYHS; DQHSYHSV; QHSYHSVA; HSYHSVAR; QLWNTTVE; LWNTTVER; WNTTVERP; NTTVERPC; TTVERPCK; TVERPCKI; VERPCKIF; DPPEKKIC; PPEKKICK; PEKKICKE; EKKICKES; KKICKESL; KICKESLP; ICKESLPN; CKESLPNF; KESLPNFL; ESLPNFLF; SLPNFLFA; LPNFLFAK; PYKQENPE; YKQENPES; KQENPESG; QENPESGW; ENPESGWA; NPESGWAA; PESGWAAY; ESGWAAYV; SGWAAYVW; GWAAYVWY; WAAYVWYG; AAYVWYGI; AYVWYGIP; YVWYGIPG; VWYGIPGR; WYGIPGRR; YGIPGRRG; WHRKTSRG; HRKTSRGP; RKTSRGPR; KTSRGPRY; TSRGPRYD; SRGPRYDK; RGPRYDKI; GPRYDKIY; QTGTIANQ; TGTIANQN; GTIANQNA; TIANQNAL; IANQNALN; ANQNALNR; NQNALNRC; QNALNRCF; NALNRCFY; ALNRCFYC; LNRCFYCT; NRCFYCTY; RCFYCTYT; CFYCTYTF; FYCTYTFN; YCTYTFNK; CTYTFNKC; TYTFNKCC; YTFNKCCF; TFNKCCFC; FNKCCFCI; NKCCFCIS; KCCFCISH; CCFCISHF; ACVILGVV; CVILGVVF; NTESLYTN; TESLYTNA; ESLYTNAT; SLYTNATL; LYTNATLD; YTNATLDY; TNATLDYG; NATLDYGG; ATLDYGGL; TLDYGGLT; LDYGGLTF; DYGGLTFG; YGGLTFGN; GGLTFGNL; GLTFGNLQ; LTFGNLQQ; TFGNLQQG; FGNLQQGL; GNLQQGLK; NLQQGLKY; LQQGLKYL; QQGLKYLR; QGLKYLRL; GLKYLRLG; LKYLRLGK; KYLRLGKS; YLRLGKSI; LRLGKSIV; RLGKSIVI; LGKSIVIG; GKSIVIGI; KSIVIGIQ; SIVIGIQC; IVIGIQCL; VIGIQCLI; IGIQCLIH; GIQCLIHV; IQCLIHVQ; QCLIHVQS; CLIHVQSL; LIHVQSLQ; IHVQSLQF; HVQSLQFL; VQSLQFLN; QSLQFLNP; SLQFLNPL; LQFLNPLL; QFLNPLLL; YQEYISPC; QEYISPCI; EYISPCIY; YISPCIYY; ISPCIYYI; SPCIYYIS; PCIYYISS; CIYYISSL; IYYISSLK; YYISSLKK; YISSLKKY; ISSLKKYT; SSLKKYTY; SLKKYTYL; LKKYTYLS; KKYTYLSQ; KYTYLSQN; YTYLSQNP; TYLSQNPA; YLSQNPAF; LSQNPAFP; SQNPAFPS; QNPAFPSI; NPAFPSIQ; PAFPSIQQ; AFPSIQQF; IVYQLQNQ; VYQLQNQL; YQLQNQLQ; QLQNQLQA; TKLAVATR; KLAVATRS; LAVATRSF; AVATRSFH; VATRSFHF; ATRSFHFV; TRSFHFVK; RSFHFVKF; SFHFVKFF; FHFVKFFF; HFVKFFFQ; FVKFFFQV; VKFFFQVR; KFFFQVRT; FFFQVRTL; FFQVRTLS; FQVRTLSF; QVRTLSFV; VRTLSFVR; RTLSFVRI; TLSFVRIF; LSFVRIFL; SFVRIFLN; FVRIFLNI; VRIFLNIF; RIFLNIFW; IFLNIFWA; PSLVEIFG; SLVEIFGF; LVEIFGFF; VEIFGFFC; EIFGFFCL; IFGFFCLN; FGFFCLNV; GFFCLNVS; FFCLNVSF; FCLNVSFL; CLNVSFLN; LNVSFLNL; NVSFLNLP; HFHLNNLS; FHLNNLSN; HLNNLSNC; LNNLSNCL; NNLSNCLN; NLSNCLNC; LSNCLNCL; SNCLNCLF; NCLNCLFH; CLNCLFHV; LNCLFHVL; NCLFHVLK; CLFHVLKA; LFHVLKAN; FHVLKANP; HVLKANPL; VLKANPLI; LKANPLIQ; KANPLIQL; ANPLIQLL; NPLIQLLS; PLIQLLSL; LIQLLSLL; IQLLSLLH; QLLSLLHL; LLSLLHLQ; LSLLHLQK; SLLHLQKQ; LLHLQKQP; LHLQKQPC; HLQKQPCT; LQKQPCTD; QKQPCTDL; LHLAQRLA; HLAQRLAF; LAQRLAFP; AQRLAFPW; QRLAFPWV; RLAFPWVG; LAFPWVGL; AFPWVGLH; FPWVGLHL; PWVGLHLR; WVGLHLRL; VGLHLRLY; GLHLRLYH; LHLRLYHH; HLRLYHHT; LRLYHHTN; RLYHHTNL; LYHHTNLI; YHHTNLIT; HHTNLITL; HTNLITLQ; TNLITLQL; NLITLQLV; LITLQLVL; ITLQLVLF; TLQLVLFF; LQLVLFFH; QLVLFFHY; LVLFFHYQ; VLFFHYQW; LFFHYQWD; FFHYQWDL; KQYSAKNQ; QYSAKNQI; YSAKNQIL; SAKNQILQ; AKNQILQN; KNQILQNP; NQILQNPF; VANSAAKQ; ANSAAKQH; NSAAKQHL; SAAKQHLP; AAKQHLPY; AKQHLPYI; KQHLPYIV; QHLPYIVL; HLPYIVLV; LPYIVLVQ; PYIVLVQH; YIVLVQHF; IVLVQHFH; VLVQHFHE; LVQHFHEL; VQHFHELQ; QHFHELQI; HFHELQIL; FHELQILN; HELQILNP; ELQILNPF; LQILNPFY; QILNPFYL; ILNPFYLI; LNPFYLIY; NPFYLIYD; IFLLAFLP; FLLAFLPW; LLAFLPWS; LAFLPWSY; AFLPWSYE; FLPWSYEG; LPWSYEGY; PWSYEGYL; WSYEGYLL; SYEGYLLF; YEGYLLFF; LKLYLLLA; KLYLLLAD; LYLLLADK; YLLLADKY; LLLADKYF; LLADKYFF; LADKYFFD; ADKYFFDF; DKYFFDFY; KYFFDFYF; YFFDFYFL; FFDFYFLQ; FDFYFLQK; HLQSAFHD; LQSAFHDT; SDKAGLFS; DKAGLFSD; KAGLFSDT; AGLFSDTF; GLFSDTFY; LFSDTFYT; FSDTFYTP; SDTFYTPL; DTFYTPLH; TFYTPLHC; FYTPLHCI; YTPLHCIE; TPLHCIEI; PLHCIEIL; LHCIEILN; HCIEILNT; CIEILNTY; IEILNTYL; EILNTYLI; ILNTYLII; LNTYLIIK; NTYLIIKT; TYLIIKTH; YLIIKTHP; LIIKTHPH; IIKTHPHT; IKTHPHTL; KTHPHTLS; THPHTLSL; HPHTLSLL; PHTLSLLH; HTLSLLHT; TLSLLHTQ; LISKTPAL; ISKTPALF; SKTPALFL; KTPALFLQ; TPALFLQA; PALFLQAL; ALFLQALL; LFLQALLG; NHAPLSPL; HAPLSPLE; APLSPLEC; PLSPLECF; LSPLECFL; SPLECFLL; LRHYIVSI; RHYIVSIP; HYIVSIPY; RYTAFDRN; YTAFDRNY; LQKLYVYV; QKLYVYVE; KLYVYVEL; LYVYVELK; YVYVELKR; VYVELKRI; YYAQHTCV; YAQHTCVY; VFYTEFEL; FYTEFELF; YTEFELFL; YTQQSRQG; TQQSRQGF; QQSRQGFY; QSRQGFYY; ETGVDQRE; TGVDQRES; GVDQRESL; GLLPFFFF; LLPFFFFW; LPFFFFWV; PFFFFWVV; FFFFWVVL; FFFWVVLS; FFWVVLSV; FWVVLSVE; WVVLSVEN; VVLSVENL; VLSVENLL; LSVENLLL; SVENLLLL; VENLLLLL; ENLLLLLH; NLLLLLHH; LLLLLHHW; LLLLHHWQ; LLLHHWQT; LLHHWQTY; LHHWQTYL; HHWQTYLH; HWQTYLHG; WQTYLHGK; QTYLHGKI; TYLHGKIN; YLHGKINL; LHGKINLH; HGKINLHP; GKINLHPI; KINLHPIF; INLHPIFH; RNSTRTPT; NSTRTPTL; STRTPTLL; TRTPTLLF; RTPTLLFH; TPTLLFHR; PTLLFHRL; TLLFHRLA; LLFHRLAP; LFHRLAPI; FHRLAPIK; HRLAPIKK; RLAPIKKI; LAPIKKII; APIKKIIT; GLLIFYYL; LLIFYYLS; LIFYYLSK; IFYYLSKY; FYYLSKYK; YYLSKYKL; YLSKYKLV; LSKYKLVT; SKYKLVTL; KYKLVTLK; YKLVTLKL; ISEGSFSN; SEGSFSNY; EGSFSNYL; GSFSNYLD; SFSNYLDP; FSNYLDPP; SNYLDPPL; NYLDPPLQ; YLDPPLQS; LDPPLQSF; DPPLQSFF; PPLQSFFS; AKPLCEAV; KPLCEAVN; PLCEAVNA; LCEAVNAV; CEAVNAVA; EAVNAVAI; AVNAVAIY; VNAVAIYP; NAVAIYPN; AVAIYPNQ; VAIYPNQG; AIYPNQGL; IYPNQGLF; YPNQGLFS; HARAVHRR; ARAVHRRL; RAVHRRLF; AVHRRLFG; VHRRLFGT; HRRLFGTN; RRLFGTNR; RLFGTNRP; LFGTNRPF; FGTNRPFL; GTNRPFLA; TNRPFLAV; NRPFLAVQ; RPFLAVQG; PFLAVQGI; FLAVQGIW; LAVQGIWA; AVQGIWAK; VQGIWAKR; QGIWAKRK; GIWAKRKI; IWAKRKIS; WAKRKIST; AKRKISTN; KRKISTNL; ATPGSKIR; TPGSKIRL; PGSKIRLM; GSKIRLMS; SKIRLMSY; KIRLMSYL; IRLMSYLY; RLMSYLYI; LMSYLYIL; MSYLYILL; SYLYILLH; YLYILLHF; LYILLHFF; YILLHFFI; ILLHFFIQ; LLHFFIQS; LHFFIQSI; HFFIQSIH; FFIQSIHS; FIQSIHSL; IQSIHSLH; QSIHSLHF; SIHSLHFI; IHSLHFIL; HSLHFILV; SLHFILVA; LHFILVAP; HFILVAPF; FILVAPFV; ILVAPFVR; LVAPFVRV; VAPFVRVK; APFVRVKF; PFVRVKFL; FVRVKFLT; VRVKFLTL; RVKFLTLP; GKISPGSS; KISPGSSF; ISPGSSFK; SPGSSFKA; KVHELHGF; VHELHGFF; HELHGFFP; ELHGFFPV; LHGFFPVK; HGFFPVKN; GFFPVKNF; FFPVKNFI; FPVKNFIH 9 mers: LQKLQKNRD; QKLQKNRDF; KLQKNRDFP; LQKNRDFPK; ASEKASTPL; SEKASTPLL; EKASTPLLL; KASTPLLLE; ASTPLLLER; STPLLLERK; TPLLLERKG; PLLLERKGG; LLLERKGGG; LLERKGGGR; LERKGGGRG; ERKGGGRGG; RKGGGRGGL; KGGGRGGLG; GGGRGGLGL; GGRGGLGLL; GRGGLGLLY; RGGLGLLYI; GGLGLLYII; GLGLLYIIK; LGLLYIIKK; GLLYIIKKK; LLYIIKKKA; LYIIKKKAT; YIIKKKATG; IIKKKATGR; IKKKATGRS; KKKATGRSC; KKATGRSCL; KATGRSCLP; ATGRSCLPM; TGRSCLPME; GRSCLPMEC; RSCLPMECS; SCLPMECSQ; CLPMECSQT; LPMECSQTM; PMECSQTMT; MECSQTMTS; ECSQTMTSG; CSQTMTSGR; SQTMTSGRK; QTMTSGRKV; TMTSGRKVH; MTSGRKVHD; TSGRKVHDS; SGRKVHDSQ; GRKVHDSQG; RKVHDSQGN; KVHDSQGNA; VHDSQGNAA; HDSQGNAAK; DSQGNAAKP; PQEGKCMTH; QEGKCMTHR; EGKCMTHRE; GKCMTHREE; KCMTHREEL; CMTHREELL; MTHREELLT; THREELLTH; HREELLTHG; REELLTHGM; EELLTHGMQ; ELLTHGMQP; LLTHGMQPN; LTHGMQPNH; THGMQPNHD; HGMQPNHDL; GMQPNHDLR; MQPNHDLRK; QPNHDLRKE; PNHDLRKES; NHDLRKESA; QTCFASLGI; TCFASLGIL; CFASLGILA; FASLGILAL; ASLGILALS; SLGILALSP; LGILALSPV; GILALSPVK; ILALSPVKL; LALSPVKLD; ALSPVKLDK; LSPVKLDKG; SPVKLDKGH; PVKLDKGHG; VKLDKGHGS; KLDKGHGSA; LDKGHGSAP; DKGHGSAPA; KGHGSAPAV; GHGSAPAVT; HGSAPAVTT; GSAPAVTTS; SAPAVTTSF; APAVTTSFS; PAVTTSFSE; AVTTSFSES; VTTSFSESW; NLDWNKKKS; LDWNKKKSS; DWNKKKSSE; WNKKKSSED; NKKKSSEDF; KKKSSEDFY; KKSSEDFYF; KSSEDFYFY; SSEDFYFYF; SEDFYFYFR; EDFYFYFRA; DFYFYFRAF; FYFYFRAFA; YFYFRAFAG; FYFRAFAGI; YFRAFAGIL; RQCRREKQK; QCRREKQKY; CRREKQKYH; RREKQKYHC; REKQKYHCF; EKQKYHCFT; KQKYHCFTC; QKYHCFTCC; KYHCFTCCK; YHCFTCCKR; HCFTCCKRL; CFTCCKRLC; FTCCKRLCK; TCCKRLCKR; CCKRLCKRL; CKRLCKRLL; KRLCKRLLG; RLCKRLLGK; SLFFCISRF; LFFCISRFM; FFCISRFMG; FCISRFMGA; CISRFMGAA; ISRFMGAAL; SRFMGAALA; RFMGAALAL; FMGAALALL; MGAALALLG; GAALALLGD; AALALLGDL; ALALLGDLV; LALLGDLVA; ALLGDLVAS; LLGDLVASV; LGDLVASVS; GDLVASVSE; DLVASVSEA; LVASVSEAA; VASVSEAAA; ASVSEAAAA; SVSEAAAAT; VSEAAAATG; SEAAAATGF; EAAAATGFS; AAAATGFSV; AAATGFSVA; AATGFSVAE; ATGFSVAEI; TGFSVAEIA; GFSVAEIAA; FSVAEIAAG; SVAEIAAGE; VAEIAAGEA; AEIAAGEAA; EIAAGEAAA; IAAGEAAAA; AAGEAAAAI; AGEAAAAIE; GEAAAAIEV; EAAAAIEVQ; AAAAIEVQI; AAAIEVQIA; AAIEVQIAS; AIEVQIASL; IEVQIASLA; EVQIASLAT; VQIASLATV; QIASLATVE; IASLATVEG; ASLATVEGI; SLATVEGIT; LATVEGITS; ATVEGITST; TVEGITSTS; VEGITSTSE; EGITSTSEA; GITSTSEAI; ITSTSEAIA; TSTSEAIAA; STSEAIAAI; TSEAIAAIG; SEAIAAIGL; EAIAAIGLT; AIAAIGLTP; IAAIGLTPQ; AAIGLTPQT; AIGLTPQTY; IGLTPQTYA; GLTPQTYAV; LTPQTYAVI; TPQTYAVIA; PQTYAVIAG; QTYAVIAGA; TYAVIAGAP; YAVIAGAPG; AVIAGAPGA; VIAGAPGAI; IAGAPGAIA; AGAPGAIAG; GAPGAIAGF; APGAIAGFA; PGAIAGFAA; GAIAGFAAL; AIAGFAALI; IAGFAALIQ; AGFAALIQT; GFAALIQTV; FAALIQTVS; AALIQTVSG; ALIQTVSGI; LIQTVSGIS; IQTVSGISS; QTVSGISSL; TVSGISSLA; VSGISSLAQ; SGISSLAQV; GISSLAQVG; ISSLAQVGY; SSLAQVGYK; SLAQVGYKF; LAQVGYKFF; AQVGYKFFD; QVGYKFFDD; VGYKFFDDW; GYKFFDDWD; YKFFDDWDH; KFFDDWDHK; FFDDWDHKV; FDDWDHKVS; DDWDHKVST; DWDHKVSTV; WDHKVSTVG; DHKVSTVGL; HKVSTVGLY; KVSTVGLYQ; VSTVGLYQQ; STVGLYQQS; TVGLYQQSG; VGLYQQSGM; GLYQQSGMA; LYQQSGMAL; YQQSGMALE; QQSGMALEL; QSGMALELF; SGMALELFN; GMALELFNP; MALELFNPD; ALELFNPDE; LELFNPDEY; ELFNPDEYY; LFNPDEYYD; FNPDEYYDI; NPDEYYDIL; PDEYYDILF; DEYYDILFP; EYYDILFPG; YYDILFPGV; YDILFPGVN; DILFPGVNT; ILFPGVNTF; LFPGVNTFV; FPGVNTFVN; PGVNTFVNN; GVNTFVNNI; VNTFVNNIQ; NTFVNNIQY; TFVNNIQYL; FVNNIQYLD; VNNIQYLDP; NNIQYLDPR; NIQYLDPRH; IQYLDPRHW; QYLDPRHWG; YLDPRHWGP; LDPRHWGPS; DPRHWGPSL; PRHWGPSLF; RHWGPSLFA; HWGPSLFAT; WGPSLFATI; GPSLFATIS; PSLFATISQ; SLFATISQA; LFATISQAL; FATISQALW; ATISQALWH; TISQALWHV; ISQALWHVI; SQALWHVIR; QALWHVIRD; ALWHVIRDD; LWHVIRDDI; WHVIRDDIP; HVIRDDIPS; VIRDDIPSI; IRDDIPSIT; RDDIPSITS; DDIPSITSQ; DIPSITSQE; IPSITSQEL; PSITSQELQ; SITSQELQR; ITSQELQRR; TSQELQRRT; SQELQRRTE; QELQRRTER; ELQRRTERF; LQRRTERFF; QRRTERFFR; RRTERFFRD; RTERFFRDS; TERFFRDSL; ERFFRDSLA; RFFRDSLAR; FFRDSLARF; FRDSLARFL; RDSLARFLE; DSLARFLEE; SLARFLEET; LARFLEETT; ARFLEETTW; RFLEETTWT; FLEETTWTI; LEETTWTIV; EETTWTIVN; ETTWTIVNA; TTWTIVNAP; TWTIVNAPI; WTIVNAPIN; TIVNAPINF; IVNAPINFY; VNAPINFYN; NAPINFYNY; APINFYNYI; PINFYNYIQ; INFYNYIQQ; NFYNYIQQY; FYNYIQQYY; YNYIQQYYS; NYIQQYYSD; YIQQYYSDL; IQQYYSDLS; QQYYSDLSP; QYYSDLSPI; YYSDLSPIR; YSDLSPIRP; SDLSPIRPS; DLSPIRPSM; LSPIRPSMV; SPIRPSMVR; PIRPSMVRQ; IRPSMVRQV; RPSMVRQVA; PSMVRQVAE; SMVRQVAER; MVRQVAERE; VRQVAEREG; RQVAEREGT; QVAEREGTR; VAEREGTRV; AEREGTRVH; EREGTRVHF; REGTRVHFG; EGTRVHFGH; GTRVHFGHT; TRVHFGHTY; RVHFGHTYS; VHFGHTYSI; HFGHTYSID; FGHTYSIDD; GHTYSIDDA; HTYSIDDAD; TYSIDDADS; YSIDDADSI; SIDDADSIE; IDDADSIEE; DDADSIEEV; DADSIEEVT; ADSIEEVTQ; DSIEEVTQR; SIEEVTQRM; IEEVTQRMD; EEVTQRMDL; EVTQRMDLR; VTQRMDLRN; TQRMDLRNQ; QRMDLRNQQ; RMDLRNQQS; MDLRNQQSV; DLRNQQSVH; LRNQQSVHS; RNQQSVHSG; NQQSVHSGE; QQSVHSGEF; QSVHSGEFI; SVHSGEFIE; VHSGEFIEK; HSGEFIEKT; SGEFIEKTI; GEFIEKTIA; EFIEKTIAP; FIEKTIAPG; IEKTIAPGG; EKTIAPGGA; KTIAPGGAN; TIAPGGANQ; IAPGGANQR; APGGANQRT; PGGANQRTA; GGANQRTAP; GANQRTAPQ; ANQRTAPQW; NQRTAPQWM; QRTAPQWML; RTAPQWMLP; TAPQWMLPL; APQWMLPLL; PQWMLPLLL; QWMLPLLLG; WMLPLLLGL; MLPLLLGLY; LPLLLGLYG; PLLLGLYGT; LLLGLYGTV; LLGLYGTVT; LGLYGTVTP; GLYGTVTPA; LYGTVTPAL; YGTVTPALE; GTVTPALEA; TVTPALEAY; VTPALEAYE; TPALEAYED; PALEAYEDG; ALEAYEDGP; LEAYEDGPN; EAYEDGPNQ; AYEDGPNQK; YEDGPNQKK; EDGPNQKKR; DGPNQKKRR; GPNQKKRRV; PNQKKRRVS; NQKKRRVSR; QKKRRVSRG; KKRRVSRGS; KRRVSRGSS; RRVSRGSSQ; RVSRGSSQK; VSRGSSQKA; SRGSSQKAK; RGSSQKAKG; GSSQKAKGT; SSQKAKGTR; SQKAKGTRA; QKAKGTRAS; KAKGTRASA; AKGTRASAK; KGTRASAKT; GTRASAKTT; TRASAKTTN; RASAKTTNK; ASAKTTNKR; SAKTTNKRR; AKTTNKRRS; KTTNKRRSR; TTNKRRSRS; TNKRRSRSS; NKRRSRSSR; KRRSRSSRS; NWGRCYYRG; WGRCYYRGR; GRCYYRGRM; RCYYRGRML; CYYRGRMLP; YYRGRMLPK; YRGRMLPKP; RGRMLPKPR; GRMLPKPRN; RMLPKPRNG; MLPKPRNGG; LPKPRNGGS; PKPRNGGSR; PREKNASLL; REKNASLLQ; EKNASLLQH; KNASLLQHS; NASLLQHSK; ASLLQHSKN; SLLQHSKNS; LLQHSKNSP; LQHSKNSPP; QHSKNSPPQ; HSKNSPPQF; SKNSPPQFK; GPNLWKSTD; PNLWKSTDV; NLWKSTDVG; LWKSTDVGG; WKSTDVGGC; KSTDVGGCN; STDVGGCNC; TDVGGCNCT; DVGGCNCTN; VGGCNCTNR; GGCNCTNRG; GCNCTNRGY; CNCTNRGYW; NCTNRGYWN; CTNRGYWNN; PSCRVTKSA; AWWRKTYSR; WWRKTYSRQ; FPLLCCRWR; PLLCCRWRT; LLCCRWRTL; LCCRWRTLG; CCRWRTLGN; CRWRTLGNA; RWRTLGNAG; WRTLGNAGS; RTLGNAGSA; TLGNAGSAN; LGNAGSANE; GNAGSANEL; NAGSANELQ; AGSANELQV; GSANELQVK; SANELQVKV; ANELQVKVP; KPNSPVPGN; PNSPVPGNE; NSPVPGNEY; GLFGQKQCL; LFGQKQCLS; FGQKQCLSS; VFWDFHRRG; FWDFHRRGK; WDFHRRGKC; DFHRRGKCS; FHRRGKCSP; HRRGKCSPS; RRGKCSPST; RGKCSPSTS; GKCSPSTSC; KCSPSTSCD; CSPSTSCDQ; SPSTSCDQH; PSTSCDQHS; STSCDQHSY; TSCDQHSYH; SCDQHSYHS; CDQHSYHSV; DQHSYHSVA; QHSYHSVAR; QLWNTTVER; LWNTTVERP; WNTTVERPC; NTTVERPCK; TTVERPCKI; TVERPCKIF; DPPEKKICK; PPEKKICKE; PEKKICKES; EKKICKESL; KKICKESLP; KICKESLPN; ICKESLPNF; CKESLPNFL; KESLPNFLF; ESLPNFLFA; SLPNFLFAK; PYKQENPES; YKQENPESG; KQENPESGW; QENPESGWA; ENPESGWAA; NPESGWAAY; PESGWAAYV; ESGWAAYVW; SGWAAYVWY; GWAAYVWYG; WAAYVWYGI; AAYVWYGIP; AYVWYGIPG; YVWYGIPGR; VWYGIPGRR; WYGIPGRRG; WHRKTSRGP; HRKTSRGPR; RKTSRGPRY; KTSRGPRYD; TSRGPRYDK; SRGPRYDKI; RGPRYDKIY; QTGTIANQN; TGTIANQNA; GTIANQNAL; TIANQNALN; IANQNALNR; ANQNALNRC; NQNALNRCF; QNALNRCFY; NALNRCFYC; ALNRCFYCT; LNRCFYCTY; NRCFYCTYT; RCFYCTYTF; CFYCTYTFN; FYCTYTFNK; YCTYTFNKC; CTYTFNKCC; TYTFNKCCF; YTFNKCCFC; TFNKCCFCI; FNKCCFCIS; NKCCFCISH; KCCFCISHF; ACVILGVVF; NTESLYTNA; TESLYTNAT; ESLYTNATL; SLYTNATLD; LYTNATLDY; YTNATLDYG; TNATLDYGG; NATLDYGGL; ATLDYGGLT; TLDYGGLTF; LDYGGLTFG; DYGGLTFGN; YGGLTFGNL; GGLTFGNLQ; GLTFGNLQQ; LTFGNLQQG; TFGNLQQGL; FGNLQQGLK; GNLQQGLKY; NLQQGLKYL; LQQGLKYLR; QQGLKYLRL; QGLKYLRLG; GLKYLRLGK; LKYLRLGKS; KYLRLGKSI; YLRLGKSIV; LRLGKSIVI; RLGKSIVIG; LGKSIVIGI; GKSIVIGIQ; KSIVIGIQC; SIVIGIQCL; IVIGIQCLI; VIGIQCLIH; IGIQCLIHV; GIQCLIHVQ; IQCLIHVQS; QCLIHVQSL; CLIHVQSLQ; LIHVQSLQF; IHVQSLQFL; HVQSLQFLN; VQSLQFLNP; QSLQFLNPL; SLQFLNPLL; LQFLNPLLL; YQEYISPCI; QEYISPCIY; EYISPCIYY; YISPCIYYI; ISPCIYYIS; SPCIYYISS; PCIYYISSL; CIYYISSLK; IYYISSLKK; YYISSLKKY; YISSLKKYT; ISSLKKYTY; SSLKKYTYL; SLKKYTYLS; LKKYTYLSQ; KKYTYLSQN; KYTYLSQNP; YTYLSQNPA; TYLSQNPAF; YLSQNPAFP; LSQNPAFPS; SQNPAFPSI; QNPAFPSIQ; NPAFPSIQQ; PAFPSIQQF; IVYQLQNQL; VYQLQNQLQ; YQLQNQLQA; TKLAVATRS; KLAVATRSF; LAVATRSFH; AVATRSFHF; VATRSFHFV; ATRSFHFVK; TRSFHFVKF; RSFHFVKFF; SFHFVKFFF; FHFVKFFFQ; HFVKFFFQV; FVKFFFQVR; VKFFFQVRT; KFFFQVRTL; FFFQVRTLS; FFQVRTLSF; FQVRTLSFV; QVRTLSFVR; VRTLSFVRI; RTLSFVRIF; TLSFVRIFL; LSFVRIFLN; SFVRIFLNI; FVRIFLNIF; VRIFLNIFW; RIFLNIFWA; PSLVEIFGF; SLVEIFGFF; LVEIFGFFC; VEIFGFFCL; EIFGFFCLN; IFGFFCLNV; FGFFCLNVS; GFFCLNVSF; FFCLNVSFL; FCLNVSFLN; CLNVSFLNL; LNVSFLNLP; HFHLNNLSN; FHLNNLSNC; HLNNLSNCL; LNNLSNCLN; NNLSNCLNC; NLSNCLNCL; LSNCLNCLF; SNCLNCLFH; NCLNCLFHV; CLNCLFHVL; LNCLFHVLK; NCLFHVLKA; CLFHVLKAN; LFHVLKANP; FHVLKANPL; HVLKANPLI; VLKANPLIQ; LKANPLIQL; KANPLIQLL; ANPLIQLLS; NPLIQLLSL; PLIQLLSLL; LIQLLSLLH; IQLLSLLHL; QLLSLLHLQ; LLSLLHLQK; LSLLHLQKQ; SLLHLQKQP; LLHLQKQPC; LHLQKQPCT; HLQKQPCTD; LQKQPCTDL; LHLAQRLAF; HLAQRLAFP; LAQRLAFPW; AQRLAFPWV; QRLAFPWVG; RLAFPWVGL; LAFPWVGLH; AFPWVGLHL; FPWVGLHLR; PWVGLHLRL; WVGLHLRLY; VGLHLRLYH; GLHLRLYHH; LHLRLYHHT; HLRLYHHTN; LRLYHHTNL; RLYHHTNLI; LYHHTNLIT; YHHTNLITL; HHTNLITLQ; HTNLITLQL; TNLITLQLV; NLITLQLVL; LITLQLVLF; ITLQLVLFF; TLQLVLFFH; LQLVLFFHY; QLVLFFHYQ; LVLFFHYQW; VLFFHYQWD; LFFHYQWDL; KQYSAKNQI; QYSAKNQIL; YSAKNQILQ; SAKNQILQN; AKNQILQNP; KNQILQNPF; VANSAAKQH; ANSAAKQHL; NSAAKQHLP; SAAKQHLPY; AAKQHLPYI; AKQHLPYIV; KQHLPYIVL; QHLPYIVLV; HLPYIVLVQ; LPYIVLVQH; PYIVLVQHF; YIVLVQHFH; IVLVQHFHE; VLVQHFHEL; LVQHFHELQ; VQHFHELQI; QHFHELQIL; HFHELQILN; FHELQILNP; HELQILNPF; ELQILNPFY; LQILNPFYL; QILNPFYLI; ILNPFYLIY; LNPFYLIYD; IFLLAFLPW; FLLAFLPWS; LLAFLPWSY; LAFLPWSYE; AFLPWSYEG; FLPWSYEGY; LPWSYEGYL; PWSYEGYLL; WSYEGYLLF; SYEGYLLFF; LKLYLLLAD; KLYLLLADK; LYLLLADKY; YLLLADKYF; LLLADKYFF; LLADKYFFD; LADKYFFDF; ADKYFFDFY; DKYFFDFYF; KYFFDFYFL; YFFDFYFLQ; FFDFYFLQK; HLQSAFHDT; SDKAGLFSD; DKAGLFSDT; KAGLFSDTF; AGLFSDTFY; GLFSDTFYT; LFSDTFYTP; FSDTFYTPL; SDTFYTPLH; DTFYTPLHC; TFYTPLHCI; FYTPLHCIE; YTPLHCIEI; TPLHCIEIL; PLHCIEILN; LHCIEILNT; HCIEILNTY; CIEILNTYL; IEILNTYLI; EILNTYLII; ILNTYLIIK; LNTYLIIKT; NTYLIIKTH; TYLIIKTHP; YLIIKTHPH; LIIKTHPHT; IIKTHPHTL; IKTHPHTLS; KTHPHTLSL; THPHTLSLL; HPHTLSLLH; PHTLSLLHT; HTLSLLHTQ; LISKTPALF; ISKTPALFL; SKTPALFLQ; KTPALFLQA; TPALFLQAL; PALFLQALL; ALFLQALLG; NHAPLSPLE; HAPLSPLEC; APLSPLECF; PLSPLECFL; LSPLECFLL; LRHYIVSIP; RHYIVSIPY; RYTAFDRNY; LQKLYVYVE; QKLYVYVEL; KLYVYVELK; LYVYVELKR; YVYVELKRI; YYAQHTCVY; VFYTEFELF; FYTEFELFL; YTQQSRQGF; TQQSRQGFY; QQSRQGFYY; ETGVDQRES; TGVDQRESL; GLLPFFFFW; LLPFFFFWV; LPFFFFWVV; PFFFFWVVL; FFFFWVVLS; FFFWVVLSV; FFWVVLSVE; FWVVLSVEN; WVVLSVENL; VVLSVENLL; VLSVENLLL; LSVENLLLL; SVENLLLLL; VENLLLLLH; ENLLLLLHH; NLLLLLHHW; LLLLLHHWQ; LLLLHHWQT; LLLHHWQTY; LLHHWQTYL; LHHWQTYLH; HHWQTYLHG; HWQTYLHGK; WQTYLHGKI; QTYLHGKIN; TYLHGKINL; YLHGKINLH; LHGKINLHP; HGKINLHPI; GKINLHPIF; KINLHPIFH; RNSTRTPTL; NSTRTPTLL; STRTPTLLF; TRTPTLLFH; RTPTLLFHR; TPTLLFHRL; PTLLFHRLA; TLLFHRLAP; LLFHRLAPI; LFHRLAPIK; FHRLAPIKK; HRLAPIKKI; RLAPIKKII; LAPIKKIIT; GLLIFYYLS; LLIFYYLSK; LIFYYLSKY; IFYYLSKYK; FYYLSKYKL; YYLSKYKLV; YLSKYKLVT; LSKYKLVTL; SKYKLVTLK; KYKLVTLKL; ISEGSFSNY; SEGSFSNYL; EGSFSNYLD; GSFSNYLDP; SFSNYLDPP; FSNYLDPPL; SNYLDPPLQ; NYLDPPLQS; YLDPPLQSF; LDPPLQSFF; DPPLQSFFS; AKPLCEAVN; KPLCEAVNA; PLCEAVNAV; LCEAVNAVA; CEAVNAVAI; EAVNAVAIY; AVNAVAIYP; VNAVAIYPN; NAVAIYPNQ; AVAIYPNQG; VAIYPNQGL; AIYPNQGLF; IYPNQGLFS; HARAVHRRL; ARAVHRRLF; RAVHRRLFG; AVHRRLFGT; VHRRLFGTN; HRRLFGTNR; RRLFGTNRP; RLFGTNRPF; LFGTNRPFL; FGTNRPFLA; GTNRPFLAV; TNRPFLAVQ; NRPFLAVQG; RPFLAVQGI; PFLAVQGIW; FLAVQGIWA; LAVQGIWAK; AVQGIWAKR; VQGIWAKRK; QGIWAKRKI; GIWAKRKIS; IWAKRKIST; WAKRKISTN; AKRKISTNL; ATPGSKIRL; TPGSKIRLM; PGSKIRLMS; GSKIRLMSY; SKIRLMSYL; KIRLMSYLY; IRLMSYLYI; RLMSYLYIL; LMSYLYILL; MSYLYILLH; SYLYILLHF; YLYILLHFF; LYILLHFFI; YILLHFFIQ; ILLHFFIQS; LLHFFIQSI; LHFFIQSIH; HFFIQSIHS; FFIQSIHSL; FIQSIHSLH; IQSIHSLHF; QSIHSLHFI; SIHSLHFIL; IHSLHFILV; HSLHFILVA; SLHFILVAP; LHFILVAPF; HFILVAPFV; FILVAPFVR; ILVAPFVRV; LVAPFVRVK; VAPFVRVKF; APFVRVKFL; PFVRVKFLT; FVRVKFLTL; VRVKFLTLP; GKISPGSSF; KISPGSSFK; ISPGSSFKA; KVHELHGFF; VHELHGFFP; HELHGFFPV; ELHGFFPVK; LHGFFPVKN; HGFFPVKNF; GFFPVKNFI; FFPVKNFIH 10 mers: LQKLQKNRDF; QKLQKNRDFP; KLQKNRDFPK; ASEKASTPLL; SEKASTPLLL; EKASTPLLLE; KASTPLLLER; ASTPLLLERK; STPLLLERKG; TPLLLERKGG; PLLLERKGGG; LLLERKGGGR; LLERKGGGRG; LERKGGGRGG; ERKGGGRGGL; RKGGGRGGLG; KGGGRGGLGL; GGGRGGLGLL; GGRGGLGLLY; GRGGLGLLYI; RGGLGLLYII; GGLGLLYIIK; GLGLLYIIKK; LGLLYIIKKK; GLLYIIKKKA; LLYIIKKKAT; LYIIKKKATG; YIIKKKATGR; IIKKKATGRS; IKKKATGRSC; KKKATGRSCL; KKATGRSCLP; KATGRSCLPM; ATGRSCLPME; TGRSCLPMEC; GRSCLPMECS; RSCLPMECSQ; SCLPMECSQT; CLPMECSQTM; LPMECSQTMT; PMECSQTMTS; MECSQTMTSG; ECSQTMTSGR; CSQTMTSGRK; SQTMTSGRKV; QTMTSGRKVH; TMTSGRKVHD; MTSGRKVHDS; TSGRKVHDSQ; SGRKVHDSQG; GRKVHDSQGN; RKVHDSQGNA; KVHDSQGNAA; VHDSQGNAAK; HDSQGNAAKP; PQEGKCMTHR; QEGKCMTHRE; EGKCMTHREE; GKCMTHREEL; KCMTHREELL; CMTHREELLT; MTHREELLTH; THREELLTHG; HREELLTHGM; REELLTHGMQ; EELLTHGMQP; ELLTHGMQPN; LLTHGMQPNH; LTHGMQPNHD; THGMQPNHDL; HGMQPNHDLR; GMQPNHDLRK; MQPNHDLRKE; QPNHDLRKES; PNHDLRKESA; QTCFASLGIL; TCFASLGILA; CFASLGILAL; FASLGILALS; ASLGILALSP; SLGILALSPV; LGILALSPVK; GILALSPVKL; ILALSPVKLD; LALSPVKLDK; ALSPVKLDKG; LSPVKLDKGH; SPVKLDKGHG; PVKLDKGHGS; VKLDKGHGSA; KLDKGHGSAP; LDKGHGSAPA; DKGHGSAPAV; KGHGSAPAVT; GHGSAPAVTT; HGSAPAVTTS; GSAPAVTTSF; SAPAVTTSFS; APAVTTSFSE; PAVTTSFSES; AVTTSFSESW; NLDWNKKKSS; LDWNKKKSSE; DWNKKKSSED; WNKKKSSEDF; NKKKSSEDFY; KKKSSEDFYF; KKSSEDFYFY; KSSEDFYFYF; SSEDFYFYFR; SEDFYFYFRA; EDFYFYFRAF; DFYFYFRAFA; FYFYFRAFAG; YFYFRAFAGI; FYFRAFAGIL; RQCRREKQKY; QCRREKQKYH; CRREKQKYHC; RREKQKYHCF; REKQKYHCFT; EKQKYHCFTC; KQKYHCFTCC; QKYHCFTCCK; KYHCFTCCKR; YHCFTCCKRL; HCFTCCKRLC; CFTCCKRLCK; FTCCKRLCKR; TCCKRLCKRL; CCKRLCKRLL; CKRLCKRLLG; KRLCKRLLGK; SLFFCISRFM; LFFCISRFMG; FFCISRFMGA; FCISRFMGAA; CISRFMGAAL; ISRFMGAALA; SRFMGAALAL; RFMGAALALL; FMGAALALLG; MGAALALLGD; GAALALLGDL; AALALLGDLV; ALALLGDLVA; LALLGDLVAS; ALLGDLVASV; LLGDLVASVS; LGDLVASVSE; GDLVASVSEA; DLVASVSEAA; LVASVSEAAA; VASVSEAAAA; ASVSEAAAAT; SVSEAAAATG; VSEAAAATGF; SEAAAATGFS; EAAAATGFSV; AAAATGFSVA; AAATGFSVAE; AATGFSVAEI; ATGFSVAEIA; TGFSVAEIAA; GFSVAEIAAG; FSVAEIAAGE; SVAEIAAGEA; VAEIAAGEAA; AEIAAGEAAA; EIAAGEAAAA; IAAGEAAAAI; AAGEAAAAIE; AGEAAAAIEV; GEAAAAIEVQ; EAAAAIEVQI; AAAAIEVQIA; AAAIEVQIAS; AAIEVQIASL; AIEVQIASLA; IEVQIASLAT; EVQIASLATV; VQIASLATVE; QIASLATVEG; IASLATVEGI; ASLATVEGIT; SLATVEGITS; LATVEGITST; ATVEGITSTS; TVEGITSTSE; VEGITSTSEA; EGITSTSEAI; GITSTSEAIA; ITSTSEAIAA; TSTSEAIAAI; STSEAIAAIG; TSEAIAAIGL; SEAIAAIGLT; EAIAAIGLTP; AIAAIGLTPQ; IAAIGLTPQT; AAIGLTPQTY; AIGLTPQTYA; IGLTPQTYAV; GLTPQTYAVI; LTPQTYAVIA; TPQTYAVIAG; PQTYAVIAGA; QTYAVIAGAP; TYAVIAGAPG; YAVIAGAPGA; AVIAGAPGAI; VIAGAPGAIA; IAGAPGAIAG; AGAPGAIAGF; GAPGAIAGFA; APGAIAGFAA; PGAIAGFAAL; GAIAGFAALI; AIAGFAALIQ; IAGFAALIQT; AGFAALIQTV; GFAALIQTVS; FAALIQTVSG; AALIQTVSGI; ALIQTVSGIS; LIQTVSGISS; IQTVSGISSL; QTVSGISSLA; TVSGISSLAQ; VSGISSLAQV; SGISSLAQVG; GISSLAQVGY; ISSLAQVGYK; SSLAQVGYKF; SLAQVGYKFF; LAQVGYKFFD; AQVGYKFFDD; QVGYKFFDDW; VGYKFFDDWD; GYKFFDDWDH; YKFFDDWDHK; KFFDDWDHKV; FFDDWDHKVS; FDDWDHKVST; DDWDHKVSTV; DWDHKVSTVG; WDHKVSTVGL; DHKVSTVGLY; HKVSTVGLYQ; KVSTVGLYQQ; VSTVGLYQQS; STVGLYQQSG; TVGLYQQSGM; VGLYQQSGMA; GLYQQSGMAL; LYQQSGMALE; YQQSGMALEL; QQSGMALELF; QSGMALELFN; SGMALELFNP; GMALELFNPD; MALELFNPDE; ALELFNPDEY; LELFNPDEYY; ELFNPDEYYD; LFNPDEYYDI; FNPDEYYDIL; NPDEYYDILF; PDEYYDILFP; DEYYDILFPG; EYYDILFPGV; YYDILFPGVN; YDILFPGVNT; DILFPGVNTF; ILFPGVNTFV; LFPGVNTFVN; FPGVNTFVNN; PGVNTFVNNI; GVNTFVNNIQ; VNTFVNNIQY; NTFVNNIQYL; TFVNNIQYLD; FVNNIQYLDP; VNNIQYLDPR; NNIQYLDPRH; NIQYLDPRHW; IQYLDPRHWG; QYLDPRHWGP; YLDPRHWGPS; LDPRHWGPSL; DPRHWGPSLF; PRHWGPSLFA; RHWGPSLFAT; HWGPSLFATI; WGPSLFATIS; GPSLFATISQ; PSLFATISQA; SLFATISQAL; LFATISQALW; FATISQALWH; ATISQALWHV; TISQALWHVI; ISQALWHVIR; SQALWHVIRD; QALWHVIRDD; ALWHVIRDDI; LWHVIRDDIP; WHVIRDDIPS; HVIRDDIPSI; VIRDDIPSIT; IRDDIPSITS; RDDIPSITSQ; DDIPSITSQE; DIPSITSQEL; IPSITSQELQ; PSITSQELQR; SITSQELQRR; ITSQELQRRT; TSQELQRRTE; SQELQRRTER; QELQRRTERF; ELQRRTERFF; LQRRTERFFR; QRRTERFFRD; RRTERFFRDS; RTERFFRDSL; TERFFRDSLA; ERFFRDSLAR; RFFRDSLARF; FFRDSLARFL; FRDSLARFLE; RDSLARFLEE; DSLARFLEET; SLARFLEETT; LARFLEETTW; ARFLEETTWT; RFLEETTWTI; FLEETTWTIV; LEETTWTIVN; EETTWTIVNA; ETTWTIVNAP; TTWTIVNAPI; TWTIVNAPIN; WTIVNAPINF; TIVNAPINFY; IVNAPINFYN; VNAPINFYNY; NAPINFYNYI; APINFYNYIQ; PINFYNYIQQ; INFYNYIQQY; NFYNYIQQYY; FYNYIQQYYS; YNYIQQYYSD; NYIQQYYSDL; YIQQYYSDLS; IQQYYSDLSP; QQYYSDLSPI; QYYSDLSPIR; YYSDLSPIRP; YSDLSPIRPS; SDLSPIRPSM; DLSPIRPSMV; LSPIRPSMVR; SPIRPSMVRQ; PIRPSMVRQV; IRPSMVRQVA; RPSMVRQVAE; PSMVRQVAER; SMVRQVAERE; MVRQVAEREG; VRQVAEREGT; RQVAEREGTR; QVAEREGTRV; VAEREGTRVH; AEREGTRVHF; EREGTRVHFG; REGTRVHFGH; EGTRVHFGHT; GTRVHFGHTY; TRVHFGHTYS; RVHFGHTYSI; VHFGHTYSID; HFGHTYSIDD; FGHTYSIDDA; GHTYSIDDAD; HTYSIDDADS; TYSIDDADSI; YSIDDADSIE; SIDDADSIEE; IDDADSIEEV; DDADSIEEVT; DADSIEEVTQ; ADSIEEVTQR; DSIEEVTQRM; SIEEVTQRMD; IEEVTQRMDL; EEVTQRMDLR; EVTQRMDLRN; VTQRMDLRNQ; TQRMDLRNQQ; QRMDLRNQQS; RMDLRNQQSV; MDLRNQQSVH; DLRNQQSVHS; LRNQQSVHSG; RNQQSVHSGE; NQQSVHSGEF; QQSVHSGEFI; QSVHSGEFIE; SVHSGEFIEK; VHSGEFIEKT; HSGEFIEKTI; SGEFIEKTIA; GEFIEKTIAP; EFIEKTIAPG; FIEKTIAPGG; IEKTIAPGGA; EKTIAPGGAN; KTIAPGGANQ; TIAPGGANQR; IAPGGANQRT; APGGANQRTA; PGGANQRTAP; GGANQRTAPQ; GANQRTAPQW; ANQRTAPQWM; NQRTAPQWML; QRTAPQWMLP; RTAPQWMLPL; TAPQWMLPLL; APQWMLPLLL; PQWMLPLLLG; QWMLPLLLGL; WMLPLLLGLY; MLPLLLGLYG; LPLLLGLYGT; PLLLGLYGTV; LLLGLYGTVT; LLGLYGTVTP; LGLYGTVTPA; GLYGTVTPAL; LYGTVTPALE; YGTVTPALEA; GTVTPALEAY; TVTPALEAYE; VTPALEAYED; TPALEAYEDG; PALEAYEDGP; ALEAYEDGPN; LEAYEDGPNQ; EAYEDGPNQK; AYEDGPNQKK; YEDGPNQKKR; EDGPNQKKRR; DGPNQKKRRV; GPNQKKRRVS; PNQKKRRVSR; NQKKRRVSRG; QKKRRVSRGS; KKRRVSRGSS; KRRVSRGSSQ; RRVSRGSSQK; RVSRGSSQKA; VSRGSSQKAK; SRGSSQKAKG; RGSSQKAKGT; GSSQKAKGTR; SSQKAKGTRA; SQKAKGTRAS; QKAKGTRASA; KAKGTRASAK; AKGTRASAKT; KGTRASAKTT; GTRASAKTTN; TRASAKTTNK; RASAKTTNKR; ASAKTTNKRR; SAKTTNKRRS; AKTTNKRRSR; KTTNKRRSRS; TTNKRRSRSS; TNKRRSRSSR; NKRRSRSSRS; NWGRCYYRGR; WGRCYYRGRM; GRCYYRGRML; RCYYRGRMLP; CYYRGRMLPK; YYRGRMLPKP; YRGRMLPKPR; RGRMLPKPRN; GRMLPKPRNG; RMLPKPRNGG; MLPKPRNGGS; LPKPRNGGSR; PREKNASLLQ; REKNASLLQH; EKNASLLQHS; KNASLLQHSK; NASLLQHSKN; ASLLQHSKNS; SLLQHSKNSP; LLQHSKNSPP; LQHSKNSPPQ; QHSKNSPPQF; HSKNSPPQFK; GPNLWKSTDV; PNLWKSTDVG; NLWKSTDVGG; LWKSTDVGGC; WKSTDVGGCN; KSTDVGGCNC; STDVGGCNCT; TDVGGCNCTN; DVGGCNCTNR; VGGCNCTNRG; GGCNCTNRGY; GCNCTNRGYW; CNCTNRGYWN; NCTNRGYWNN; AWWRKTYSRQ; FPLLCCRWRT; PLLCCRWRTL; LLCCRWRTLG; LCCRWRTLGN; CCRWRTLGNA; CRWRTLGNAG; RWRTLGNAGS; WRTLGNAGSA; RTLGNAGSAN; TLGNAGSANE; LGNAGSANEL; GNAGSANELQ; NAGSANELQV; AGSANELQVK; GSANELQVKV; SANELQVKVP; KPNSPVPGNE; PNSPVPGNEY; GLFGQKQCLS; LFGQKQCLSS; VFWDFHRRGK; FWDFHRRGKC; WDFHRRGKCS; DFHRRGKCSP; FHRRGKCSPS; HRRGKCSPST; RRGKCSPSTS; RGKCSPSTSC; GKCSPSTSCD; KCSPSTSCDQ; CSPSTSCDQH; SPSTSCDQHS; PSTSCDQHSY; STSCDQHSYH; TSCDQHSYHS; SCDQHSYHSV; CDQHSYHSVA; DQHSYHSVAR; QLWNTTVERP; LWNTTVERPC; WNTTVERPCK; NTTVERPCKI; TTVERPCKIF; DPPEKKICKE; PPEKKICKES; PEKKICKESL; EKKICKESLP; KKICKESLPN; KICKESLPNF; ICKESLPNFL; CKESLPNFLF; KESLPNFLFA; ESLPNFLFAK; PYKQENPESG; YKQENPESGW; KQENPESGWA; QENPESGWAA; ENPESGWAAY; NPESGWAAYV; PESGWAAYVW; ESGWAAYVWY; SGWAAYVWYG; GWAAYVWYGI; WAAYVWYGIP; AAYVWYGIPG; AYVWYGIPGR; YVWYGIPGRR; VWYGIPGRRG; WHRKTSRGPR; HRKTSRGPRY; RKTSRGPRYD; KTSRGPRYDK; TSRGPRYDKI; SRGPRYDKIY; QTGTIANQNA; TGTIANQNAL; GTIANQNALN; TIANQNALNR; IANQNALNRC; ANQNALNRCF; NQNALNRCFY; QNALNRCFYC; NALNRCFYCT; ALNRCFYCTY; LNRCFYCTYT; NRCFYCTYTF; RCFYCTYTFN; CFYCTYTFNK; FYCTYTFNKC; YCTYTFNKCC; CTYTFNKCCF; TYTFNKCCFC; YTFNKCCFCI; TFNKCCFCIS; FNKCCFCISH; NKCCFCISHF; NTESLYTNAT; TESLYTNATL; ESLYTNATLD; SLYTNATLDY; LYTNATLDYG; YTNATLDYGG; TNATLDYGGL; NATLDYGGLT; ATLDYGGLTF; TLDYGGLTFG; LDYGGLTFGN; DYGGLTFGNL; YGGLTFGNLQ; GGLTFGNLQQ; GLTFGNLQQG; LTFGNLQQGL; TFGNLQQGLK; FGNLQQGLKY; GNLQQGLKYL; NLQQGLKYLR; LQQGLKYLRL; QQGLKYLRLG; QGLKYLRLGK; GLKYLRLGKS; LKYLRLGKSI; KYLRLGKSIV; YLRLGKSIVI; LRLGKSIVIG; RLGKSIVIGI; LGKSIVIGIQ; GKSIVIGIQC; KSIVIGIQCL; SIVIGIQCLI; IVIGIQCLIH; VIGIQCLIHV; IGIQCLIHVQ; GIQCLIHVQS; IQCLIHVQSL; QCLIHVQSLQ; CLIHVQSLQF; LIHVQSLQFL; IHVQSLQFLN; HVQSLQFLNP; VQSLQFLNPL; QSLQFLNPLL; SLQFLNPLLL; YQEYISPCIY; QEYISPCIYY; EYISPCIYYI; YISPCIYYIS; ISPCIYYISS; SPCIYYISSL; PCIYYISSLK; CIYYISSLKK; IYYISSLKKY; YYISSLKKYT; YISSLKKYTY; ISSLKKYTYL; SSLKKYTYLS; SLKKYTYLSQ; LKKYTYLSQN; KKYTYLSQNP; KYTYLSQNPA; YTYLSQNPAF; TYLSQNPAFP; YLSQNPAFPS; LSQNPAFPSI; SQNPAFPSIQ; QNPAFPSIQQ; NPAFPSIQQF; IVYQLQNQLQ; VYQLQNQLQA; TKLAVATRSF; KLAVATRSFH; LAVATRSFHF; AVATRSFHFV; VATRSFHFVK; ATRSFHFVKF; TRSFHFVKFF; RSFHFVKFFF; SFHFVKFFFQ; FHFVKFFFQV; HFVKFFFQVR; FVKFFFQVRT; VKFFFQVRTL; KFFFQVRTLS; FFFQVRTLSF; FFQVRTLSFV; FQVRTLSFVR; QVRTLSFVRI; VRTLSFVRIF; RTLSFVRIFL; TLSFVRIFLN; LSFVRIFLNI; SFVRIFLNIF; FVRIFLNIFW; VRIFLNIFWA; PSLVEIFGFF; SLVEIFGFFC; LVEIFGFFCL; VEIFGFFCLN; EIFGFFCLNV; IFGFFCLNVS; FGFFCLNVSF; GFFCLNVSFL; FFCLNVSFLN; FCLNVSFLNL; CLNVSFLNLP; HFHLNNLSNC; FHLNNLSNCL; HLNNLSNCLN; LNNLSNCLNC; NNLSNCLNCL; NLSNCLNCLF; LSNCLNCLFH; SNCLNCLFHV; NCLNCLFHVL; CLNCLFHVLK; LNCLFHVLKA; NCLFHVLKAN; CLFHVLKANP; LFHVLKANPL; FHVLKANPLI; HVLKANPLIQ; VLKANPLIQL; LKANPLIQLL; KANPLIQLLS; ANPLIQLLSL; NPLIQLLSLL; PLIQLLSLLH; LIQLLSLLHL; IQLLSLLHLQ; QLLSLLHLQK; LLSLLHLQKQ; LSLLHLQKQP; SLLHLQKQPC; LLHLQKQPCT; LHLQKQPCTD; HLQKQPCTDL; LHLAQRLAFP; HLAQRLAFPW; LAQRLAFPWV; AQRLAFPWVG; QRLAFPWVGL; RLAFPWVGLH; LAFPWVGLHL; AFPWVGLHLR; FPWVGLHLRL; PWVGLHLRLY; WVGLHLRLYH; VGLHLRLYHH; GLHLRLYHHT; LHLRLYHHTN; HLRLYHHTNL; LRLYHHTNLI; RLYHHTNLIT; LYHHTNLITL; YHHTNLITLQ; HHTNLITLQL; HTNLITLQLV; TNLITLQLVL; NLITLQLVLF; LITLQLVLFF; ITLQLVLFFH; TLQLVLFFHY; LQLVLFFHYQ; QLVLFFHYQW; LVLFFHYQWD; VLFFHYQWDL; KQYSAKNQIL; QYSAKNQILQ; YSAKNQILQN; SAKNQILQNP; AKNQILQNPF; VANSAAKQHL; ANSAAKQHLP; NSAAKQHLPY; SAAKQHLPYI; AAKQHLPYIV; AKQHLPYIVL; KQHLPYIVLV; QHLPYIVLVQ; HLPYIVLVQH; LPYIVLVQHF; PYIVLVQHFH; YIVLVQHFHE; IVLVQHFHEL; VLVQHFHELQ; LVQHFHELQI; VQHFHELQIL; QHFHELQILN; HFHELQILNP; FHELQILNPF; HELQILNPFY; ELQILNPFYL; LQILNPFYLI; QILNPFYLIY; ILNPFYLIYD; IFLLAFLPWS; FLLAFLPWSY; LLAFLPWSYE; LAFLPWSYEG; AFLPWSYEGY; FLPWSYEGYL; LPWSYEGYLL; PWSYEGYLLF; WSYEGYLLFF; LKLYLLLADK; KLYLLLADKY; LYLLLADKYF; YLLLADKYFF; LLLADKYFFD; LLADKYFFDF; LADKYFFDFY; ADKYFFDFYF; DKYFFDFYFL; KYFFDFYFLQ; YFFDFYFLQK; SDKAGLFSDT; DKAGLFSDTF; KAGLFSDTFY; AGLFSDTFYT; GLFSDTFYTP; LFSDTFYTPL; FSDTFYTPLH; SDTFYTPLHC; DTFYTPLHCI; TFYTPLHCIE; FYTPLHCIEI; YTPLHCIEIL; TPLHCIEILN; PLHCIEILNT; LHCIEILNTY; HCIEILNTYL; CIEILNTYLI; IEILNTYLII; EILNTYLIIK; ILNTYLIIKT; LNTYLIIKTH; NTYLIIKTHP; TYLIIKTHPH; YLIIKTHPHT; LIIKTHPHTL; IIKTHPHTLS; IKTHPHTLSL; KTHPHTLSLL; THPHTLSLLH; HPHTLSLLHT; PHTLSLLHTQ; LISKTPALFL; ISKTPALFLQ; SKTPALFLQA; KTPALFLQAL; TPALFLQALL; PALFLQALLG; NHAPLSPLEC; HAPLSPLECF; APLSPLECFL; PLSPLECFLL; LRHYIVSIPY; LQKLYVYVEL; QKLYVYVELK; KLYVYVELKR; LYVYVELKRI; VFYTEFELFL; YTQQSRQGFY; TQQSRQGFYY; ETGVDQRESL; GLLPFFFFWV; LLPFFFFWVV; LPFFFFWVVL; PFFFFWVVLS; FFFFWVVLSV; FFFWVVLSVE; FFWVVLSVEN; FWVVLSVENL; WVVLSVENLL; VVLSVENLLL; VLSVENLLLL; LSVENLLLLL; SVENLLLLLH; VENLLLLLHH; ENLLLLLHHW; NLLLLLHHWQ; LLLLLHHWQT; LLLLHHWQTY; LLLHHWQTYL; LLHHWQTYLH; LHHWQTYLHG; HHWQTYLHGK; HWQTYLHGKI; WQTYLHGKIN; QTYLHGKINL; TYLHGKINLH; YLHGKINLHP; LHGKINLHPI; HGKINLHPIF; GKINLHPIFH; RNSTRTPTLL; NSTRTPTLLF; STRTPTLLFH; TRTPTLLFHR; RTPTLLFHRL; TPTLLFHRLA; PTLLFHRLAP; TLLFHRLAPI; LLFHRLAPIK; LFHRLAPIKK; FHRLAPIKKI; HRLAPIKKII; RLAPIKKIIT; GLLIFYYLSK; LLIFYYLSKY; LIFYYLSKYK; IFYYLSKYKL; FYYLSKYKLV; YYLSKYKLVT; YLSKYKLVTL; LSKYKLVTLK; SKYKLVTLKL; ISEGSFSNYL; SEGSFSNYLD; EGSFSNYLDP; GSFSNYLDPP; SFSNYLDPPL; FSNYLDPPLQ; SNYLDPPLQS; NYLDPPLQSF; YLDPPLQSFF; LDPPLQSFFS; AKPLCEAVNA; KPLCEAVNAV; PLCEAVNAVA; LCEAVNAVAI; CEAVNAVAIY; EAVNAVAIYP; AVNAVAIYPN; VNAVAIYPNQ; NAVAIYPNQG; AVAIYPNQGL; VAIYPNQGLF; AIYPNQGLFS; HARAVHRRLF; ARAVHRRLFG; RAVHRRLFGT; AVHRRLFGTN; VHRRLFGTNR; HRRLFGTNRP; RRLFGTNRPF; RLFGTNRPFL; LFGTNRPFLA; FGTNRPFLAV; GTNRPFLAVQ; TNRPFLAVQG; NRPFLAVQGI; RPFLAVQGIW; PFLAVQGIWA; FLAVQGIWAK; LAVQGIWAKR; AVQGIWAKRK; VQGIWAKRKI; QGIWAKRKIS; GIWAKRKIST; IWAKRKISTN; WAKRKISTNL; ATPGSKIRLM; TPGSKIRLMS; PGSKIRLMSY; GSKIRLMSYL; SKIRLMSYLY; KIRLMSYLYI; IRLMSYLYIL; RLMSYLYILL; LMSYLYILLH; MSYLYILLHF; SYLYILLHFF; YLYILLHFFI; LYILLHFFIQ; YILLHFFIQS; ILLHFFIQSI; LLHFFIQSIH; LHFFIQSIHS; HFFIQSIHSL; FFIQSIHSLH; FIQSIHSLHF; IQSIHSLHFI; QSIHSLHFIL; SIHSLHFILV; IHSLHFILVA; HSLHFILVAP; SLHFILVAPF; LHFILVAPFV; HFILVAPFVR; FILVAPFVRV; ILVAPFVRVK; LVAPFVRVKF; VAPFVRVKFL; APFVRVKFLT; PFVRVKFLTL; FVRVKFLTLP; GKISPGSSFK; KISPGSSFKA; KVHELHGFFP; VHELHGFFPV; HELHGFFPVK; ELHGFFPVKN; LHGFFPVKNF; HGFFPVKNFI; GFFPVKNFIH 11 mers: LQKLQKNRDFP; QKLQKNRDFPK; ASEKASTPLLL; SEKASTPLLLE; EKASTPLLLER; KASTPLLLERK; ASTPLLLERKG; STPLLLERKGG; TPLLLERKGGG; PLLLERKGGGR; LLLERKGGGRG; LLERKGGGRGG; LERKGGGRGGL; ERKGGGRGGLG; RKGGGRGGLGL; KGGGRGGLGLL; GGGRGGLGLLY; GGRGGLGLLYI; GRGGLGLLYII; RGGLGLLYIIK; GGLGLLYIIKK; GLGLLYIIKKK; LGLLYIIKKKA; GLLYIIKKKAT; LLYIIKKKATG; LYIIKKKATGR; YIIKKKATGRS; IIKKKATGRSC; IKKKATGRSCL; KKKATGRSCLP; KKATGRSCLPM; KATGRSCLPME; ATGRSCLPMEC; TGRSCLPMECS; GRSCLPMECSQ; RSCLPMECSQT; SCLPMECSQTM; CLPMECSQTMT; LPMECSQTMTS; PMECSQTMTSG; MECSQTMTSGR; ECSQTMTSGRK; CSQTMTSGRKV; SQTMTSGRKVH; QTMTSGRKVHD; TMTSGRKVHDS; MTSGRKVHDSQ; TSGRKVHDSQG; SGRKVHDSQGN; GRKVHDSQGNA; RKVHDSQGNAA; KVHDSQGNAAK; VHDSQGNAAKP; PQEGKCMTHRE; QEGKCMTHREE; EGKCMTHREEL; GKCMTHREELL; KCMTHREELLT; CMTHREELLTH; MTHREELLTHG; THREELLTHGM; HREELLTHGMQ; REELLTHGMQP; EELLTHGMQPN; ELLTHGMQPNH; LLTHGMQPNHD; LTHGMQPNHDL; THGMQPNHDLR; HGMQPNHDLRK; GMQPNHDLRKE; MQPNHDLRKES; QPNHDLRKESA; QTCFASLGILA; TCFASLGILAL; CFASLGILALS; FASLGILALSP; ASLGILALSPV; SLGILALSPVK; LGILALSPVKL; GILALSPVKLD; ILALSPVKLDK; LALSPVKLDKG; ALSPVKLDKGH; LSPVKLDKGHG; SPVKLDKGHGS; PVKLDKGHGSA; VKLDKGHGSAP; KLDKGHGSAPA; LDKGHGSAPAV; DKGHGSAPAVT; KGHGSAPAVTT; GHGSAPAVTTS; HGSAPAVTTSF; GSAPAVTTSFS; SAPAVTTSFSE; APAVTTSFSES; PAVTTSFSESW; NLDWNKKKSSE; LDWNKKKSSED; DWNKKKSSEDF; WNKKKSSEDFY; NKKKSSEDFYF; KKKSSEDFYFY; KKSSEDFYFYF; KSSEDFYFYFR; SSEDFYFYFRA; SEDFYFYFRAF; EDFYFYFRAFA; DFYFYFRAFAG; FYFYFRAFAGI; YFYFRAFAGIL; RQCRREKQKYH; QCRREKQKYHC; CRREKQKYHCF; RREKQKYHCFT; REKQKYHCFTC; EKQKYHCFTCC; KQKYHCFTCCK; QKYHCFTCCKR; KYHCFTCCKRL; YHCFTCCKRLC; HCFTCCKRLCK; CFTCCKRLCKR; FTCCKRLCKRL; TCCKRLCKRLL; CCKRLCKRLLG; CKRLCKRLLGK; SLFFCISRFMG; LFFCISRFMGA; FFCISRFMGAA; FCISRFMGAAL; CISRFMGAALA; ISRFMGAALAL; SRFMGAALALL; RFMGAALALLG; FMGAALALLGD; MGAALALLGDL; GAALALLGDLV; AALALLGDLVA; ALALLGDLVAS; LALLGDLVASV; ALLGDLVASVS; LLGDLVASVSE; LGDLVASVSEA; GDLVASVSEAA; DLVASVSEAAA; LVASVSEAAAA; VASVSEAAAAT; ASVSEAAAATG; SVSEAAAATGF; VSEAAAATGFS; SEAAAATGFSV; EAAAATGFSVA; AAAATGFSVAE; AAATGFSVAEI; AATGFSVAEIA; ATGFSVAEIAA; TGFSVAEIAAG; GFSVAEIAAGE; FSVAEIAAGEA; SVAEIAAGEAA; VAEIAAGEAAA; AEIAAGEAAAA; EIAAGEAAAAI; IAAGEAAAAIE; AAGEAAAAIEV; AGEAAAAIEVQ; GEAAAAIEVQI; EAAAAIEVQIA; AAAAIEVQIAS; AAAIEVQIASL; AAIEVQIASLA; AIEVQIASLAT; IEVQIASLATV; EVQIASLATVE; VQIASLATVEG; QIASLATVEGI; IASLATVEGIT; ASLATVEGITS; SLATVEGITST; LATVEGITSTS; ATVEGITSTSE; TVEGITSTSEA; VEGITSTSEAI; EGITSTSEAIA; GITSTSEAIAA; ITSTSEAIAAI; TSTSEAIAAIG; STSEAIAAIGL; TSEAIAAIGLT; SEAIAAIGLTP; EAIAAIGLTPQ; AIAAIGLTPQT; IAAIGLTPQTY; AAIGLTPQTYA; AIGLTPQTYAV; IGLTPQTYAVI; GLTPQTYAVIA; LTPQTYAVIAG; TPQTYAVIAGA; PQTYAVIAGAP; QTYAVIAGAPG; TYAVIAGAPGA; YAVIAGAPGAI; AVIAGAPGAIA; VIAGAPGAIAG; IAGAPGAIAGF; AGAPGAIAGFA; GAPGAIAGFAA; APGAIAGFAAL; PGAIAGFAALI; GAIAGFAALIQ; AIAGFAALIQT; IAGFAALIQTV; AGFAALIQTVS; GFAALIQTVSG; FAALIQTVSGI; AALIQTVSGIS; ALIQTVSGISS; LIQTVSGISSL; IQTVSGISSLA; QTVSGISSLAQ; TVSGISSLAQV; VSGISSLAQVG; SGISSLAQVGY; GISSLAQVGYK; ISSLAQVGYKF; SSLAQVGYKFF; SLAQVGYKFFD; LAQVGYKFFDD; AQVGYKFFDDW; QVGYKFFDDWD; VGYKFFDDWDH; GYKFFDDWDHK; YKFFDDWDHKV; KFFDDWDHKVS; FFDDWDHKVST; FDDWDHKVSTV; DDWDHKVSTVG; DWDHKVSTVGL; WDHKVSTVGLY; DHKVSTVGLYQ; HKVSTVGLYQQ; KVSTVGLYQQS; VSTVGLYQQSG; STVGLYQQSGM; TVGLYQQSGMA; VGLYQQSGMAL; GLYQQSGMALE; LYQQSGMALEL; YQQSGMALELF; QQSGMALELFN; QSGMALELFNP; SGMALELFNPD; GMALELFNPDE; MALELFNPDEY; ALELFNPDEYY; LELFNPDEYYD; ELFNPDEYYDI; LFNPDEYYDIL; FNPDEYYDILF; NPDEYYDILFP; PDEYYDILFPG; DEYYDILFPGV; EYYDILFPGVN; YYDILFPGVNT; YDILFPGVNTF; DILFPGVNTFV; ILFPGVNTFVN; LFPGVNTFVNN; FPGVNTFVNNI; PGVNTFVNNIQ; GVNTFVNNIQY; VNTFVNNIQYL; NTFVNNIQYLD; TFVNNIQYLDP; FVNNIQYLDPR; VNNIQYLDPRH; NNIQYLDPRHW; NIQYLDPRHWG; IQYLDPRHWGP; QYLDPRHWGPS; YLDPRHWGPSL; LDPRHWGPSLF; DPRHWGPSLFA; PRHWGPSLFAT; RHWGPSLFATI; HWGPSLFATIS; WGPSLFATISQ; GPSLFATISQA; PSLFATISQAL; SLFATISQALW; LFATISQALWH; FATISQALWHV; ATISQALWHVI; TISQALWHVIR; ISQALWHVIRD; SQALWHVIRDD; QALWHVIRDDI; ALWHVIRDDIP; LWHVIRDDIPS; WHVIRDDIPSI; HVIRDDIPSIT; VIRDDIPSITS; IRDDIPSITSQ; RDDIPSITSQE; DDIPSITSQEL; DIPSITSQELQ; IPSITSQELQR; PSITSQELQRR; SITSQELQRRT; ITSQELQRRTE; TSQELQRRTER; SQELQRRTERF; QELQRRTERFF; ELQRRTERFFR; LQRRTERFFRD; QRRTERFFRDS; RRTERFFRDSL; RTERFFRDSLA; TERFFRDSLAR; ERFFRDSLARF; RFFRDSLARFL; FFRDSLARFLE; FRDSLARFLEE; RDSLARFLEET; DSLARFLEETT; SLARFLEETTW; LARFLEETTWT; ARFLEETTWTI; RFLEETTWTIV; FLEETTWTIVN; LEETTWTIVNA; EETTWTIVNAP; ETTWTIVNAPI; TTWTIVNAPIN; TWTIVNAPINF; WTIVNAPINFY; TIVNAPINFYN; IVNAPINFYNY; VNAPINFYNYI; NAPINFYNYIQ; APINFYNYIQQ; PINFYNYIQQY; INFYNYIQQYY; NFYNYIQQYYS; FYNYIQQYYSD; YNYIQQYYSDL; NYIQQYYSDLS; YIQQYYSDLSP; IQQYYSDLSPI; QQYYSDLSPIR; QYYSDLSPIRP; YYSDLSPIRPS; YSDLSPIRPSM; SDLSPIRPSMV; DLSPIRPSMVR; LSPIRPSMVRQ; SPIRPSMVRQV; PIRPSMVRQVA; IRPSMVRQVAE; RPSMVRQVAER; PSMVRQVAERE; SMVRQVAEREG; MVRQVAEREGT; VRQVAEREGTR; RQVAEREGTRV; QVAEREGTRVH; VAEREGTRVHF; AEREGTRVHFG; EREGTRVHFGH; REGTRVHFGHT; EGTRVHFGHTY; GTRVHFGHTYS; TRVHFGHTYSI; RVHFGHTYSID; VHFGHTYSIDD; HFGHTYSIDDA; FGHTYSIDDAD; GHTYSIDDADS; HTYSIDDADSI; TYSIDDADSIE; YSIDDADSIEE; SIDDADSIEEV; IDDADSIEEVT; DDADSIEEVTQ; DADSIEEVTQR; ADSIEEVTQRM; DSIEEVTQRMD; SIEEVTQRMDL; IEEVTQRMDLR; EEVTQRMDLRN; EVTQRMDLRNQ; VTQRMDLRNQQ; TQRMDLRNQQS; QRMDLRNQQSV; RMDLRNQQSVH; MDLRNQQSVHS; DLRNQQSVHSG; LRNQQSVHSGE; RNQQSVHSGEF; NQQSVHSGEFI; QQSVHSGEFIE; QSVHSGEFIEK; SVHSGEFIEKT; VHSGEFIEKTI; HSGEFIEKTIA; SGEFIEKTIAP; GEFIEKTIAPG; EFIEKTIAPGG; FIEKTIAPGGA; IEKTIAPGGAN; EKTIAPGGANQ; KTIAPGGANQR; TIAPGGANQRT; IAPGGANQRTA; APGGANQRTAP; PGGANQRTAPQ; GGANQRTAPQW; GANQRTAPQWM; ANQRTAPQWML; NQRTAPQWMLP; QRTAPQWMLPL; RTAPQWMLPLL; TAPQWMLPLLL; APQWMLPLLLG; PQWMLPLLLGL; QWMLPLLLGLY; WMLPLLLGLYG; MLPLLLGLYGT; LPLLLGLYGTV; PLLLGLYGTVT; LLLGLYGTVTP; LLGLYGTVTPA; LGLYGTVTPAL; GLYGTVTPALE; LYGTVTPALEA; YGTVTPALEAY; GTVTPALEAYE; TVTPALEAYED; VTPALEAYEDG; TPALEAYEDGP; PALEAYEDGPN; ALEAYEDGPNQ; LEAYEDGPNQK; EAYEDGPNQKK; AYEDGPNQKKR; YEDGPNQKKRR; EDGPNQKKRRV; DGPNQKKRRVS; GPNQKKRRVSR; PNQKKRRVSRG; NQKKRRVSRGS; QKKRRVSRGSS; KKRRVSRGSSQ; KRRVSRGSSQK; RRVSRGSSQKA; RVSRGSSQKAK; VSRGSSQKAKG; SRGSSQKAKGT; RGSSQKAKGTR; GSSQKAKGTRA; SSQKAKGTRAS; SQKAKGTRASA; QKAKGTRASAK; KAKGTRASAKT; AKGTRASAKTT; KGTRASAKTTN; GTRASAKTTNK; TRASAKTTNKR; RASAKTTNKRR; ASAKTTNKRRS; SAKTTNKRRSR; AKTTNKRRSRS; KTTNKRRSRSS; TTNKRRSRSSR; TNKRRSRSSRS; NWGRCYYRGRM; WGRCYYRGRML; GRCYYRGRMLP; RCYYRGRMLPK; CYYRGRMLPKP; YYRGRMLPKPR; YRGRMLPKPRN; RGRMLPKPRNG; GRMLPKPRNGG; RMLPKPRNGGS; MLPKPRNGGSR; PREKNASLLQH; REKNASLLQHS; EKNASLLQHSK; KNASLLQHSKN; NASLLQHSKNS; ASLLQHSKNSP; SLLQHSKNSPP; LLQHSKNSPPQ; LQHSKNSPPQF; QHSKNSPPQFK; GPNLWKSTDVG; PNLWKSTDVGG; NLWKSTDVGGC; LWKSTDVGGCN; WKSTDVGGCNC; KSTDVGGCNCT; STDVGGCNCTN; TDVGGCNCTNR; DVGGCNCTNRG; VGGCNCTNRGY; GGCNCTNRGYW; GCNCTNRGYWN; CNCTNRGYWNN; FPLLCCRWRTL; PLLCCRWRTLG; LLCCRWRTLGN; LCCRWRTLGNA; CCRWRTLGNAG; CRWRTLGNAGS; RWRTLGNAGSA; WRTLGNAGSAN; RTLGNAGSANE; TLGNAGSANEL; LGNAGSANELQ; GNAGSANELQV; NAGSANELQVK; AGSANELQVKV; GSANELQVKVP; KPNSPVPGNEY; GLFGQKQCLSS; VFWDFHRRGKC; FWDFHRRGKCS; WDFHRRGKCSP; DFHRRGKCSPS; FHRRGKCSPST; HRRGKCSPSTS; RRGKCSPSTSC; RGKCSPSTSCD; GKCSPSTSCDQ; KCSPSTSCDQH; CSPSTSCDQHS; SPSTSCDQHSY; PSTSCDQHSYH; STSCDQHSYHS; TSCDQHSYHSV; SCDQHSYHSVA; CDQHSYHSVAR; QLWNTTVERPC; LWNTTVERPCK; WNTTVERPCKI; NTTVERPCKIF; DPPEKKICKES; PPEKKICKESL; PEKKICKESLP; EKKICKESLPN; KKICKESLPNF; KICKESLPNFL; ICKESLPNFLF; CKESLPNFLFA; KESLPNFLFAK; PYKQENPESGW; YKQENPESGWA; KQENPESGWAA; QENPESGWAAY; ENPESGWAAYV; NPESGWAAYVW; PESGWAAYVWY; ESGWAAYVWYG; SGWAAYVWYGI; GWAAYVWYGIP; WAAYVWYGIPG; AAYVWYGIPGR; AYVWYGIPGRR; YVWYGIPGRRG; WHRKTSRGPRY; HRKTSRGPRYD; RKTSRGPRYDK; KTSRGPRYDKI; TSRGPRYDKIY; QTGTIANQNAL; TGTIANQNALN; GTIANQNALNR; TIANQNALNRC; IANQNALNRCF; ANQNALNRCFY; NQNALNRCFYC; QNALNRCFYCT; NALNRCFYCTY; ALNRCFYCTYT; LNRCFYCTYTF; NRCFYCTYTFN; RCFYCTYTFNK; CFYCTYTFNKC; FYCTYTFNKCC; YCTYTFNKCCF; CTYTFNKCCFC; TYTFNKCCFCI; YTFNKCCFCIS; TFNKCCFCISH; FNKCCFCISHF; NTESLYTNATL; TESLYTNATLD; ESLYTNATLDY; SLYTNATLDYG; LYTNATLDYGG; YTNATLDYGGL; TNATLDYGGLT; NATLDYGGLTF; ATLDYGGLTFG; TLDYGGLTFGN; LDYGGLTFGNL; DYGGLTFGNLQ; YGGLTFGNLQQ; GGLTFGNLQQG; GLTFGNLQQGL; LTFGNLQQGLK; TFGNLQQGLKY; FGNLQQGLKYL; GNLQQGLKYLR; NLQQGLKYLRL; LQQGLKYLRLG; QQGLKYLRLGK; QGLKYLRLGKS; GLKYLRLGKSI; LKYLRLGKSIV; KYLRLGKSIVI; YLRLGKSIVIG; LRLGKSIVIGI; RLGKSIVIGIQ; LGKSIVIGIQC; GKSIVIGIQCL; KSIVIGIQCLI; SIVIGIQCLIH; IVIGIQCLIHV; VIGIQCLIHVQ; IGIQCLIHVQS; GIQCLIHVQSL; IQCLIHVQSLQ; QCLIHVQSLQF; CLIHVQSLQFL; LIHVQSLQFLN; IHVQSLQFLNP; HVQSLQFLNPL; VQSLQFLNPLL; QSLQFLNPLLL; YQEYISPCIYY; QEYISPCIYYI; EYISPCIYYIS; YISPCIYYISS; ISPCIYYISSL; SPCIYYISSLK; PCIYYISSLKK; CIYYISSLKKY; IYYISSLKKYT; YYISSLKKYTY; YISSLKKYTYL; ISSLKKYTYLS; SSLKKYTYLSQ; SLKKYTYLSQN; LKKYTYLSQNP; KKYTYLSQNPA; KYTYLSQNPAF; YTYLSQNPAFP; TYLSQNPAFPS; YLSQNPAFPSI; LSQNPAFPSIQ; SQNPAFPSIQQ; QNPAFPSIQQF; IVYQLQNQLQA; TKLAVATRSFH; KLAVATRSFHF; LAVATRSFHFV; AVATRSFHFVK; VATRSFHFVKF; ATRSFHFVKFF; TRSFHFVKFFF; RSFHFVKFFFQ; SFHFVKFFFQV; FHFVKFFFQVR; HFVKFFFQVRT; FVKFFFQVRTL; VKFFFQVRTLS; KFFFQVRTLSF; FFFQVRTLSFV; FFQVRTLSFVR; FQVRTLSFVRI; QVRTLSFVRIF; VRTLSFVRIFL; RTLSFVRIFLN; TLSFVRIFLNI; LSFVRIFLNIF; SFVRIFLNIFW; FVRIFLNIFWA; PSLVEIFGFFC; SLVEIFGFFCL; LVEIFGFFCLN; VEIFGFFCLNV; EIFGFFCLNVS; IFGFFCLNVSF; FGFFCLNVSFL; GFFCLNVSFLN; FFCLNVSFLNL; FCLNVSFLNLP; HFHLNNLSNCL; FHLNNLSNCLN; HLNNLSNCLNC; LNNLSNCLNCL; NNLSNCLNCLF; NLSNCLNCLFH; LSNCLNCLFHV; SNCLNCLFHVL; NCLNCLFHVLK; CLNCLFHVLKA; LNCLFHVLKAN; NCLFHVLKANP; CLFHVLKANPL; LFHVLKANPLI; FHVLKANPLIQ; HVLKANPLIQL; VLKANPLIQLL; LKANPLIQLLS; KANPLIQLLSL; ANPLIQLLSLL; NPLIQLLSLLH; PLIQLLSLLHL; LIQLLSLLHLQ; IQLLSLLHLQK; QLLSLLHLQKQ; LLSLLHLQKQP; LSLLHLQKQPC; SLLHLQKQPCT; LLHLQKQPCTD; LHLQKQPCTDL; LHLAQRLAFPW; HLAQRLAFPWV; LAQRLAFPWVG; AQRLAFPWVGL; QRLAFPWVGLH; RLAFPWVGLHL; LAFPWVGLHLR; AFPWVGLHLRL; FPWVGLHLRLY; PWVGLHLRLYH; WVGLHLRLYHH; VGLHLRLYHHT; GLHLRLYHHTN; LHLRLYHHTNL; HLRLYHHTNLI; LRLYHHTNLIT; RLYHHTNLITL; LYHHTNLITLQ; YHHTNLITLQL; HHTNLITLQLV; HTNLITLQLVL; TNLITLQLVLF; NLITLQLVLFF; LITLQLVLFFH; ITLQLVLFFHY; TLQLVLFFHYQ; LQLVLFFHYQW; QLVLFFHYQWD; LVLFFHYQWDL; KQYSAKNQILQ; QYSAKNQILQN; YSAKNQILQNP; SAKNQILQNPF; VANSAAKQHLP; ANSAAKQHLPY; NSAAKQHLPYI; SAAKQHLPYIV; AAKQHLPYIVL; AKQHLPYIVLV; KQHLPYIVLVQ; QHLPYIVLVQH; HLPYIVLVQHF; LPYIVLVQHFH; PYIVLVQHFHE; YIVLVQHFHEL; IVLVQHFHELQ; VLVQHFHELQI; LVQHFHELQIL; VQHFHELQILN; QHFHELQILNP; HFHELQILNPF; FHELQILNPFY; HELQILNPFYL; ELQILNPFYLI; LQILNPFYLIY; QILNPFYLIYD; IFLLAFLPWSY; FLLAFLPWSYE; LLAFLPWSYEG; LAFLPWSYEGY; AFLPWSYEGYL; FLPWSYEGYLL; LPWSYEGYLLF; PWSYEGYLLFF; LKLYLLLADKY; KLYLLLADKYF; LYLLLADKYFF; YLLLADKYFFD; LLLADKYFFDF; LLADKYFFDFY; LADKYFFDFYF; ADKYFFDFYFL; DKYFFDFYFLQ; KYFFDFYFLQK; SDKAGLFSDTF; DKAGLFSDTFY; KAGLFSDTFYT; AGLFSDTFYTP; GLFSDTFYTPL; LFSDTFYTPLH; FSDTFYTPLHC; SDTFYTPLHCI; DTFYTPLHCIE; TFYTPLHCIEI; FYTPLHCIEIL; YTPLHCIEILN; TPLHCIEILNT; PLHCIEILNTY; LHCIEILNTYL; HCIEILNTYLI; CIEILNTYLII; IEILNTYLIIK; EILNTYLIIKT; ILNTYLIIKTH; LNTYLIIKTHP; NTYLIIKTHPH; TYLIIKTHPHT; YLIIKTHPHTL; LIIKTHPHTLS; IIKTHPHTLSL; IKTHPHTLSLL; KTHPHTLSLLH; THPHTLSLLHT; HPHTLSLLHTQ; LISKTPALFLQ; ISKTPALFLQA; SKTPALFLQAL; KTPALFLQALL; TPALFLQALLG; NHAPLSPLECF; HAPLSPLECFL; APLSPLECFLL; LQKLYVYVELK; QKLYVYVELKR; KLYVYVELKRI; YTQQSRQGFYY; GLLPFFFFWVV; LLPFFFFWVVL; LPFFFFWVVLS; PFFFFWVVLSV; FFFFWVVLSVE; FFFWVVLSVEN; FFWVVLSVENL; FWVVLSVENLL; WVVLSVENLLL; VVLSVENLLLL; VLSVENLLLLL; LSVENLLLLLH; SVENLLLLLHH; VENLLLLLHHW; ENLLLLLHHWQ; NLLLLLHHWQT; LLLLLHHWQTY; LLLLHHWQTYL; LLLHHWQTYLH; LLHHWQTYLHG; LHHWQTYLHGK; HHWQTYLHGKI; HWQTYLHGKIN; WQTYLHGKINL; QTYLHGKINLH; TYLHGKINLHP; YLHGKINLHPI; LHGKINLHPIF; HGKINLHPIFH; RNSTRTPTLLF; NSTRTPTLLFH; STRTPTLLFHR; TRTPTLLFHRL; RTPTLLFHRLA; TPTLLFHRLAP; PTLLFHRLAPI; TLLFHRLAPIK; LLFHRLAPIKK; LFHRLAPIKKI; FHRLAPIKKII; HRLAPIKKIIT; GLLIFYYLSKY; LLIFYYLSKYK; LIFYYLSKYKL; IFYYLSKYKLV; FYYLSKYKLVT; YYLSKYKLVTL; YLSKYKLVTLK; LSKYKLVTLKL; ISEGSFSNYLD; SEGSFSNYLDP; EGSFSNYLDPP; GSFSNYLDPPL; SFSNYLDPPLQ; FSNYLDPPLQS; SNYLDPPLQSF; NYLDPPLQSFF; YLDPPLQSFFS; AKPLCEAVNAV; KPLCEAVNAVA; PLCEAVNAVAI; LCEAVNAVAIY; CEAVNAVAIYP; EAVNAVAIYPN; AVNAVAIYPNQ; VNAVAIYPNQG; NAVAIYPNQGL; AVAIYPNQGLF; VAIYPNQGLFS; HARAVHRRLFG; ARAVHRRLFGT; RAVHRRLFGTN; AVHRRLFGTNR; VHRRLFGTNRP; HRRLFGTNRPF; RRLFGTNRPFL; RLFGTNRPFLA; LFGTNRPFLAV; FGTNRPFLAVQ; GTNRPFLAVQG; TNRPFLAVQGI; NRPFLAVQGIW; RPFLAVQGIWA; PFLAVQGIWAK; FLAVQGIWAKR; LAVQGIWAKRK; AVQGIWAKRKI; VQGIWAKRKIS; QGIWAKRKIST; GIWAKRKISTN; IWAKRKISTNL; ATPGSKIRLMS; TPGSKIRLMSY; PGSKIRLMSYL; GSKIRLMSYLY; SKIRLMSYLYI; KIRLMSYLYIL; IRLMSYLYILL; RLMSYLYILLH; LMSYLYILLHF; MSYLYILLHFF; SYLYILLHFFI; YLYILLHFFIQ; LYILLHFFIQS; YILLHFFIQSI; ILLHFFIQSIH; LLHFFIQSIHS; LHFFIQSIHSL; HFFIQSIHSLH; FFIQSIHSLHF; FIQSIHSLHFI; IQSIHSLHFIL; QSIHSLHFILV; SIHSLHFILVA; IHSLHFILVAP; HSLHFILVAPF; SLHFILVAPFV; LHFILVAPFVR; HFILVAPFVRV; FILVAPFVRVK; ILVAPFVRVKF; LVAPFVRVKFL; VAPFVRVKFLT; APFVRVKFLTL; PFVRVKFLTLP; GKISPGSSFKA; KVHELHGFFPV; VHELHGFFPVK; HELHGFFPVKN; ELHGFFPVKNF; LHGFFPVKNFI; HGFFPVKNFIH BK virus complementary reading frame 1 8 mers: MDKVLNRE; DKVLNREE; KVLNREES; VLNREESM; LNREESME; NREESMEL; REESMELM; EESMELMD; ESMELMDL; SMELMDLL; MELMDLLG; ELMDLLGL; LMDLLGLE; MDLLGLER; DLLGLERA; LLGLERAA; LGLERAAW; GLERAAWG; LERAAWGN; ERAAWGNL; RAAWGNLP; AAWGNLPL; AWGNLPLM; WGNLPLMR; GNLPLMRK; NLPLMRKA; LPLMRKAY; PLMRKAYL; LMRKAYLR; MRKAYLRK; RKAYLRKC; KAYLRKCK; AYLRKCKE; YLRKCKEF; LRKCKEFH; RKCKEFHP; KCKEFHPD; CKEFHPDK; KEFHPDKG; EFHPDKGG; FHPDKGGD; HPDKGGDE; PDKGGDED; DKGGDEDK; KGGDEDKM; GGDEDKMK; GDEDKMKR; DEDKMKRM; EDKMKRMN; DKMKRMNT; KMKRMNTL; MKRMNTLY; KRMNTLYK; RMNTLYKK; MNTLYKKM; NTLYKKME; TLYKKMEQ; LYKKMEQD; YKKMEQDV; KKMEQDVK; KMEQDVKV; MEQDVKVA; EQDVKVAH; QDVKVAHQ; DVKVAHQP; VKVAHQPD; KVAHQPDF; VAHQPDFG; AHQPDFGT; HQPDFGTW; QPDFGTWS; PDFGTWSS; DFGTWSSS; FGTWSSSE; GTWSSSEV; TWSSSEVC; WSSSEVCA; SSSEVCAD; SSEVCADF; SEVCADFP; EVCADFPL; VCADFPLC; CADFPLCP; ADFPLCPD; DFPLCPDT; FPLCPDTL; PLCPDTLY; LCPDTLYC; CPDTLYCK; PDTLYCKE; DTLYCKEW; TLYCKEWP; LYCKEWPI; YCKEWPIC; CKEWPICS; KEWPICSK; EWPICSKK; WPICSKKP; PICSKKPS; ICSKKPSV; CSKKPSVH; SKKPSVHC; KKPSVHCP; KPSVHCPC; PSVHCPCM; SVHCPCML; VHCPCMLC; HCPCMLCQ; CPCMLCQL; PCMLCQLR; CMLCQLRL; MLCQLRLR; LCQLRLRH; CQLRLRHL; QLRLRHLN; LRLRHLNR; RLRHLNRK; LRHLNRKF; RHLNRKFL; HLNRKFLR; LNRKFLRK; NRKFLRKE; RKFLRKEP; KFLRKEPL; FLRKEPLV; LRKEPLVW; RKEPLVWI; KEPLVWID; EPLVWIDC; PLVWIDCY; LVWIDCYC; VWIDCYCI; WIDCYCID; IDCYCIDC; DCYCIDCF; CYCIDCFT; YCIDCFTQ; CIDCFTQW; IDCFTQWF; DCFTQWFG; CFTQWFGL; FTQWFGLD; TQWFGLDL; QWFGLDLT; WFGLDLTE; FGLDLTEE; GLDLTEET; LDLTEETL; DLTEETLQ; LTEETLQW; TEETLQWW; EETLQWWV; ETLQWWVQ; TLQWWVQI; LQWWVQII; QWWVQIIG; WWVQIIGE; WVQIIGET; VQIIGETP; QIIGETPF; IIGETPFR; IGETPFRD; GETPFRDL; ETPFRDLK; TPFRDLKL; KALSNYFF; ALSNYFFY; LSNYFFYR; SNYFFYRC; NYFFYRCQ; YFFYRCQP; FFYRCQPM; FYRCQPME; YRCQPMEQ; RCQPMEQK; CQPMEQKS; QPMEQKSG; PMEQKSGS; MEQKSGSP; EQKSGSPG; QKSGSPGG; KSGSPGGV; SGSPGGVP; GSPGGVPL; SPGGVPLM; PGGVPLMK; GGVPLMKN; GVPLMKNG; VPLMKNGM; PLMKNGMK; LMKNGMKI; MKNGMKIY; KNGMKIYF; NGMKIYFA; GMKIYFAM; MKIYFAMK; KIYFAMKI; IYFAMKIC; YFAMKICL; FAMKICLP; AMKICLPV; MKICLPVM; KICLPVMK; ICLPVMKK; CLPVMKKQ; LPVMKKQQ; PVMKKQQQ; VMKKQQQI; MKKQQQIL; KKQQQILN; KQQQILNT; QQQILNTQ; QQILNTQH; QILNTQHH; ILNTQHHP; LNTQHHPK; NTQHHPKK; TQHHPKKK; QHHPKKKE; HHPKKKER; KTLKTFPL; TLKTFPLI; LKTFPLIY; KTFPLIYT; TFPLIYTS; FPLIYTSF; PLIYTSFL; LIYTSFLV; IYTSFLVK; YTSFLVKL; TSFLVKLY; SFLVKLYL; FLVKLYLV; LVKLYLVI; VKLYLVIE; KLYLVIEP; LYLVIEPL; YLVIEPLP; LVIEPLPA; VIEPLPAL; IEPLPALL; EPLPALLC; PLPALLCI; LPALLCIL; PALLCILL; ALLCILLK; LLCILLKK; LCILLKKK; CILLKKKL; ILLKKKLK; LLKKKLKF; LKKKLKFC; KKKLKFCI; KKLKFCIK; KLKFCIKN; LKFCIKNL; KFCIKNLW; FCIKNLWK; CIKNLWKN; IKNLWKNI; KNLWKNIL; LLLVDTCV; LLVDTCVL; LVDTCVLG; VDTCVLGI; DTCVLGII; TCVLGIIL; CVLGIILY; VLGIILYS; LGIILYSF; LHIDIEFL; HIDIEFLQ; IDIEFLQL; DIEFLQLI; IEFLQLII; EFLQLIIS; FLQLIISV; LQLIISVK; QLIISVKS; LIISVKSC; IISVKSCV; ISVKSCVP; SVKSCVPL; VKSCVPLV; KSCVPLVF; FVRVLIRN; VRVLIRNT; RVLIRNTY; VLIRNTYY; LIRNTYYI; IRNTYYIV; RNTYYIVP; RSMILAQK; SMILAQKS; MILAQKSL; ILAQKSLK; LAQKSLKK; AQKSLKKQ; QKSLKKQS; KSLKKQSR; SLKKQSRC; LKKQSRCL; KKQSRCLG; KQSRCLGN; RQSVRMCF; QSVRMCFY; SVRMCFYY; RSVKSVRK; SVKSVRKK; VKSVRKKT; KSVRKKTS; SVRKKTSL; VRKKTSLI; RKKTSLIT; KKTSLITL; KTSLITLS; TSLITLSI; SLITLSIM; LITLSIMK; ITLSIMKS; TLSIMKST; LSIMKSTL; SIMKSTLQ; IMKSTLQM; MKSTLQML; KSTLQMLL; STLQMLLF; TLQMLLFL; LQMLLFLQ; QMLLFLQK; MLLFLQKV; LLFLQKVK; LFLQKVKI; FLQKVKIK; LQKVKIKK; QKVKIKKV; KVKIKKVF; VKIKKVFV; KIKKVFVS; IKKVFVSK; KKVFVSKQ; YLELMEML; LELMEMLY; NNIWQVLL; NIWQVLLG; IWQVLLGC; WQVLLGCT; QVLLGCTV; VLLGCTVC; LLGCTVCY; LGCTVCYL; GCTVCYLK; CTVCYLKW; TVCYLKWI; VCYLKWIL; YLIFCTVL; LIFCTVLF; IFCTVLFS; FCTVLFSM; CTVLFSMY; TVLFSMYL; VLFSMYLK; LFSMYLKE; FSMYLKED; SMYLKEDT; MYLKEDTG; YLKEDTGY; LKEDTGYL; KEDTGYLK; EDTGYLKV; DTGYLKVP; TGYLKVPL; GYLKVPLI; YLKVPLIV; LKVPLIVE; KVPLIVEK; VPLIVEKQ; PLIVEKQH; ISTWLFLK; STWLFLKM; KGQELNQR; GQELNQRI; QELNQRIC; ELNQRICL; LNQRICLQ; NQRICLQD; QRICLQDM; RICLQDME; TKEPKYFH; KEPKYFHQ; EPKYFHQA; PKYFHQAW; KYFHQAWL; YFHQAWLQ; MSILSLKP; SILSLKPC; ILSLKPCK; LSLKPCKL; SLKPCKLD; LKPCKLDL; ENPYKTQS; NPYKTQSS; PYKTQSSY; YKTQSSYL; KTQSSYLK; TQSSYLKK; QSSYLKKE; SSYLKKEF; SYLKKEFY; YLKKEFYK; LKKEFYKV; KKEFYKVE; LILQLIYN; ILQLIYNL; LQLIYNLE; QLIYNLEL; LIYNLELL; IYNLELLN; YNLELLNG; NLELLNGR; LELLNGRK; ELLNGRKG; LLNGRKGW; LNGRKGWI; NGRKGWIL; GRKGWILR; NIIYAWGN; IIYAWGNV; IYAWGNVF; YAWGNVFL; AWGNVFLI; WGNVFLIL; GNVFLILQ; NVFLILQE; VFLILQEK; FLILQEKR; LILQEKRI; ILQEKRIQ; LQEKRIQK; QEKRIQKL; EKRIQKLK; KRIQKLKT; RIQKLKTL; IQKLKTLD; QKLKTLDM; KLKTLDMD; LKTLDMDQ; KTLDMDQA; TLDMDQAL; LDMDQALN; DMDQALNP; MDQALNPN; DQALNPNH; QALNPNHN; ALNPNHNA; LNPNHNAL; NPNHNALP; PNHNALPK; NHNALPKS; HNALPKSQ; NALPKSQI; ALPKSQIL; LPKSQILQ; PKSQILQP; KSQILQPL; SQILQPLL; QILQPLLK; ILQPLLKI; LQPLLKIP; QPLLKIPK; PLLKIPKG; LLKIPKGQ; LKIPKGQT; KIPKGQTP; IPKGQTPI; PKGQTPIV; KGQTPIVK; GQTPIVKS; QTPIVKSC; TPIVKSCI; PIVKSCIC; IVKSCICV; VKSCICVK; KSCICVKA; SCICVKAF; CICVKAFS; ICVKAFSV; CVKAFSVL; VKAFSVLK; KAFSVLKG; AFSVLKGL; FSVLKGLK; SVLKGLKH; VLKGLKHH; LKGLKHHP; KGLKHHPQ; GLKHHPQN; LKHHPQNN; KHHPQNNT; HHPQNNTS; HPQNNTSL; PQNNTSLK; QNNTSLKV; NNTSLKVA; NTSLKVAY; TSLKVAYT; SLKVAYTK; LKVAYTKA; KVAYTKAA; VAYTKAAF; AYTKAAFI; YTKAAFIK; TKAAFIKC; KAAFIKCI; AAFIKCIC; AFIKCICT; FIKCICTI; IKCICTIK; KCICTIKA; CICTIKAP; ICTIKAPV; SILVCNCP; ILVCNCPC; LVCNCPCL; VCNCPCLS; CNCPCLSI; NCPCLSIY; CPCLSIYL; PCLSIYLI; CLSIYLII; LSIYLIIS; SIYLIISG; IYLIISGS; YLIISGSP; LIISGSPG; IISGSPGS; ISGSPGSL; SGSPGSLS; GSPGSLSV; SPGSLSVP; PGSLSVPS; GSLSVPSN; SLSVPSNT; LSVPSNTL; SVPSNTLT; VPSNTLTS; PSNTLTSS; SNTLTSST; NTLTSSTW; TLTSSTWD; LTSSTWDS; TSSTWDSI; SSTWDSIP; STWDSIPY; TWDSIPYI; WDSIPYIG; DSIPYIGC; SIPYIGCP; IPYIGCPS; PYIGCPST; YIGCPSTL; IGCPSTLW; GCPSTLWV; CPSTLWVL; PSTLWVLL; STLWVLLF; TLWVLLFI; LWVLLFIR; WVLLFIRS; VLLFIRSL; LLFIRSLS; LFIRSLSK; FIRSLSKK; IRSLSKKE; RSLSKKEI; SLSKKEIG; GFFTDLFL; FFTDLFLR; FTDLFLRR; TDLFLRRI; DLFLRRIL; LFLRRILK; FLRRILKY; LRRILKYL; RRILKYLA; RILKYLAR; ILKYLARP; LKYLARPL; KYLARPLH; YLARPLHC; LARPLHCC; ARPLHCCV; RPLHCCVP; PLHCCVPE; LHCCVPEL; HCCVPELL; CCVPELLV; CVPELLVN; VPELLVNR; PELLVNRP; ELLVNRPQ; LLVNRPQI; LVNRPQIS; VNRPQISA; NRPQISAA; RPQISAAE; PQISAAET; QISAAETY; ISAAETYR; SAAETYRL; AAETYRLS; AETYRLSA; ETYRLSAL; TYRLSALQ; YRLSALQR; RLSALQRG; LSALQRGP; SALQRGPT; ALQRGPTP; LQRGPTPC; QRGPTPCS; RGPTPCSS; GPTPCSSS; PTPCSSSN; TPCSSSNT; PCSSSNTV; CSSSNTVV; SSSNTVVA; SSNTVVAV; SNTVVAVL; NTVVAVLV; TVVAVLVT; STGGTFSP; TGGTFSPP; GGTFSPPV; GTFSPPVK; TFSPPVKV; FSPPVKVP; SPPVKVPK; PPVKVPKY; PVKVPKYL; VKVPKYLA; KVPKYLAF; VPKYLAFS; PKYLAFSF; KYLAFSFL; YLAFSFLL; LAFSFLLG; AFSFLLGS; FSFLLGSG; SFLLGSGT; FLLGSGTQ; LLGSGTQH; LGSGTQHS; GSGTQHST; SGTQHSTG; ALWSVFIT; LWSVFITW; WSVFITWD; SVFITWDW; VFITWDWA; FITWDWAV; ITWDWAVG; TWDWAVGF; WDWAVGFL; DWAVGFLG; WAVGFLGV; AVGFLGVI; VGFLGVIV; GFLGVIVP; FLGVIVPS; LGVIVPSG; GVIVPSGY; VIVPSGYF; IVPSGYFD; VPSGYFDL; FISTPCIS; ISTPCISK; STPCISKG; TPCISKGS; PCISKGSP; CISKGSPP; ISKGSPPT; SKGSPPTA; KGSPPTAK; GSPPTAKK; SPPTAKKW; PPTAKKWK; PTAKKWKL; TAKKWKLL; AKKWKLLP; IGFPPPCS; GFPPPCSC; FPPPCSCT; PPPCSCTF; PPCSCTFC; PCSCTFCD; CSCTFCDP; SCTFCDPA; RLSMLVIP; LSMLVIPI; SMLVIPIT; MLVIPITS; LVIPITSV; VIPITSVC; IPITSVCT; PITSVCTV; ITSVCTVT; TSVCTVTA; SVCTVTAS; VCTVTASH; CTVTASHI; TVTASHIS; VTASHISR; TASHISRF; ASHISRFP; SHISRFPQ; HISRFPQV; ISRFPQVR; SRFPQVRS; RFPQVRSS; FPQVRSSF; PQVRSSFK; QVRSSFKL; VRSSFKLG; RSSFKLGR; SSFKLGRG; SFKLGRGI; FKLGRGIL; KLGRGILA; LGRGILAV; GRGILAVL; QGSIFLSG; GSIFLSGL; SIFLSGLS; IFLSGLSL; FLSGLSLL; LSGLSLLK; SGLSLLKS; GLSLLKSF; LSLLKSFS; SLLKSFSA; LLKSFSAL; LKSFSALS; KSFSALSF; SFSALSFR; FSALSFRL; SALSFRLK; ALSFRLKP; LSFRLKPL; SFRLKPLR; FRLKPLRF; RLKPLRFS; LKPLRFSS; KPLRFSSG; PLRFSSGS; LRFSSGSP; RFSSGSPI; FSSGSPIS; SSGSPISG; SGSPISGF; GSPISGFR; SPISGFRK; PISGFRKH; ISGFRKHS; SGFRKHST; GFRKHSTS; FRKHSTSV; RKHSTSVI; KHSTSVIA; HSTSVIAS; STSVIAST; TSVIASTP; SVIASTPV; VIASTPVL; IASTPVLT; ASTPVLTS; STPVLTSR; TPVLTSRT; PVLTSRTS; VLTSRTST; LTSRTSTP; TSRTSTPP; SRTSTPPF; RTSTPPFI; TSTPPFIS; STPPFISS; TPPFISSF; PPFISSFG; PFISSFGT; FISSFGTC; ISSFGTCT; SSFGTCTG; SFGTCTGS; FGTCTGSF; GTCTGSFG; TCTGSFGF; CTGSFGFL; TGSFGFLG; GSFGFLGA; SFGFLGAA; FGFLGAAP; GFLGAAPG; FLGAAPGH; LGAAPGHS; GAAPGHSP; AAPGHSPF; APGHSPFL; PGHSPFLL; GHSPFLLV; HSPFLLVG; SPFLLVGA; PFLLVGAI; FLLVGAIF; LLVGAIFI; LVGAIFIC; VGAIFICF; GAIFICFK; AIFICFKS; IFICFKSR; FICFKSRC; ICFKSRCY; CFKSRCYS; FKSRCYSP; KSRCYSPV; SRCYSPVQ; RCYSPVQA; RQHPLRSS; QHPLRSSS; HPLRSSSL; PLRSSSLI; LRSSSLIS; RSSSLIST; SSSLISTS; SSLISTSW; SLISTSWG; LISTSWGN; ISTSWGNS; STSWGNSF; TSWGNSFF; SWGNSFFY; WGNSFFYK; GNSFFYKL; NSFFYKLS; VHSLCNFF; HSLCNFFY; SLCNFFYT; LCNFFYTV; CNFFYTVS; NFFYTVSI; FFYTVSII; FYTVSIIY; YTVSIIYT; TVSIIYTI; VSIIYTIS; SIIYTISM; IIYTISMA; IYTISMAK; YTISMAKM; TISMAKMY; ISMAKMYT; SMAKMYTG; MAKMYTGT; AKMYTGTF; KMYTGTFP; MYTGTFPF; YTGTFPFS; TGTFPFSY; GTFPFSYL; TFPFSYLS; FPFSYLSN; PFSYLSNH; GPNRGKIR; PNRGKIRI; NRGKIRII; RGKIRIIL; GKIRIILL; KIRIILLN; IRIILLNI; RIILLNII; IILLNIII; ILLNIIIK; LLNIIIKV; LNIIIKVY; NIIIKVYR; IIIKVYRG; IIKVYRGI; IKVYRGIY; KVYRGIYN; VYRGIYNC; YRGIYNCP; RGIYNCPG; GIYNCPGS; IYNCPGSF; YNCPGSFL; NCPGSFLQ; CPGSFLQK; PGSFLQKS; GSFLQKSS; SFLQKSSQ; FLQKSSQG; LQKSSQGV; QKSSQGVS; KSSQGVSK; SSQGVSKK; SQGVSKKS; QGVSKKSF; GVSKKSFC; VSKKSFCS; SKKSFCSS; KKSFCSSL; KSFCSSLQ; SFCSSLQF; FCSSLQFL; GYRRYIIP; YRRYIIPN; RRYIIPNN; RYIIPNNM; YIIPNNMP; IIPNNMPQ; IPNNMPQS; PNNMPQSL; NNMPQSLG; NMPQSLGN; MPQSLGNS; PQSLGNSS; QSLGNSSK; SLGNSSKQ; LGNSSKQR; GNSSKQRR; NSSKQRRT; SSKQRRTP; SKQRRTPM; KQRRTPMP; QRRTPMPR; RRTPMPRI; RTPMPRIK; TPMPRIKV; PMPRIKVL; MPRIKVLN; PRIKVLNI; RIKVLNII; IKVLNIIN; KVLNIINK; VLNIINKS; LNIINKSI; NIINKSIY; IINKSIYT; INKSIYTR; NKSIYTRK; KSIYTRKQ; SIYTRKQN; IYTRKQNI; YTRKQNII; TRKQNIIV; RKQNIIVL; KQNIIVLI; QNIIVLIW; NIIVLIWV; IIVLIWVK; IVLIWVKQ; VLIWVKQF; LIWVKQFQ; IWVKQFQS; WVKQFQSH; VKQFQSHA; LLIEAYSG; LIEAYSGN; IEAYSGNF; EAYSGNFV; AYSGNFVI; YSGNFVIP; SGNFVIPI; GNFVIPII; NFVIPIIK; FVIPIIKE; VIPIIKEL; IPIIKELI; PIIKELIP; IIKELIPY; IKELIPYL; KELIPYLS; GTNTTNSL; TNTTNSLN; SSKPSNSP; SKPSNSPR; KPSNSPRS; PSNSPRST; SNSPRSTS; NSPRSTSN; SPRSTSNY; PRSTSNYS; RSTSNYSI; STSNYSIC; TSNYSICL; SNYSICLR; NYSICLRS; GTCYALYS; TCYALYSS; CYALYSSK; YALYSSKG; ALYSSKGC; LYSSKGCN; YSSKGCNL; SSKGCNLN; SKGCNLNF; KGCNLNFY; GCNLNFYS; CNLNFYSS; NLNFYSSS; LNFYSSSS; NFYSSSSL; FYSSSSLP; YSSSSLPS; SSSSLPSS; SSSLPSSN; SSLPSSNF; SLPSSNFS; LPSSNFSH; KSCGSSSL; SCGSSSLR; CGSSSLRY; GSSSLRYT; SSSLRYTG; SSLRYTGN; SSTHEPGN; STHEPGNT; THEPGNTK; HEPGNTKK; EPGNTKKK; PGNTKKKG; GNTKKKGL; NTKKKGLL; TKKKGLLT; ESFTESFT; SFTESFTA; FTESFTAG; TESFTAGK; ESFTAGKA; SFTAGKAV; FTAGKAVV; TAGKAVVL; AGKAVVLL; GKAVVLLF; KAVVLLFF; AVVLLFFP; VVLLFFPS; VLLFFPST; LLFFPSTL; LFFPSTLS; FFPSTLSS; FPSTLSSP; PSTLSSPL; STLSSPLQ; TLSSPLQN; LSSPLQNS; SSPLQNSS; SPLQNSSK; PLQNSSKS; LQNSSKSS; QNSSKSSK; NSSKSSKI; SSKSSKIK; SKSSKIKI; KSSKIKIK; SSKIKIKI; SKIKIKIL; ALFFVPVQ; LFFVPVQV; FFVPVQVL; FVPVQVLP; VPVQVLPT; PVQVLPTF; VQVLPTFT; QVLPTFTE; VLPTFTEA; LPTFTEAC; PTFTEACR; TFTEACRD; FTEACRDS; TEACRDSW; EACRDSWR; ACRDSWRR; CRDSWRRT; RDSWRRTM; DSWRRTMA; SWRRTMAF; WRRTMAFV; RRTMAFVQ; RTMAFVQF; TMAFVQFN; MAFVQFNW; AFVQFNWG; FVQFNWGQ; VQFNWGQG; QFNWGQGQ; FNWGQGQD; NWGQGQDS; ARKTCLSC; RKTCLSCT; KTCLSCTF; TCLSCTFL; CLSCTFLP; LSCTFLPE; SCTFLPEV; CTFLPEVM; TFLPEVMV; FLPEVMVW; LPEVMVWL; PEVMVWLH; EVMVWLHS; VMVWLHSM; MVWLHSMG; VWLHSMGK; WLHSMGKQ; LHSMGKQL; HSMGKQLL; SMGKQLLP; MGKQLLPV; GKQLLPVS; KQLLPVSH; QLLPVSHA; LLPVSHAL; LPVSHALS; PVSHALSF; VSHALSFL; SHALSFLR; HALSFLRS; ALSFLRSW; LSFLRSWF; SFLRSWFG; FLRSWFGC; LRSWFGCI; RSWFGCIP; SWFGCIPL; GHGLAAFH; HGLAAFHG; AAPPCGLF; APPCGLFF; PPCGLFFY; PCGLFFYN; CGLFFYNI; EAEAASAS; AEAASAST; EAASASTL; AASASTLS; ASASTLSL; SASTLSLK; GLAKLFGE; LAKLFGEI; AKLFGEIP; KLFGEIPI; LFGEIPIL; FGEIPILL; GEIPILLQ; EIPILLQF; IPILLQFL; PILLQFLQ 9 mers: MDKVLNREE; DKVLNREES; KVLNREESM; VLNREESME; LNREESMEL; NREESMELM; REESMELMD; EESMELMDL; ESMELMDLL; SMELMDLLG; MELMDLLGL; ELMDLLGLE; LMDLLGLER; MDLLGLERA; DLLGLERAA; LLGLERAAW; LGLERAAWG; GLERAAWGN; LERAAWGNL; ERAAWGNLP; RAAWGNLPL; AAWGNLPLM; AWGNLPLMR; WGNLPLMRK; GNLPLMRKA; NLPLMRKAY; LPLMRKAYL; PLMRKAYLR; LMRKAYLRK; MRKAYLRKC; RKAYLRKCK; KAYLRKCKE; AYLRKCKEF; YLRKCKEFH; LRKCKEFHP; RKCKEFHPD; KCKEFHPDK; CKEFHPDKG; KEFHPDKGG; EFHPDKGGD; FHPDKGGDE; HPDKGGDED; PDKGGDEDK; DKGGDEDKM; KGGDEDKMK; GGDEDKMKR; GDEDKMKRM; DEDKMKRMN; EDKMKRMNT; DKMKRMNTL; KMKRMNTLY; MKRMNTLYK; KRMNTLYKK; RMNTLYKKM; MNTLYKKME; NTLYKKMEQ; TLYKKMEQD; LYKKMEQDV; YKKMEQDVK; KKMEQDVKV; KMEQDVKVA; MEQDVKVAH; EQDVKVAHQ; QDVKVAHQP; DVKVAHQPD; VKVAHQPDF; KVAHQPDFG; VAHQPDFGT; AHQPDFGTW; HQPDFGTWS; QPDFGTWSS; PDFGTWSSS; DFGTWSSSE; FGTWSSSEV; GTWSSSEVC; TWSSSEVCA; WSSSEVCAD; SSSEVCADF; SSEVCADFP; SEVCADFPL; EVCADFPLC; VCADFPLCP; CADFPLCPD; ADFPLCPDT; DFPLCPDTL; FPLCPDTLY; PLCPDTLYC; LCPDTLYCK; CPDTLYCKE; PDTLYCKEW; DTLYCKEWP; TLYCKEWPI; LYCKEWPIC; YCKEWPICS; CKEWPICSK; KEWPICSKK; EWPICSKKP; WPICSKKPS; PICSKKPSV; ICSKKPSVH; CSKKPSVHC; SKKPSVHCP; KKPSVHCPC; KPSVHCPCM; PSVHCPCML; SVHCPCMLC; VHCPCMLCQ; HCPCMLCQL; CPCMLCQLR; PCMLCQLRL; CMLCQLRLR; MLCQLRLRH; LCQLRLRHL; CQLRLRHLN; QLRLRHLNR; LRLRHLNRK; RLRHLNRKF; LRHLNRKFL; RHLNRKFLR; HLNRKFLRK; LNRKFLRKE; NRKFLRKEP; RKFLRKEPL; KFLRKEPLV; FLRKEPLVW; LRKEPLVWI; RKEPLVWID; KEPLVWIDC; EPLVWIDCY; PLVWIDCYC; LVWIDCYCI; VWIDCYCID; WIDCYCIDC; IDCYCIDCF; DCYCIDCFT; CYCIDCFTQ; YCIDCFTQW; CIDCFTQWF; IDCFTQWFG; DCFTQWFGL; CFTQWFGLD; FTQWFGLDL; TQWFGLDLT; QWFGLDLTE; WFGLDLTEE; FGLDLTEET; GLDLTEETL; LDLTEETLQ; DLTEETLQW; LTEETLQWW; TEETLQWWV; EETLQWWVQ; ETLQWWVQI; TLQWWVQII; LQWWVQIIG; QWWVQIIGE; WWVQIIGET; WVQIIGETP; VQIIGETPF; QIIGETPFR; IIGETPFRD; IGETPFRDL; GETPFRDLK; ETPFRDLKL; KALSNYFFY; ALSNYFFYR; LSNYFFYRC; SNYFFYRCQ; NYFFYRCQP; YFFYRCQPM; FFYRCQPME; FYRCQPMEQ; YRCQPMEQK; RCQPMEQKS; CQPMEQKSG; QPMEQKSGS; PMEQKSGSP; MEQKSGSPG; EQKSGSPGG; QKSGSPGGV; KSGSPGGVP; SGSPGGVPL; GSPGGVPLM; SPGGVPLMK; PGGVPLMKN; GGVPLMKNG; GVPLMKNGM; VPLMKNGMK; PLMKNGMKI; LMKNGMKIY; MKNGMKIYF; KNGMKIYFA; NGMKIYFAM; GMKIYFAMK; MKIYFAMKI; KIYFAMKIC; IYFAMKICL; YFAMKICLP; FAMKICLPV; AMKICLPVM; MKICLPVMK; KICLPVMKK; ICLPVMKKQ; CLPVMKKQQ; LPVMKKQQQ; PVMKKQQQI; VMKKQQQIL; MKKQQQILN; KKQQQILNT; KQQQILNTQ; QQQILNTQH; QQILNTQHH; QILNTQHHP; ILNTQHHPK; LNTQHHPKK; NTQHHPKKK; TQHHPKKKE; QHHPKKKER; KTLKTFPLI; TLKTFPLIY; LKTFPLIYT; KTFPLIYTS; TFPLIYTSF; FPLIYTSFL; PLIYTSFLV; LIYTSFLVK; IYTSFLVKL; YTSFLVKLY; TSFLVKLYL; SFLVKLYLV; FLVKLYLVI; LVKLYLVIE; VKLYLVIEP; KLYLVIEPL; LYLVIEPLP; YLVIEPLPA; LVIEPLPAL; VIEPLPALL; IEPLPALLC; EPLPALLCI; PLPALLCIL; LPALLCILL; PALLCILLK; ALLCILLKK; LLCILLKKK; LCILLKKKL; CILLKKKLK; ILLKKKLKF; LLKKKLKFC; LKKKLKFCI; KKKLKFCIK; KKLKFCIKN; KLKFCIKNL; LKFCIKNLW; KFCIKNLWK; FCIKNLWKN; CIKNLWKNI; IKNLWKNIL; LLLVDTCVL; LLVDTCVLG; LVDTCVLGI; VDTCVLGII; DTCVLGIIL; TCVLGIILY; CVLGIILYS; VLGIILYSF; LHIDIEFLQ; HIDIEFLQL; IDIEFLQLI; DIEFLQLII; IEFLQLIIS; EFLQLIISV; FLQLIISVK; LQLIISVKS; QLIISVKSC; LIISVKSCV; IISVKSCVP; ISVKSCVPL; SVKSCVPLV; VKSCVPLVF; FVRVLIRNT; VRVLIRNTY; RVLIRNTYY; VLIRNTYYI; LIRNTYYIV; IRNTYYIVP; RSMILAQKS; SMILAQKSL; MILAQKSLK; ILAQKSLKK; LAQKSLKKQ; AQKSLKKQS; QKSLKKQSR; KSLKKQSRC; SLKKQSRCL; LKKQSRCLG; KKQSRCLGN; RQSVRMCFY; QSVRMCFYY; RSVKSVRKK; SVKSVRKKT; VKSVRKKTS; KSVRKKTSL; SVRKKTSLI; VRKKTSLIT; RKKTSLITL; KKTSLITLS; KTSLITLSI; TSLITLSIM; SLITLSIMK; LITLSIMKS; ITLSIMKST; TLSIMKSTL; LSIMKSTLQ; SIMKSTLQM; IMKSTLQML; MKSTLQMLL; KSTLQMLLF; STLQMLLFL; TLQMLLFLQ; LQMLLFLQK; QMLLFLQKV; MLLFLQKVK; LLFLQKVKI; LFLQKVKIK; FLQKVKIKK; LQKVKIKKV; QKVKIKKVF; KVKIKKVFV; VKIKKVFVS; KIKKVFVSK; IKKVFVSKQ; YLELMEMLY; NNIWQVLLG; NIWQVLLGC; IWQVLLGCT; WQVLLGCTV; QVLLGCTVC; VLLGCTVCY; LLGCTVCYL; LGCTVCYLK; GCTVCYLKW; CTVCYLKWI; TVCYLKWIL; YLIFCTVLF; LIFCTVLFS; IFCTVLFSM; FCTVLFSMY; CTVLFSMYL; TVLFSMYLK; VLFSMYLKE; LFSMYLKED; FSMYLKEDT; SMYLKEDTG; MYLKEDTGY; YLKEDTGYL; LKEDTGYLK; KEDTGYLKV; EDTGYLKVP; DTGYLKVPL; TGYLKVPLI; GYLKVPLIV; YLKVPLIVE; LKVPLIVEK; KVPLIVEKQ; VPLIVEKQH; ISTWLFLKM; KGQELNQRI; GQELNQRIC; QELNQRICL; ELNQRICLQ; LNQRICLQD; NQRICLQDM; QRICLQDME; TKEPKYFHQ; KEPKYFHQA; EPKYFHQAW; PKYFHQAWL; KYFHQAWLQ; MSILSLKPC; SILSLKPCK; ILSLKPCKL; LSLKPCKLD; SLKPCKLDL; ENPYKTQSS; NPYKTQSSY; PYKTQSSYL; YKTQSSYLK; KTQSSYLKK; TQSSYLKKE; QSSYLKKEF; SSYLKKEFY; SYLKKEFYK; YLKKEFYKV; LKKEFYKVE; LILQLIYNL; ILQLIYNLE; LQLIYNLEL; QLIYNLELL; LIYNLELLN; IYNLELLNG; YNLELLNGR; NLELLNGRK; LELLNGRKG; ELLNGRKGW; LLNGRKGWI; LNGRKGWIL; NGRKGWILR; NIIYAWGNV; IIYAWGNVF; IYAWGNVFL; YAWGNVFLI; AWGNVFLIL; WGNVFLILQ; GNVFLILQE; NVFLILQEK; VFLILQEKR; FLILQEKRI; LILQEKRIQ; ILQEKRIQK; LQEKRIQKL; QEKRIQKLK; EKRIQKLKT; KRIQKLKTL; RIQKLKTLD; IQKLKTLDM; QKLKTLDMD; KLKTLDMDQ; LKTLDMDQA; KTLDMDQAL; TLDMDQALN; LDMDQALNP; DMDQALNPN; MDQALNPNH; DQALNPNHN; QALNPNHNA; ALNPNHNAL; LNPNHNALP; NPNHNALPK; PNHNALPKS; NHNALPKSQ; HNALPKSQI; NALPKSQIL; ALPKSQILQ; LPKSQILQP; PKSQILQPL; KSQILQPLL; SQILQPLLK; QILQPLLKI; ILQPLLKIP; LQPLLKIPK; QPLLKIPKG; PLLKIPKGQ; LLKIPKGQT; LKIPKGQTP; KIPKGQTPI; IPKGQTPIV; PKGQTPIVK; KGQTPIVKS; GQTPIVKSC; QTPIVKSCI; TPIVKSCIC; PIVKSCICV; IVKSCICVK; VKSCICVKA; KSCICVKAF; SCICVKAFS; CICVKAFSV; ICVKAFSVL; CVKAFSVLK; VKAFSVLKG; KAFSVLKGL; AFSVLKGLK; FSVLKGLKH; SVLKGLKHH; VLKGLKHHP; LKGLKHHPQ; KGLKHHPQN; GLKHHPQNN; LKHHPQNNT; KHHPQNNTS; HHPQNNTSL; HPQNNTSLK; PQNNTSLKV; QNNTSLKVA; NNTSLKVAY; NTSLKVAYT; TSLKVAYTK; SLKVAYTKA; LKVAYTKAA; KVAYTKAAF; VAYTKAAFI; AYTKAAFIK; YTKAAFIKC; TKAAFIKCI; KAAFIKCIC; AAFIKCICT; AFIKCICTI; FIKCICTIK; IKCICTIKA; KCICTIKAP; CICTIKAPV; SILVCNCPC; ILVCNCPCL; LVCNCPCLS; VCNCPCLSI; CNCPCLSIY; NCPCLSIYL; CPCLSIYLI; PCLSIYLII; CLSIYLIIS; LSIYLIISG; SIYLIISGS; IYLIISGSP; YLIISGSPG; LIISGSPGS; IISGSPGSL; ISGSPGSLS; SGSPGSLSV; GSPGSLSVP; SPGSLSVPS; PGSLSVPSN; GSLSVPSNT; SLSVPSNTL; LSVPSNTLT; SVPSNTLTS; VPSNTLTSS; PSNTLTSST; SNTLTSSTW; NTLTSSTWD; TLTSSTWDS; LTSSTWDSI; TSSTWDSIP; SSTWDSIPY; STWDSIPYI; TWDSIPYIG; WDSIPYIGC; DSIPYIGCP; SIPYIGCPS; IPYIGCPST; PYIGCPSTL; YIGCPSTLW; IGCPSTLWV; GCPSTLWVL; CPSTLWVLL; PSTLWVLLF; STLWVLLFI; TLWVLLFIR; LWVLLFIRS; WVLLFIRSL; VLLFIRSLS; LLFIRSLSK; LFIRSLSKK; FIRSLSKKE; IRSLSKKEI; RSLSKKEIG; GFFTDLFLR; FFTDLFLRR; FTDLFLRRI; TDLFLRRIL; DLFLRRILK; LFLRRILKY; FLRRILKYL; LRRILKYLA; RRILKYLAR; RILKYLARP; ILKYLARPL; LKYLARPLH; KYLARPLHC; YLARPLHCC; LARPLHCCV; ARPLHCCVP; RPLHCCVPE; PLHCCVPEL; LHCCVPELL; HCCVPELLV; CCVPELLVN; CVPELLVNR; VPELLVNRP; PELLVNRPQ; ELLVNRPQI; LLVNRPQIS; LVNRPQISA; VNRPQISAA; NRPQISAAE; RPQISAAET; PQISAAETY; QISAAETYR; ISAAETYRL; SAAETYRLS; AAETYRLSA; AETYRLSAL; ETYRLSALQ; TYRLSALQR; YRLSALQRG; RLSALQRGP; LSALQRGPT; SALQRGPTP; ALQRGPTPC; LQRGPTPCS; QRGPTPCSS; RGPTPCSSS; GPTPCSSSN; PTPCSSSNT; TPCSSSNTV; PCSSSNTVV; CSSSNTVVA; SSSNTVVAV; SSNTVVAVL; SNTVVAVLV; NTVVAVLVT; STGGTFSPP; TGGTFSPPV; GGTFSPPVK; GTFSPPVKV; TFSPPVKVP; FSPPVKVPK; SPPVKVPKY; PPVKVPKYL; PVKVPKYLA; VKVPKYLAF; KVPKYLAFS; VPKYLAFSF; PKYLAFSFL; KYLAFSFLL; YLAFSFLLG; LAFSFLLGS; AFSFLLGSG; FSFLLGSGT; SFLLGSGTQ; FLLGSGTQH; LLGSGTQHS; LGSGTQHST; GSGTQHSTG; ALWSVFITW; LWSVFITWD; WSVFITWDW; SVFITWDWA; VFITWDWAV; FITWDWAVG; ITWDWAVGF; TWDWAVGFL; WDWAVGFLG; DWAVGFLGV; WAVGFLGVI; AVGFLGVIV; VGFLGVIVP; GFLGVIVPS; FLGVIVPSG; LGVIVPSGY; GVIVPSGYF; VIVPSGYFD; IVPSGYFDL; FISTPCISK; ISTPCISKG; STPCISKGS; TPCISKGSP; PCISKGSPP; CISKGSPPT; ISKGSPPTA; SKGSPPTAK; KGSPPTAKK; GSPPTAKKW; SPPTAKKWK; PPTAKKWKL; PTAKKWKLL; TAKKWKLLP; IGFPPPCSC; GFPPPCSCT; FPPPCSCTF; PPPCSCTFC; PPCSCTFCD; PCSCTFCDP; CSCTFCDPA; RLSMLVIPI; LSMLVIPIT; SMLVIPITS; MLVIPITSV; LVIPITSVC; VIPITSVCT; IPITSVCTV; PITSVCTVT; ITSVCTVTA; TSVCTVTAS; SVCTVTASH; VCTVTASHI; CTVTASHIS; TVTASHISR; VTASHISRF; TASHISRFP; ASHISRFPQ; SHISRFPQV; HISRFPQVR; ISRFPQVRS; SRFPQVRSS; RFPQVRSSF; FPQVRSSFK; PQVRSSFKL; QVRSSFKLG; VRSSFKLGR; RSSFKLGRG; SSFKLGRGI; SFKLGRGIL; FKLGRGILA; KLGRGILAV; LGRGILAVL; QGSIFLSGL; GSIFLSGLS; SIFLSGLSL; IFLSGLSLL; FLSGLSLLK; LSGLSLLKS; SGLSLLKSF; GLSLLKSFS; LSLLKSFSA; SLLKSFSAL; LLKSFSALS; LKSFSALSF; KSFSALSFR; SFSALSFRL; FSALSFRLK; SALSFRLKP; ALSFRLKPL; LSFRLKPLR; SFRLKPLRF; FRLKPLRFS; RLKPLRFSS; LKPLRFSSG; KPLRFSSGS; PLRFSSGSP; LRFSSGSPI; RFSSGSPIS; FSSGSPISG; SSGSPISGF; SGSPISGFR; GSPISGFRK; SPISGFRKH; PISGFRKHS; ISGFRKHST; SGFRKHSTS; GFRKHSTSV; FRKHSTSVI; RKHSTSVIA; KHSTSVIAS; HSTSVIAST; STSVIASTP; TSVIASTPV; SVIASTPVL; VIASTPVLT; IASTPVLTS; ASTPVLTSR; STPVLTSRT; TPVLTSRTS; PVLTSRTST; VLTSRTSTP; LTSRTSTPP; TSRTSTPPF; SRTSTPPFI; RTSTPPFIS; TSTPPFISS; STPPFISSF; TPPFISSFG; PPFISSFGT; PFISSFGTC; FISSFGTCT; ISSFGTCTG; SSFGTCTGS; SFGTCTGSF; FGTCTGSFG; GTCTGSFGF; TCTGSFGFL; CTGSFGFLG; TGSFGFLGA; GSFGFLGAA; SFGFLGAAP; FGFLGAAPG; GFLGAAPGH; FLGAAPGHS; LGAAPGHSP; GAAPGHSPF; AAPGHSPFL; APGHSPFLL; PGHSPFLLV; GHSPFLLVG; HSPFLLVGA; SPFLLVGAI; PFLLVGAIF; FLLVGAIFI; LLVGAIFIC; LVGAIFICF; VGAIFICFK; GAIFICFKS; AIFICFKSR; IFICFKSRC; FICFKSRCY; ICFKSRCYS; CFKSRCYSP; FKSRCYSPV; KSRCYSPVQ; SRCYSPVQA; RQHPLRSSS; QHPLRSSSL; HPLRSSSLI; PLRSSSLIS; LRSSSLIST; RSSSLISTS; SSSLISTSW; SSLISTSWG; SLISTSWGN; LISTSWGNS; ISTSWGNSF; STSWGNSFF; TSWGNSFFY; SWGNSFFYK; WGNSFFYKL; GNSFFYKLS; VHSLCNFFY; HSLCNFFYT; SLCNFFYTV; LCNFFYTVS; CNFFYTVSI; NFFYTVSII; FFYTVSIIY; FYTVSIIYT; YTVSIIYTI; TVSIIYTIS; VSIIYTISM; SIIYTISMA; IIYTISMAK; IYTISMAKM; YTISMAKMY; TISMAKMYT; ISMAKMYTG; SMAKMYTGT; MAKMYTGTF; AKMYTGTFP; KMYTGTFPF; MYTGTFPFS; YTGTFPFSY; TGTFPFSYL; GTFPFSYLS; TFPFSYLSN; FPFSYLSNH; GPNRGKIRI; PNRGKIRII; NRGKIRIIL; RGKIRIILL; GKIRIILLN; KIRIILLNI; IRIILLNII; RIILLNIII; IILLNIIIK; ILLNIIIKV; LLNIIIKVY; LNIIIKVYR; NIIIKVYRG; IIIKVYRGI; IIKVYRGIY; IKVYRGIYN; KVYRGIYNC; VYRGIYNCP; YRGIYNCPG; RGIYNCPGS; GIYNCPGSF; IYNCPGSFL; YNCPGSFLQ; NCPGSFLQK; CPGSFLQKS; PGSFLQKSS; GSFLQKSSQ; SFLQKSSQG; FLQKSSQGV; LQKSSQGVS; QKSSQGVSK; KSSQGVSKK; SSQGVSKKS; SQGVSKKSF; QGVSKKSFC; GVSKKSFCS; VSKKSFCSS; SKKSFCSSL; KKSFCSSLQ; KSFCSSLQF; SFCSSLQFL; GYRRYIIPN; YRRYIIPNN; RRYIIPNNM; RYIIPNNMP; YIIPNNMPQ; IIPNNMPQS; IPNNMPQSL; PNNMPQSLG; NNMPQSLGN; NMPQSLGNS; MPQSLGNSS; PQSLGNSSK; QSLGNSSKQ; SLGNSSKQR; LGNSSKQRR; GNSSKQRRT; NSSKQRRTP; SSKQRRTPM; SKQRRTPMP; KQRRTPMPR; QRRTPMPRI; RRTPMPRIK; RTPMPRIKV; TPMPRIKVL; PMPRIKVLN; MPRIKVLNI; PRIKVLNII; RIKVLNIIN; IKVLNIINK; KVLNIINKS; VLNIINKSI; LNIINKSIY; NIINKSIYT; IINKSIYTR; INKSIYTRK; NKSIYTRKQ; KSIYTRKQN; SIYTRKQNI; IYTRKQNII; YTRKQNIIV; TRKQNIIVL; RKQNIIVLI; KQNIIVLIW; QNIIVLIWV; NIIVLIWVK; IIVLIWVKQ; IVLIWVKQF; VLIWVKQFQ; LIWVKQFQS; IWVKQFQSH; WVKQFQSHA; LLIEAYSGN; LIEAYSGNF; IEAYSGNFV; EAYSGNFVI; AYSGNFVIP; YSGNFVIPI; SGNFVIPII; GNFVIPIIK; NFVIPIIKE; FVIPIIKEL; VIPIIKELI; IPIIKELIP; PIIKELIPY; IIKELIPYL; IKELIPYLS; GTNTTNSLN; SSKPSNSPR; SKPSNSPRS; KPSNSPRST; PSNSPRSTS; SNSPRSTSN; NSPRSTSNY; SPRSTSNYS; PRSTSNYSI; RSTSNYSIC; STSNYSICL; TSNYSICLR; SNYSICLRS; GTCYALYSS; TCYALYSSK; CYALYSSKG; YALYSSKGC; ALYSSKGCN; LYSSKGCNL; YSSKGCNLN; SSKGCNLNF; SKGCNLNFY; KGCNLNFYS; GCNLNFYSS; CNLNFYSSS; NLNFYSSSS; LNFYSSSSL; NFYSSSSLP; FYSSSSLPS; YSSSSLPSS; SSSSLPSSN; SSSLPSSNF; SSLPSSNFS; SLPSSNFSH; KSCGSSSLR; SCGSSSLRY; CGSSSLRYT; GSSSLRYTG; SSSLRYTGN; SSTHEPGNT; STHEPGNTK; THEPGNTKK; HEPGNTKKK; EPGNTKKKG; PGNTKKKGL; GNTKKKGLL; NTKKKGLLT; ESFTESFTA; SFTESFTAG; FTESFTAGK; TESFTAGKA; ESFTAGKAV; SFTAGKAVV; FTAGKAVVL; TAGKAVVLL; AGKAVVLLF; GKAVVLLFF; KAVVLLFFP; AVVLLFFPS; VVLLFFPST; VLLFFPSTL; LLFFPSTLS; LFFPSTLSS; FFPSTLSSP; FPSTLSSPL; PSTLSSPLQ; STLSSPLQN; TLSSPLQNS; LSSPLQNSS; SSPLQNSSK; SPLQNSSKS; PLQNSSKSS; LQNSSKSSK; QNSSKSSKI; NSSKSSKIK; SSKSSKIKI; SKSSKIKIK; KSSKIKIKI; SSKIKIKIL; ALFFVPVQV; LFFVPVQVL; FFVPVQVLP; FVPVQVLPT; VPVQVLPTF; PVQVLPTFT; VQVLPTFTE; QVLPTFTEA; VLPTFTEAC; LPTFTEACR; PTFTEACRD; TFTEACRDS; FTEACRDSW; TEACRDSWR; EACRDSWRR; ACRDSWRRT; CRDSWRRTM; RDSWRRTMA; DSWRRTMAF; SWRRTMAFV; WRRTMAFVQ; RRTMAFVQF; RTMAFVQFN; TMAFVQFNW; MAFVQFNWG; AFVQFNWGQ; FVQFNWGQG; VQFNWGQGQ; QFNWGQGQD; FNWGQGQDS; ARKTCLSCT; RKTCLSCTF; KTCLSCTFL; TCLSCTFLP; CLSCTFLPE; LSCTFLPEV; SCTFLPEVM; CTFLPEVMV; TFLPEVMVW; FLPEVMVWL; LPEVMVWLH; PEVMVWLHS; EVMVWLHSM; VMVWLHSMG; MVWLHSMGK; VWLHSMGKQ; WLHSMGKQL; LHSMGKQLL; HSMGKQLLP; SMGKQLLPV; MGKQLLPVS; GKQLLPVSH; KQLLPVSHA; QLLPVSHAL; LLPVSHALS; LPVSHALSF; PVSHALSFL; VSHALSFLR; SHALSFLRS; HALSFLRSW; ALSFLRSWF; LSFLRSWFG; SFLRSWFGC; FLRSWFGCI; LRSWFGCIP; RSWFGCIPL; GHGLAAFHG; AAPPCGLFF; APPCGLFFY; PPCGLFFYN; PCGLFFYNI; EAEAASAST; AEAASASTL; EAASASTLS; AASASTLSL; ASASTLSLK; GLAKLFGEI; LAKLFGEIP; AKLFGEIPI; KLFGEIPIL; LFGEIPILL; FGEIPILLQ; GEIPILLQF; EIPILLQFL; IPILLQFLQ 10 mers: MDKVLNREES; DKVLNREESM; KVLNREESME; VLNREESMEL; LNREESMELM; NREESMELMD; REESMELMDL; EESMELMDLL; ESMELMDLLG; SMELMDLLGL; MELMDLLGLE; ELMDLLGLER; LMDLLGLERA; MDLLGLERAA; DLLGLERAAW; LLGLERAAWG; LGLERAAWGN; GLERAAWGNL; LERAAWGNLP; ERAAWGNLPL; RAAWGNLPLM; AAWGNLPLMR; AWGNLPLMRK; WGNLPLMRKA; GNLPLMRKAY; NLPLMRKAYL; LPLMRKAYLR; PLMRKAYLRK; LMRKAYLRKC; MRKAYLRKCK; RKAYLRKCKE; KAYLRKCKEF; AYLRKCKEFH; YLRKCKEFHP; LRKCKEFHPD; RKCKEFHPDK; KCKEFHPDKG; CKEFHPDKGG; KEFHPDKGGD; EFHPDKGGDE; FHPDKGGDED; HPDKGGDEDK; PDKGGDEDKM; DKGGDEDKMK; KGGDEDKMKR; GGDEDKMKRM; GDEDKMKRMN; DEDKMKRMNT; EDKMKRMNTL; DKMKRMNTLY; KMKRMNTLYK; MKRMNTLYKK; KRMNTLYKKM; RMNTLYKKME; MNTLYKKMEQ; NTLYKKMEQD; TLYKKMEQDV; LYKKMEQDVK; YKKMEQDVKV; KKMEQDVKVA; KMEQDVKVAH; MEQDVKVAHQ; EQDVKVAHQP; QDVKVAHQPD; DVKVAHQPDF; VKVAHQPDFG; KVAHQPDFGT; VAHQPDFGTW; AHQPDFGTWS; HQPDFGTWSS; QPDFGTWSSS; PDFGTWSSSE; DFGTWSSSEV; FGTWSSSEVC; GTWSSSEVCA; TWSSSEVCAD; WSSSEVCADF; SSSEVCADFP; SSEVCADFPL; SEVCADFPLC; EVCADFPLCP; VCADFPLCPD; CADFPLCPDT; ADFPLCPDTL; DFPLCPDTLY; FPLCPDTLYC; PLCPDTLYCK; LCPDTLYCKE; CPDTLYCKEW; PDTLYCKEWP; DTLYCKEWPI; TLYCKEWPIC; LYCKEWPICS; YCKEWPICSK; CKEWPICSKK; KEWPICSKKP; EWPICSKKPS; WPICSKKPSV; PICSKKPSVH; ICSKKPSVHC; CSKKPSVHCP; SKKPSVHCPC; KKPSVHCPCM; KPSVHCPCML; PSVHCPCMLC; SVHCPCMLCQ; VHCPCMLCQL; HCPCMLCQLR; CPCMLCQLRL; PCMLCQLRLR; CMLCQLRLRH; MLCQLRLRHL; LCQLRLRHLN; CQLRLRHLNR; QLRLRHLNRK; LRLRHLNRKF; RLRHLNRKFL; LRHLNRKFLR; RHLNRKFLRK; HLNRKFLRKE; LNRKFLRKEP; NRKFLRKEPL; RKFLRKEPLV; KFLRKEPLVW; FLRKEPLVWI; LRKEPLVWID; RKEPLVWIDC; KEPLVWIDCY; EPLVWIDCYC; PLVWIDCYCI; LVWIDCYCID; VWIDCYCIDC; WIDCYCIDCF; IDCYCIDCFT; DCYCIDCFTQ; CYCIDCFTQW; YCIDCFTQWF; CIDCFTQWFG; IDCFTQWFGL; DCFTQWFGLD; CFTQWFGLDL; FTQWFGLDLT; TQWFGLDLTE; QWFGLDLTEE; WFGLDLTEET; FGLDLTEETL; GLDLTEETLQ; LDLTEETLQW; DLTEETLQWW; LTEETLQWWV; TEETLQWWVQ; EETLQWWVQI; ETLQWWVQII; TLQWWVQIIG; LQWWVQIIGE; QWWVQIIGET; WWVQIIGETP; WVQIIGETPF; VQIIGETPFR; QIIGETPFRD; IIGETPFRDL; IGETPFRDLK; GETPFRDLKL; KALSNYFFYR; ALSNYFFYRC; LSNYFFYRCQ; SNYFFYRCQP; NYFFYRCQPM; YFFYRCQPME; FFYRCQPMEQ; FYRCQPMEQK; YRCQPMEQKS; RCQPMEQKSG; CQPMEQKSGS; QPMEQKSGSP; PMEQKSGSPG; MEQKSGSPGG; EQKSGSPGGV; QKSGSPGGVP; KSGSPGGVPL; SGSPGGVPLM; GSPGGVPLMK; SPGGVPLMKN; PGGVPLMKNG; GGVPLMKNGM; GVPLMKNGMK; VPLMKNGMKI; PLMKNGMKIY; LMKNGMKIYF; MKNGMKIYFA; KNGMKIYFAM; NGMKIYFAMK; GMKIYFAMKI; MKIYFAMKIC; KIYFAMKICL; IYFAMKICLP; YFAMKICLPV; FAMKICLPVM; AMKICLPVMK; MKICLPVMKK; KICLPVMKKQ; ICLPVMKKQQ; CLPVMKKQQQ; LPVMKKQQQI; PVMKKQQQIL; VMKKQQQILN; MKKQQQILNT; KKQQQILNTQ; KQQQILNTQH; QQQILNTQHH; QQILNTQHHP; QILNTQHHPK; ILNTQHHPKK; LNTQHHPKKK; NTQHHPKKKE; TQHHPKKKER; KTLKTFPLIY; TLKTFPLIYT; LKTFPLIYTS; KTFPLIYTSF; TFPLIYTSFL; FPLIYTSFLV; PLIYTSFLVK; LIYTSFLVKL; IYTSFLVKLY; YTSFLVKLYL; TSFLVKLYLV; SFLVKLYLVI; FLVKLYLVIE; LVKLYLVIEP; VKLYLVIEPL; KLYLVIEPLP; LYLVIEPLPA; YLVIEPLPAL; LVIEPLPALL; VIEPLPALLC; IEPLPALLCI; EPLPALLCIL; PLPALLCILL; LPALLCILLK; PALLCILLKK; ALLCILLKKK; LLCILLKKKL; LCILLKKKLK; CILLKKKLKF; ILLKKKLKFC; LLKKKLKFCI; LKKKLKFCIK; KKKLKFCIKN; KKLKFCIKNL; KLKFCIKNLW; LKFCIKNLWK; KFCIKNLWKN; FCIKNLWKNI; CIKNLWKNIL; LLLVDTCVLG; LLVDTCVLGI; LVDTCVLGII; VDTCVLGIIL; DTCVLGIILY; TCVLGIILYS; CVLGIILYSF; LHIDIEFLQL; HIDIEFLQLI; IDIEFLQLII; DIEFLQLIIS; IEFLQLIISV; EFLQLIISVK; FLQLIISVKS; LQLIISVKSC; QLIISVKSCV; LIISVKSCVP; IISVKSCVPL; ISVKSCVPLV; SVKSCVPLVF; FVRVLIRNTY; VRVLIRNTYY; RVLIRNTYYI; VLIRNTYYIV; LIRNTYYIVP; RSMILAQKSL; SMILAQKSLK; MILAQKSLKK; ILAQKSLKKQ; LAQKSLKKQS; AQKSLKKQSR; QKSLKKQSRC; KSLKKQSRCL; SLKKQSRCLG; LKKQSRCLGN; RQSVRMCFYY; RSVKSVRKKT; SVKSVRKKTS; VKSVRKKTSL; KSVRKKTSLI; SVRKKTSLIT; VRKKTSLITL; RKKTSLITLS; KKTSLITLSI; KTSLITLSIM; TSLITLSIMK; SLITLSIMKS; LITLSIMKST; ITLSIMKSTL; TLSIMKSTLQ; LSIMKSTLQM; SIMKSTLQML; IMKSTLQMLL; MKSTLQMLLF; KSTLQMLLFL; STLQMLLFLQ; TLQMLLFLQK; LQMLLFLQKV; QMLLFLQKVK; MLLFLQKVKI; LLFLQKVKIK; LFLQKVKIKK; FLQKVKIKKV; LQKVKIKKVF; QKVKIKKVFV; KVKIKKVFVS; VKIKKVFVSK; KIKKVFVSKQ; NNIWQVLLGC; NIWQVLLGCT; IWQVLLGCTV; WQVLLGCTVC; QVLLGCTVCY; VLLGCTVCYL; LLGCTVCYLK; LGCTVCYLKW; GCTVCYLKWI; CTVCYLKWIL; YLIFCTVLFS; LIFCTVLFSM; IFCTVLFSMY; FCTVLFSMYL; CTVLFSMYLK; TVLFSMYLKE; VLFSMYLKED; LFSMYLKEDT; FSMYLKEDTG; SMYLKEDTGY; MYLKEDTGYL; YLKEDTGYLK; LKEDTGYLKV; KEDTGYLKVP; EDTGYLKVPL; DTGYLKVPLI; TGYLKVPLIV; GYLKVPLIVE; YLKVPLIVEK; LKVPLIVEKQ; KVPLIVEKQH; KGQELNQRIC; GQELNQRICL; QELNQRICLQ; ELNQRICLQD; LNQRICLQDM; NQRICLQDME; TKEPKYFHQA; KEPKYFHQAW; EPKYFHQAWL; PKYFHQAWLQ; MSILSLKPCK; SILSLKPCKL; ILSLKPCKLD; LSLKPCKLDL; ENPYKTQSSY; NPYKTQSSYL; PYKTQSSYLK; YKTQSSYLKK; KTQSSYLKKE; TQSSYLKKEF; QSSYLKKEFY; SSYLKKEFYK; SYLKKEFYKV; YLKKEFYKVE; LILQLIYNLE; ILQLIYNLEL; LQLIYNLELL; QLIYNLELLN; LIYNLELLNG; IYNLELLNGR; YNLELLNGRK; NLELLNGRKG; LELLNGRKGW; ELLNGRKGWI; LLNGRKGWIL; LNGRKGWILR; NIIYAWGNVF; IIYAWGNVFL; IYAWGNVFLI; YAWGNVFLIL; AWGNVFLILQ; WGNVFLILQE; GNVFLILQEK; NVFLILQEKR; VFLILQEKRI; FLILQEKRIQ; LILQEKRIQK; ILQEKRIQKL; LQEKRIQKLK; QEKRIQKLKT; EKRIQKLKTL; KRIQKLKTLD; RIQKLKTLDM; IQKLKTLDMD; QKLKTLDMDQ; KLKTLDMDQA; LKTLDMDQAL; KTLDMDQALN; TLDMDQALNP; LDMDQALNPN; DMDQALNPNH; MDQALNPNHN; DQALNPNHNA; QALNPNHNAL; ALNPNHNALP; LNPNHNALPK; NPNHNALPKS; PNHNALPKSQ; NHNALPKSQI; HNALPKSQIL; NALPKSQILQ; ALPKSQILQP; LPKSQILQPL; PKSQILQPLL; KSQILQPLLK; SQILQPLLKI; QILQPLLKIP; ILQPLLKIPK; LQPLLKIPKG; QPLLKIPKGQ; PLLKIPKGQT; LLKIPKGQTP; LKIPKGQTPI; KIPKGQTPIV; IPKGQTPIVK; PKGQTPIVKS; KGQTPIVKSC; GQTPIVKSCI; QTPIVKSCIC; TPIVKSCICV; PIVKSCICVK; IVKSCICVKA; VKSCICVKAF; KSCICVKAFS; SCICVKAFSV; CICVKAFSVL; ICVKAFSVLK; CVKAFSVLKG; VKAFSVLKGL; KAFSVLKGLK; AFSVLKGLKH; FSVLKGLKHH; SVLKGLKHHP; VLKGLKHHPQ; LKGLKHHPQN; KGLKHHPQNN; GLKHHPQNNT; LKHHPQNNTS; KHHPQNNTSL; HHPQNNTSLK; HPQNNTSLKV; PQNNTSLKVA; QNNTSLKVAY; NNTSLKVAYT; NTSLKVAYTK; TSLKVAYTKA; SLKVAYTKAA; LKVAYTKAAF; KVAYTKAAFI; VAYTKAAFIK; AYTKAAFIKC; YTKAAFIKCI; TKAAFIKCIC; KAAFIKCICT; AAFIKCICTI; AFIKCICTIK; FIKCICTIKA; IKCICTIKAP; KCICTIKAPV; SILVCNCPCL; ILVCNCPCLS; LVCNCPCLSI; VCNCPCLSIY; CNCPCLSIYL; NCPCLSIYLI; CPCLSIYLII; PCLSIYLIIS; CLSIYLIISG; LSIYLIISGS; SIYLIISGSP; IYLIISGSPG; YLIISGSPGS; LIISGSPGSL; IISGSPGSLS; ISGSPGSLSV; SGSPGSLSVP; GSPGSLSVPS; SPGSLSVPSN; PGSLSVPSNT; GSLSVPSNTL; SLSVPSNTLT; LSVPSNTLTS; SVPSNTLTSS; VPSNTLTSST; PSNTLTSSTW; SNTLTSSTWD; NTLTSSTWDS; TLTSSTWDSI; LTSSTWDSIP; TSSTWDSIPY; SSTWDSIPYI; STWDSIPYIG; TWDSIPYIGC; WDSIPYIGCP; DSIPYIGCPS; SIPYIGCPST; IPYIGCPSTL; PYIGCPSTLW; YIGCPSTLWV; IGCPSTLWVL; GCPSTLWVLL; CPSTLWVLLF; PSTLWVLLFI; STLWVLLFIR; TLWVLLFIRS; LWVLLFIRSL; WVLLFIRSLS; VLLFIRSLSK; LLFIRSLSKK; LFIRSLSKKE; FIRSLSKKEI; IRSLSKKEIG; GFFTDLFLRR; FFTDLFLRRI; FTDLFLRRIL; TDLFLRRILK; DLFLRRILKY; LFLRRILKYL; FLRRILKYLA; LRRILKYLAR; RRILKYLARP; RILKYLARPL; ILKYLARPLH; LKYLARPLHC; KYLARPLHCC; YLARPLHCCV; LARPLHCCVP; ARPLHCCVPE; RPLHCCVPEL; PLHCCVPELL; LHCCVPELLV; HCCVPELLVN; CCVPELLVNR; CVPELLVNRP; VPELLVNRPQ; PELLVNRPQI; ELLVNRPQIS; LLVNRPQISA; LVNRPQISAA; VNRPQISAAE; NRPQISAAET; RPQISAAETY; PQISAAETYR; QISAAETYRL; ISAAETYRLS; SAAETYRLSA; AAETYRLSAL; AETYRLSALQ; ETYRLSALQR; TYRLSALQRG; YRLSALQRGP; RLSALQRGPT; LSALQRGPTP; SALQRGPTPC; ALQRGPTPCS; LQRGPTPCSS; QRGPTPCSSS; RGPTPCSSSN; GPTPCSSSNT; PTPCSSSNTV; TPCSSSNTVV; PCSSSNTVVA; CSSSNTVVAV; SSSNTVVAVL; SSNTVVAVLV; SNTVVAVLVT; STGGTFSPPV; TGGTFSPPVK; GGTFSPPVKV; GTFSPPVKVP; TFSPPVKVPK; FSPPVKVPKY; SPPVKVPKYL; PPVKVPKYLA; PVKVPKYLAF; VKVPKYLAFS; KVPKYLAFSF; VPKYLAFSFL; PKYLAFSFLL; KYLAFSFLLG; YLAFSFLLGS; LAFSFLLGSG; AFSFLLGSGT; FSFLLGSGTQ; SFLLGSGTQH; FLLGSGTQHS; LLGSGTQHST; LGSGTQHSTG; ALWSVFITWD; LWSVFITWDW; WSVFITWDWA; SVFITWDWAV; VFITWDWAVG; FITWDWAVGF; ITWDWAVGFL; TWDWAVGFLG; WDWAVGFLGV; DWAVGFLGVI; WAVGFLGVIV; AVGFLGVIVP; VGFLGVIVPS; GFLGVIVPSG; FLGVIVPSGY; LGVIVPSGYF; GVIVPSGYFD; VIVPSGYFDL; FISTPCISKG; ISTPCISKGS; STPCISKGSP; TPCISKGSPP; PCISKGSPPT; CISKGSPPTA; ISKGSPPTAK; SKGSPPTAKK; KGSPPTAKKW; GSPPTAKKWK; SPPTAKKWKL; PPTAKKWKLL; PTAKKWKLLP; IGFPPPCSCT; GFPPPCSCTF; FPPPCSCTFC; PPPCSCTFCD; PPCSCTFCDP; PCSCTFCDPA; RLSMLVIPIT; LSMLVIPITS; SMLVIPITSV; MLVIPITSVC; LVIPITSVCT; VIPITSVCTV; IPITSVCTVT; PITSVCTVTA; ITSVCTVTAS; TSVCTVTASH; SVCTVTASHI; VCTVTASHIS; CTVTASHISR; TVTASHISRF; VTASHISRFP; TASHISRFPQ; ASHISRFPQV; SHISRFPQVR; HISRFPQVRS; ISRFPQVRSS; SRFPQVRSSF; RFPQVRSSFK; FPQVRSSFKL; PQVRSSFKLG; QVRSSFKLGR; VRSSFKLGRG; RSSFKLGRGI; SSFKLGRGIL; SFKLGRGILA; FKLGRGILAV; KLGRGILAVL; QGSIFLSGLS; GSIFLSGLSL; SIFLSGLSLL; IFLSGLSLLK; FLSGLSLLKS; LSGLSLLKSF; SGLSLLKSFS; GLSLLKSFSA; LSLLKSFSAL; SLLKSFSALS; LLKSFSALSF; LKSFSALSFR; KSFSALSFRL; SFSALSFRLK; FSALSFRLKP; SALSFRLKPL; ALSFRLKPLR; LSFRLKPLRF; SFRLKPLRFS; FRLKPLRFSS; RLKPLRFSSG; LKPLRFSSGS; KPLRFSSGSP; PLRFSSGSPI; LRFSSGSPIS; RFSSGSPISG; FSSGSPISGF; SSGSPISGFR; SGSPISGFRK; GSPISGFRKH; SPISGFRKHS; PISGFRKHST; ISGFRKHSTS; SGFRKHSTSV; GFRKHSTSVI; FRKHSTSVIA; RKHSTSVIAS; KHSTSVIAST; HSTSVIASTP; STSVIASTPV; TSVIASTPVL; SVIASTPVLT; VIASTPVLTS; IASTPVLTSR; ASTPVLTSRT; STPVLTSRTS; TPVLTSRTST; PVLTSRTSTP; VLTSRTSTPP; LTSRTSTPPF; TSRTSTPPFI; SRTSTPPFIS; RTSTPPFISS; TSTPPFISSF; STPPFISSFG; TPPFISSFGT; PPFISSFGTC; PFISSFGTCT; FISSFGTCTG; ISSFGTCTGS; SSFGTCTGSF; SFGTCTGSFG; FGTCTGSFGF; GTCTGSFGFL; TCTGSFGFLG; CTGSFGFLGA; TGSFGFLGAA; GSFGFLGAAP; SFGFLGAAPG; FGFLGAAPGH; GFLGAAPGHS; FLGAAPGHSP; LGAAPGHSPF; GAAPGHSPFL; AAPGHSPFLL; APGHSPFLLV; PGHSPFLLVG; GHSPFLLVGA; HSPFLLVGAI; SPFLLVGAIF; PFLLVGAIFI; FLLVGAIFIC; LLVGAIFICF; LVGAIFICFK; VGAIFICFKS; GAIFICFKSR; AIFICFKSRC; IFICFKSRCY; FICFKSRCYS; ICFKSRCYSP; CFKSRCYSPV; FKSRCYSPVQ; KSRCYSPVQA; RQHPLRSSSL; QHPLRSSSLI; HPLRSSSLIS; PLRSSSLIST; LRSSSLISTS; RSSSLISTSW; SSSLISTSWG; SSLISTSWGN; SLISTSWGNS; LISTSWGNSF; ISTSWGNSFF; STSWGNSFFY; TSWGNSFFYK; SWGNSFFYKL; WGNSFFYKLS; VHSLCNFFYT; HSLCNFFYTV; SLCNFFYTVS; LCNFFYTVSI; CNFFYTVSII; NFFYTVSIIY; FFYTVSIIYT; FYTVSIIYTI; YTVSIIYTIS; TVSIIYTISM; VSIIYTISMA; SIIYTISMAK; IIYTISMAKM; IYTISMAKMY; YTISMAKMYT; TISMAKMYTG; ISMAKMYTGT; SMAKMYTGTF; MAKMYTGTFP; AKMYTGTFPF; KMYTGTFPFS; MYTGTFPFSY; YTGTFPFSYL; TGTFPFSYLS; GTFPFSYLSN; TFPFSYLSNH; GPNRGKIRII; PNRGKIRIIL; NRGKIRIILL; RGKIRIILLN; GKIRIILLNI; KIRIILLNII; IRIILLNIII; RIILLNIIIK; IILLNIIIKV; ILLNIIIKVY; LLNIIIKVYR; LNIIIKVYRG; NIIIKVYRGI; IIIKVYRGIY; IIKVYRGIYN; IKVYRGIYNC; KVYRGIYNCP; VYRGIYNCPG; YRGIYNCPGS; RGIYNCPGSF; GIYNCPGSFL; IYNCPGSFLQ; YNCPGSFLQK; NCPGSFLQKS; CPGSFLQKSS; PGSFLQKSSQ; GSFLQKSSQG; SFLQKSSQGV; FLQKSSQGVS; LQKSSQGVSK; QKSSQGVSKK; KSSQGVSKKS; SSQGVSKKSF; SQGVSKKSFC; QGVSKKSFCS; GVSKKSFCSS; VSKKSFCSSL; SKKSFCSSLQ; KKSFCSSLQF; KSFCSSLQFL; GYRRYIIPNN; YRRYIIPNNM; RRYIIPNNMP; RYIIPNNMPQ; YIIPNNMPQS; IIPNNMPQSL; IPNNMPQSLG; PNNMPQSLGN; NNMPQSLGNS; NMPQSLGNSS; MPQSLGNSSK; PQSLGNSSKQ; QSLGNSSKQR; SLGNSSKQRR; LGNSSKQRRT; GNSSKQRRTP; NSSKQRRTPM; SSKQRRTPMP; SKQRRTPMPR; KQRRTPMPRI; QRRTPMPRIK; RRTPMPRIKV; RTPMPRIKVL; TPMPRIKVLN; PMPRIKVLNI; MPRIKVLNII; PRIKVLNIIN; RIKVLNIINK; IKVLNIINKS; KVLNIINKSI; VLNIINKSIY; LNIINKSIYT; NIINKSIYTR; IINKSIYTRK; INKSIYTRKQ; NKSIYTRKQN; KSIYTRKQNI; SIYTRKQNII; IYTRKQNIIV; YTRKQNIIVL; TRKQNIIVLI; RKQNIIVLIW; KQNIIVLIWV; QNIIVLIWVK; NIIVLIWVKQ; IIVLIWVKQF; IVLIWVKQFQ; VLIWVKQFQS; LIWVKQFQSH; IWVKQFQSHA; LLIEAYSGNF; LIEAYSGNFV; IEAYSGNFVI; EAYSGNFVIP; AYSGNFVIPI; YSGNFVIPII; SGNFVIPIIK; GNFVIPIIKE; NFVIPIIKEL; FVIPIIKELI; VIPIIKELIP; IPIIKELIPY; PIIKELIPYL; IIKELIPYLS; SSKPSNSPRS; SKPSNSPRST; KPSNSPRSTS; PSNSPRSTSN; SNSPRSTSNY; NSPRSTSNYS; SPRSTSNYSI; PRSTSNYSIC; RSTSNYSICL; STSNYSICLR; TSNYSICLRS; GTCYALYSSK; TCYALYSSKG; CYALYSSKGC; YALYSSKGCN; ALYSSKGCNL; LYSSKGCNLN; YSSKGCNLNF; SSKGCNLNFY; SKGCNLNFYS; KGCNLNFYSS; GCNLNFYSSS; CNLNFYSSSS; NLNFYSSSSL; LNFYSSSSLP; NFYSSSSLPS; FYSSSSLPSS; YSSSSLPSSN; SSSSLPSSNF; SSSLPSSNFS; SSLPSSNFSH; KSCGSSSLRY; SCGSSSLRYT; CGSSSLRYTG; GSSSLRYTGN; SSTHEPGNTK; STHEPGNTKK; THEPGNTKKK; HEPGNTKKKG; EPGNTKKKGL; PGNTKKKGLL; GNTKKKGLLT; ESFTESFTAG; SFTESFTAGK; FTESFTAGKA; TESFTAGKAV; ESFTAGKAVV; SFTAGKAVVL; FTAGKAVVLL; TAGKAVVLLF; AGKAVVLLFF; GKAVVLLFFP; KAVVLLFFPS; AVVLLFFPST; VVLLFFPSTL; VLLFFPSTLS; LLFFPSTLSS; LFFPSTLSSP; FFPSTLSSPL; FPSTLSSPLQ; PSTLSSPLQN; STLSSPLQNS; TLSSPLQNSS; LSSPLQNSSK; SSPLQNSSKS; SPLQNSSKSS; PLQNSSKSSK; LQNSSKSSKI; QNSSKSSKIK; NSSKSSKIKI; SSKSSKIKIK; SKSSKIKIKI; KSSKIKIKIL; ALFFVPVQVL; LFFVPVQVLP; FFVPVQVLPT; FVPVQVLPTF; VPVQVLPTFT; PVQVLPTFTE; VQVLPTFTEA; QVLPTFTEAC; VLPTFTEACR; LPTFTEACRD; PTFTEACRDS; TFTEACRDSW; FTEACRDSWR; TEACRDSWRR; EACRDSWRRT; ACRDSWRRTM; CRDSWRRTMA; RDSWRRTMAF; DSWRRTMAFV; SWRRTMAFVQ; WRRTMAFVQF; RRTMAFVQFN; RTMAFVQFNW; TMAFVQFNWG; MAFVQFNWGQ; AFVQFNWGQG; FVQFNWGQGQ; VQFNWGQGQD; QFNWGQGQDS; ARKTCLSCTF; RKTCLSCTFL; KTCLSCTFLP; TCLSCTFLPE; CLSCTFLPEV; LSCTFLPEVM; SCTFLPEVMV; CTFLPEVMVW; TFLPEVMVWL; FLPEVMVWLH; LPEVMVWLHS; PEVMVWLHSM; EVMVWLHSMG; VMVWLHSMGK; MVWLHSMGKQ; VWLHSMGKQL; WLHSMGKQLL; LHSMGKQLLP; HSMGKQLLPV; SMGKQLLPVS; MGKQLLPVSH; GKQLLPVSHA; KQLLPVSHAL; QLLPVSHALS; LLPVSHALSF; LPVSHALSFL; PVSHALSFLR; VSHALSFLRS; SHALSFLRSW; HALSFLRSWF; ALSFLRSWFG; LSFLRSWFGC; SFLRSWFGCI; FLRSWFGCIP; LRSWFGCIPL; AAPPCGLFFY; APPCGLFFYN; PPCGLFFYNI; EAEAASASTL; AEAASASTLS; EAASASTLSL; AASASTLSLK; GLAKLFGEIP; LAKLFGEIPI; AKLFGEIPIL; KLFGEIPILL; LFGEIPILLQ; FGEIPILLQF; GEIPILLQFL; EIPILLQFLQ 11 mers: MDKVLNREESM; DKVLNREESME; KVLNREESMEL; VLNREESMELM; LNREESMELMD; NREESMELMDL; REESMELMDLL; EESMELMDLLG; ESMELMDLLGL; SMELMDLLGLE; MELMDLLGLER; ELMDLLGLERA; LMDLLGLERAA; MDLLGLERAAW; DLLGLERAAWG; LLGLERAAWGN; LGLERAAWGNL; GLERAAWGNLP; LERAAWGNLPL; ERAAWGNLPLM; RAAWGNLPLMR; AAWGNLPLMRK; AWGNLPLMRKA; WGNLPLMRKAY; GNLPLMRKAYL; NLPLMRKAYLR; LPLMRKAYLRK; PLMRKAYLRKC; LMRKAYLRKCK; MRKAYLRKCKE; RKAYLRKCKEF; KAYLRKCKEFH; AYLRKCKEFHP; YLRKCKEFHPD; LRKCKEFHPDK; RKCKEFHPDKG; KCKEFHPDKGG; CKEFHPDKGGD; KEFHPDKGGDE; EFHPDKGGDED; FHPDKGGDEDK; HPDKGGDEDKM; PDKGGDEDKMK; DKGGDEDKMKR; KGGDEDKMKRM; GGDEDKMKRMN; GDEDKMKRMNT; DEDKMKRMNTL; EDKMKRMNTLY; DKMKRMNTLYK; KMKRMNTLYKK; MKRMNTLYKKM; KRMNTLYKKME; RMNTLYKKMEQ; MNTLYKKMEQD; NTLYKKMEQDV; TLYKKMEQDVK; LYKKMEQDVKV; YKKMEQDVKVA; KKMEQDVKVAH; KMEQDVKVAHQ; MEQDVKVAHQP; EQDVKVAHQPD; QDVKVAHQPDF; DVKVAHQPDFG; VKVAHQPDFGT; KVAHQPDFGTW; VAHQPDFGTWS; AHQPDFGTWSS; HQPDFGTWSSS; QPDFGTWSSSE; PDFGTWSSSEV; DFGTWSSSEVC; FGTWSSSEVCA; GTWSSSEVCAD; TWSSSEVCADF; WSSSEVCADFP; SSSEVCADFPL; SSEVCADFPLC; SEVCADFPLCP; EVCADFPLCPD; VCADFPLCPDT; CADFPLCPDTL; ADFPLCPDTLY; DFPLCPDTLYC; FPLCPDTLYCK; PLCPDTLYCKE; LCPDTLYCKEW; CPDTLYCKEWP; PDTLYCKEWPI; DTLYCKEWPIC; TLYCKEWPICS; LYCKEWPICSK; YCKEWPICSKK; CKEWPICSKKP; KEWPICSKKPS; EWPICSKKPSV; WPICSKKPSVH; PICSKKPSVHC; ICSKKPSVHCP; CSKKPSVHCPC; SKKPSVHCPCM; KKPSVHCPCML; KPSVHCPCMLC; PSVHCPCMLCQ; SVHCPCMLCQL; VHCPCMLCQLR; HCPCMLCQLRL; CPCMLCQLRLR; PCMLCQLRLRH; CMLCQLRLRHL; MLCQLRLRHLN; LCQLRLRHLNR; CQLRLRHLNRK; QLRLRHLNRKF; LRLRHLNRKFL; RLRHLNRKFLR; LRHLNRKFLRK; RHLNRKFLRKE; HLNRKFLRKEP; LNRKFLRKEPL; NRKFLRKEPLV; RKFLRKEPLVW; KFLRKEPLVWI; FLRKEPLVWID; LRKEPLVWIDC; RKEPLVWIDCY; KEPLVWIDCYC; EPLVWIDCYCI; PLVWIDCYCID; LVWIDCYCIDC; VWIDCYCIDCF; WIDCYCIDCFT; IDCYCIDCFTQ; DCYCIDCFTQW; CYCIDCFTQWF; YCIDCFTQWFG; CIDCFTQWFGL; IDCFTQWFGLD; DCFTQWFGLDL; CFTQWFGLDLT; FTQWFGLDLTE; TQWFGLDLTEE; QWFGLDLTEET; WFGLDLTEETL; FGLDLTEETLQ; GLDLTEETLQW; LDLTEETLQWW; DLTEETLQWWV; LTEETLQWWVQ; TEETLQWWVQI; EETLQWWVQII; ETLQWWVQIIG; TLQWWVQIIGE; LQWWVQIIGET; QWWVQIIGETP; WWVQIIGETPF; WVQIIGETPFR; VQIIGETPFRD; QIIGETPFRDL; IIGETPFRDLK; IGETPFRDLKL; KALSNYFFYRC; ALSNYFFYRCQ; LSNYFFYRCQP; SNYFFYRCQPM; NYFFYRCQPME; YFFYRCQPMEQ; FFYRCQPMEQK; FYRCQPMEQKS; YRCQPMEQKSG; RCQPMEQKSGS; CQPMEQKSGSP; QPMEQKSGSPG; PMEQKSGSPGG; MEQKSGSPGGV; EQKSGSPGGVP; QKSGSPGGVPL; KSGSPGGVPLM; SGSPGGVPLMK; GSPGGVPLMKN; SPGGVPLMKNG; PGGVPLMKNGM; GGVPLMKNGMK; GVPLMKNGMKI; VPLMKNGMKIY; PLMKNGMKIYF; LMKNGMKIYFA; MKNGMKIYFAM; KNGMKIYFAMK; NGMKIYFAMKI; GMKIYFAMKIC; MKIYFAMKICL; KIYFAMKICLP; IYFAMKICLPV; YFAMKICLPVM; FAMKICLPVMK; AMKICLPVMKK; MKICLPVMKKQ; KICLPVMKKQQ; ICLPVMKKQQQ; CLPVMKKQQQI; LPVMKKQQQIL; PVMKKQQQILN; VMKKQQQILNT; MKKQQQILNTQ; KKQQQILNTQH; KQQQILNTQHH; QQQILNTQHHP; QQILNTQHHPK; QILNTQHHPKK; ILNTQHHPKKK; LNTQHHPKKKE; NTQHHPKKKER; KTLKTFPLIYT; TLKTFPLIYTS; LKTFPLIYTSF; KTFPLIYTSFL; TFPLIYTSFLV; FPLIYTSFLVK; PLIYTSFLVKL; LIYTSFLVKLY; IYTSFLVKLYL; YTSFLVKLYLV; TSFLVKLYLVI; SFLVKLYLVIE; FLVKLYLVIEP; LVKLYLVIEPL; VKLYLVIEPLP; KLYLVIEPLPA; LYLVIEPLPAL; YLVIEPLPALL; LVIEPLPALLC; VIEPLPALLCI; IEPLPALLCIL; EPLPALLCILL; PLPALLCILLK; LPALLCILLKK; PALLCILLKKK; ALLCILLKKKL; LLCILLKKKLK; LCILLKKKLKF; CILLKKKLKFC; ILLKKKLKFCI; LLKKKLKFCIK; LKKKLKFCIKN; KKKLKFCIKNL; KKLKFCIKNLW; KLKFCIKNLWK; LKFCIKNLWKN; KFCIKNLWKNI; FCIKNLWKNIL; LLLVDTCVLGI; LLVDTCVLGII; LVDTCVLGIIL; VDTCVLGIILY; DTCVLGIILYS; TCVLGIILYSF; LHIDIEFLQLI; HIDIEFLQLII; IDIEFLQLIIS; DIEFLQLIISV; IEFLQLIISVK; EFLQLIISVKS; FLQLIISVKSC; LQLIISVKSCV; QLIISVKSCVP; LIISVKSCVPL; IISVKSCVPLV; ISVKSCVPLVF; FVRVLIRNTYY; VRVLIRNTYYI; RVLIRNTYYIV; VLIRNTYYIVP; RSMILAQKSLK; SMILAQKSLKK; MILAQKSLKKQ; ILAQKSLKKQS; LAQKSLKKQSR; AQKSLKKQSRC; QKSLKKQSRCL; KSLKKQSRCLG; SLKKQSRCLGN; RSVKSVRKKTS; SVKSVRKKTSL; VKSVRKKTSLI; KSVRKKTSLIT; SVRKKTSLITL; VRKKTSLITLS; RKKTSLITLSI; KKTSLITLSIM; KTSLITLSIMK; TSLITLSIMKS; SLITLSIMKST; LITLSIMKSTL; ITLSIMKSTLQ; TLSIMKSTLQM; LSIMKSTLQML; SIMKSTLQMLL; IMKSTLQMLLF; MKSTLQMLLFL; KSTLQMLLFLQ; STLQMLLFLQK; TLQMLLFLQKV; LQMLLFLQKVK; QMLLFLQKVKI; MLLFLQKVKIK; LLFLQKVKIKK; LFLQKVKIKKV; FLQKVKIKKVF; LQKVKIKKVFV; QKVKIKKVFVS; KVKIKKVFVSK; VKIKKVFVSKQ; NNIWQVLLGCT; NIWQVLLGCTV; IWQVLLGCTVC; WQVLLGCTVCY; QVLLGCTVCYL; VLLGCTVCYLK; LLGCTVCYLKW; LGCTVCYLKWI; GCTVCYLKWIL; YLIFCTVLFSM; LIFCTVLFSMY; IFCTVLFSMYL; FCTVLFSMYLK; CTVLFSMYLKE; TVLFSMYLKED; VLFSMYLKEDT; LFSMYLKEDTG; FSMYLKEDTGY; SMYLKEDTGYL; MYLKEDTGYLK; YLKEDTGYLKV; LKEDTGYLKVP; KEDTGYLKVPL; EDTGYLKVPLI; DTGYLKVPLIV; TGYLKVPLIVE; GYLKVPLIVEK; YLKVPLIVEKQ; LKVPLIVEKQH; KGQELNQRICL; GQELNQRICLQ; QELNQRICLQD; ELNQRICLQDM; LNQRICLQDME; TKEPKYFHQAW; KEPKYFHQAWL; EPKYFHQAWLQ; MSILSLKPCKL; SILSLKPCKLD; ILSLKPCKLDL; ENPYKTQSSYL; NPYKTQSSYLK; PYKTQSSYLKK; YKTQSSYLKKE; KTQSSYLKKEF; TQSSYLKKEFY; QSSYLKKEFYK; SSYLKKEFYKV; SYLKKEFYKVE; LILQLIYNLEL; ILQLIYNLELL; LQLIYNLELLN; QLIYNLELLNG; LIYNLELLNGR; IYNLELLNGRK; YNLELLNGRKG; NLELLNGRKGW; LELLNGRKGWI; ELLNGRKGWIL; LLNGRKGWILR; NIIYAWGNVFL; IIYAWGNVFLI; IYAWGNVFLIL; YAWGNVFLILQ; AWGNVFLILQE; WGNVFLILQEK; GNVFLILQEKR; NVFLILQEKRI; VFLILQEKRIQ; FLILQEKRIQK; LILQEKRIQKL; ILQEKRIQKLK; LQEKRIQKLKT; QEKRIQKLKTL; EKRIQKLKTLD; KRIQKLKTLDM; RIQKLKTLDMD; IQKLKTLDMDQ; QKLKTLDMDQA; KLKTLDMDQAL; LKTLDMDQALN; KTLDMDQALNP; TLDMDQALNPN; LDMDQALNPNH; DMDQALNPNHN; MDQALNPNHNA; DQALNPNHNAL; QALNPNHNALP; ALNPNHNALPK; LNPNHNALPKS; NPNHNALPKSQ; PNHNALPKSQI; NHNALPKSQIL; HNALPKSQILQ; NALPKSQILQP; ALPKSQILQPL; LPKSQILQPLL; PKSQILQPLLK; KSQILQPLLKI; SQILQPLLKIP; QILQPLLKIPK; ILQPLLKIPKG; LQPLLKIPKGQ; QPLLKIPKGQT; PLLKIPKGQTP; LLKIPKGQTPI; LKIPKGQTPIV; KIPKGQTPIVK; IPKGQTPIVKS; PKGQTPIVKSC; KGQTPIVKSCI; GQTPIVKSCIC; QTPIVKSCICV; TPIVKSCICVK; PIVKSCICVKA; IVKSCICVKAF; VKSCICVKAFS; KSCICVKAFSV; SCICVKAFSVL; CICVKAFSVLK; ICVKAFSVLKG; CVKAFSVLKGL; VKAFSVLKGLK; KAFSVLKGLKH; AFSVLKGLKHH; FSVLKGLKHHP; SVLKGLKHHPQ; VLKGLKHHPQN; LKGLKHHPQNN; KGLKHHPQNNT; GLKHHPQNNTS; LKHHPQNNTSL; KHHPQNNTSLK; HHPQNNTSLKV; HPQNNTSLKVA; PQNNTSLKVAY; QNNTSLKVAYT; NNTSLKVAYTK; NTSLKVAYTKA; TSLKVAYTKAA; SLKVAYTKAAF; LKVAYTKAAFI; KVAYTKAAFIK; VAYTKAAFIKC; AYTKAAFIKCI; YTKAAFIKCIC; TKAAFIKCICT; KAAFIKCICTI; AAFIKCICTIK; AFIKCICTIKA; FIKCICTIKAP; IKCICTIKAPV; SILVCNCPCLS; ILVCNCPCLSI; LVCNCPCLSIY; VCNCPCLSIYL; CNCPCLSIYLI; NCPCLSIYLII; CPCLSIYLIIS; PCLSIYLIISG; CLSIYLIISGS; LSIYLIISGSP; SIYLIISGSPG; IYLIISGSPGS; YLIISGSPGSL; LIISGSPGSLS; IISGSPGSLSV; ISGSPGSLSVP; SGSPGSLSVPS; GSPGSLSVPSN; SPGSLSVPSNT; PGSLSVPSNTL; GSLSVPSNTLT; SLSVPSNTLTS; LSVPSNTLTSS; SVPSNTLTSST; VPSNTLTSSTW; PSNTLTSSTWD; SNTLTSSTWDS; NTLTSSTWDSI; TLTSSTWDSIP; LTSSTWDSIPY; TSSTWDSIPYI; SSTWDSIPYIG; STWDSIPYIGC; TWDSIPYIGCP; WDSIPYIGCPS; DSIPYIGCPST; SIPYIGCPSTL; IPYIGCPSTLW; PYIGCPSTLWV; YIGCPSTLWVL; IGCPSTLWVLL; GCPSTLWVLLF; CPSTLWVLLFI; PSTLWVLLFIR; STLWVLLFIRS; TLWVLLFIRSL; LWVLLFIRSLS; WVLLFIRSLSK; VLLFIRSLSKK; LLFIRSLSKKE; LFIRSLSKKEI; FIRSLSKKEIG; GFFTDLFLRRI; FFTDLFLRRIL; FTDLFLRRILK; TDLFLRRILKY; DLFLRRILKYL; LFLRRILKYLA; FLRRILKYLAR; LRRILKYLARP; RRILKYLARPL; RILKYLARPLH; ILKYLARPLHC; LKYLARPLHCC; KYLARPLHCCV; YLARPLHCCVP; LARPLHCCVPE; ARPLHCCVPEL; RPLHCCVPELL; PLHCCVPELLV; LHCCVPELLVN; HCCVPELLVNR; CCVPELLVNRP; CVPELLVNRPQ; VPELLVNRPQI; PELLVNRPQIS; ELLVNRPQISA; LLVNRPQISAA; LVNRPQISAAE; VNRPQISAAET; NRPQISAAETY; RPQISAAETYR; PQISAAETYRL; QISAAETYRLS; ISAAETYRLSA; SAAETYRLSAL; AAETYRLSALQ; AETYRLSALQR; ETYRLSALQRG; TYRLSALQRGP; YRLSALQRGPT; RLSALQRGPTP; LSALQRGPTPC; SALQRGPTPCS; ALQRGPTPCSS; LQRGPTPCSSS; QRGPTPCSSSN; RGPTPCSSSNT; GPTPCSSSNTV; PTPCSSSNTVV; TPCSSSNTVVA; PCSSSNTVVAV; CSSSNTVVAVL; SSSNTVVAVLV; SSNTVVAVLVT; STGGTFSPPVK; TGGTFSPPVKV; GGTFSPPVKVP; GTFSPPVKVPK; TFSPPVKVPKY; FSPPVKVPKYL; SPPVKVPKYLA; PPVKVPKYLAF; PVKVPKYLAFS; VKVPKYLAFSF; KVPKYLAFSFL; VPKYLAFSFLL; PKYLAFSFLLG; KYLAFSFLLGS; YLAFSFLLGSG; LAFSFLLGSGT; AFSFLLGSGTQ; FSFLLGSGTQH; SFLLGSGTQHS; FLLGSGTQHST; LLGSGTQHSTG; ALWSVFITWDW; LWSVFITWDWA; WSVFITWDWAV; SVFITWDWAVG; VFITWDWAVGF; FITWDWAVGFL; ITWDWAVGFLG; TWDWAVGFLGV; WDWAVGFLGVI; DWAVGFLGVIV; WAVGFLGVIVP; AVGFLGVIVPS; VGFLGVIVPSG; GFLGVIVPSGY; FLGVIVPSGYF; LGVIVPSGYFD; GVIVPSGYFDL; FISTPCISKGS; ISTPCISKGSP; STPCISKGSPP; TPCISKGSPPT; PCISKGSPPTA; CISKGSPPTAK; ISKGSPPTAKK; SKGSPPTAKKW; KGSPPTAKKWK; GSPPTAKKWKL; SPPTAKKWKLL; PPTAKKWKLLP; IGFPPPCSCTF; GFPPPCSCTFC; FPPPCSCTFCD; PPPCSCTFCDP; PPCSCTFCDPA; RLSMLVIPITS; LSMLVIPITSV; SMLVIPITSVC; MLVIPITSVCT; LVIPITSVCTV; VIPITSVCTVT; IPITSVCTVTA; PITSVCTVTAS; ITSVCTVTASH; TSVCTVTASHI; SVCTVTASHIS; VCTVTASHISR; CTVTASHISRF; TVTASHISRFP; VTASHISRFPQ; TASHISRFPQV; ASHISRFPQVR; SHISRFPQVRS; HISRFPQVRSS; ISRFPQVRSSF; SRFPQVRSSFK; RFPQVRSSFKL; FPQVRSSFKLG; PQVRSSFKLGR; QVRSSFKLGRG; VRSSFKLGRGI; RSSFKLGRGIL; SSFKLGRGILA; SFKLGRGILAV; FKLGRGILAVL; QGSIFLSGLSL; GSIFLSGLSLL; SIFLSGLSLLK; IFLSGLSLLKS; FLSGLSLLKSF; LSGLSLLKSFS; SGLSLLKSFSA; GLSLLKSFSAL; LSLLKSFSALS; SLLKSFSALSF; LLKSFSALSFR; LKSFSALSFRL; KSFSALSFRLK; SFSALSFRLKP; FSALSFRLKPL; SALSFRLKPLR; ALSFRLKPLRF; LSFRLKPLRFS; SFRLKPLRFSS; FRLKPLRFSSG; RLKPLRFSSGS; LKPLRFSSGSP; KPLRFSSGSPI; PLRFSSGSPIS; LRFSSGSPISG; RFSSGSPISGF; FSSGSPISGFR; SSGSPISGFRK; SGSPISGFRKH; GSPISGFRKHS; SPISGFRKHST; PISGFRKHSTS; ISGFRKHSTSV; SGFRKHSTSVI; GFRKHSTSVIA; FRKHSTSVIAS; RKHSTSVIAST; KHSTSVIASTP; HSTSVIASTPV; STSVIASTPVL; TSVIASTPVLT; SVIASTPVLTS; VIASTPVLTSR; IASTPVLTSRT; ASTPVLTSRTS; STPVLTSRTST; TPVLTSRTSTP; PVLTSRTSTPP; VLTSRTSTPPF; LTSRTSTPPFI; TSRTSTPPFIS; SRTSTPPFISS; RTSTPPFISSF; TSTPPFISSFG; STPPFISSFGT; TPPFISSFGTC; PPFISSFGTCT; PFISSFGTCTG; FISSFGTCTGS; ISSFGTCTGSF; SSFGTCTGSFG; SFGTCTGSFGF; FGTCTGSFGFL; GTCTGSFGFLG; TCTGSFGFLGA; CTGSFGFLGAA; TGSFGFLGAAP; GSFGFLGAAPG; SFGFLGAAPGH; FGFLGAAPGHS; GFLGAAPGHSP; FLGAAPGHSPF; LGAAPGHSPFL; GAAPGHSPFLL; AAPGHSPFLLV; APGHSPFLLVG; PGHSPFLLVGA; GHSPFLLVGAI; HSPFLLVGAIF; SPFLLVGAIFI; PFLLVGAIFIC; FLLVGAIFICF; LLVGAIFICFK; LVGAIFICFKS; VGAIFICFKSR; GAIFICFKSRC; AIFICFKSRCY; IFICFKSRCYS; FICFKSRCYSP; ICFKSRCYSPV; CFKSRCYSPVQ; FKSRCYSPVQA; RQHPLRSSSLI; QHPLRSSSLIS; HPLRSSSLIST; PLRSSSLISTS; LRSSSLISTSW; RSSSLISTSWG; SSSLISTSWGN; SSLISTSWGNS; SLISTSWGNSF; LISTSWGNSFF; ISTSWGNSFFY; STSWGNSFFYK; TSWGNSFFYKL; SWGNSFFYKLS; VHSLCNFFYTV; HSLCNFFYTVS; SLCNFFYTVSI; LCNFFYTVSII; CNFFYTVSIIY; NFFYTVSIIYT; FFYTVSIIYTI; FYTVSIIYTIS; YTVSIIYTISM; TVSIIYTISMA; VSIIYTISMAK; SIIYTISMAKM; IIYTISMAKMY; IYTISMAKMYT; YTISMAKMYTG; TISMAKMYTGT; ISMAKMYTGTF; SMAKMYTGTFP; MAKMYTGTFPF; AKMYTGTFPFS; KMYTGTFPFSY; MYTGTFPFSYL; YTGTFPFSYLS; TGTFPFSYLSN; GTFPFSYLSNH; GPNRGKIRIIL; PNRGKIRIILL; NRGKIRIILLN; RGKIRIILLNI; GKIRIILLNII; KIRIILLNIII; IRIILLNIIIK; RIILLNIIIKV; IILLNIIIKVY; ILLNIIIKVYR; LLNIIIKVYRG; LNIIIKVYRGI; NIIIKVYRGIY; IIIKVYRGIYN; IIKVYRGIYNC; IKVYRGIYNCP; KVYRGIYNCPG; VYRGIYNCPGS; YRGIYNCPGSF; RGIYNCPGSFL; GIYNCPGSFLQ; IYNCPGSFLQK; YNCPGSFLQKS; NCPGSFLQKSS; CPGSFLQKSSQ; PGSFLQKSSQG; GSFLQKSSQGV; SFLQKSSQGVS; FLQKSSQGVSK; LQKSSQGVSKK; QKSSQGVSKKS; KSSQGVSKKSF; SSQGVSKKSFC; SQGVSKKSFCS; QGVSKKSFCSS; GVSKKSFCSSL; VSKKSFCSSLQ; SKKSFCSSLQF; KKSFCSSLQFL; GYRRYIIPNNM; YRRYIIPNNMP; RRYIIPNNMPQ; RYIIPNNMPQS; YIIPNNMPQSL; IIPNNMPQSLG; IPNNMPQSLGN; PNNMPQSLGNS; NNMPQSLGNSS; NMPQSLGNSSK; MPQSLGNSSKQ; PQSLGNSSKQR; QSLGNSSKQRR; SLGNSSKQRRT; LGNSSKQRRTP; GNSSKQRRTPM; NSSKQRRTPMP; SSKQRRTPMPR; SKQRRTPMPRI; KQRRTPMPRIK; QRRTPMPRIKV; RRTPMPRIKVL; RTPMPRIKVLN; TPMPRIKVLNI; PMPRIKVLNII; MPRIKVLNIIN; PRIKVLNIINK; RIKVLNIINKS; IKVLNIINKSI; KVLNIINKSIY; VLNIINKSIYT; LNIINKSIYTR; NIINKSIYTRK; IINKSIYTRKQ; INKSIYTRKQN; NKSIYTRKQNI; KSIYTRKQNII; SIYTRKQNIIV; IYTRKQNIIVL; YTRKQNIIVLI; TRKQNIIVLIW; RKQNIIVLIWV; KQNIIVLIWVK; QNIIVLIWVKQ; NIIVLIWVKQF; IIVLIWVKQFQ; IVLIWVKQFQS; VLIWVKQFQSH; LIWVKQFQSHA; LLIEAYSGNFV; LIEAYSGNFVI; IEAYSGNFVIP; EAYSGNFVIPI; AYSGNFVIPII; YSGNFVIPIIK; SGNFVIPIIKE; GNFVIPIIKEL; NFVIPIIKELI; FVIPIIKELIP; VIPIIKELIPY; IPIIKELIPYL; PIIKELIPYLS; SSKPSNSPRST; SKPSNSPRSTS; KPSNSPRSTSN; PSNSPRSTSNY; SNSPRSTSNYS; NSPRSTSNYSI; SPRSTSNYSIC; PRSTSNYSICL; RSTSNYSICLR; STSNYSICLRS; GTCYALYSSKG; TCYALYSSKGC; CYALYSSKGCN; YALYSSKGCNL; ALYSSKGCNLN; LYSSKGCNLNF; YSSKGCNLNFY; SSKGCNLNFYS; SKGCNLNFYSS; KGCNLNFYSSS; GCNLNFYSSSS; CNLNFYSSSSL; NLNFYSSSSLP; LNFYSSSSLPS; NFYSSSSLPSS; FYSSSSLPSSN; YSSSSLPSSNF; SSSSLPSSNFS; SSSLPSSNFSH; KSCGSSSLRYT; SCGSSSLRYTG; CGSSSLRYTGN; SSTHEPGNTKK; STHEPGNTKKK; THEPGNTKKKG; HEPGNTKKKGL; EPGNTKKKGLL; PGNTKKKGLLT; ESFTESFTAGK; SFTESFTAGKA; FTESFTAGKAV; TESFTAGKAVV; ESFTAGKAVVL; SFTAGKAVVLL; FTAGKAVVLLF; TAGKAVVLLFF; AGKAVVLLFFP; GKAVVLLFFPS; KAVVLLFFPST; AVVLLFFPSTL; VVLLFFPSTLS; VLLFFPSTLSS; LLFFPSTLSSP; LFFPSTLSSPL; FFPSTLSSPLQ; FPSTLSSPLQN; PSTLSSPLQNS; STLSSPLQNSS; TLSSPLQNSSK; LSSPLQNSSKS; SSPLQNSSKSS; SPLQNSSKSSK; PLQNSSKSSKI; LQNSSKSSKIK; QNSSKSSKIKI; NSSKSSKIKIK; SSKSSKIKIKI; SKSSKIKIKIL; ALFFVPVQVLP; LFFVPVQVLPT; FFVPVQVLPTF; FVPVQVLPTFT; VPVQVLPTFTE; PVQVLPTFTEA; VQVLPTFTEAC; QVLPTFTEACR; VLPTFTEACRD; LPTFTEACRDS; PTFTEACRDSW; TFTEACRDSWR; FTEACRDSWRR; TEACRDSWRRT; EACRDSWRRTM; ACRDSWRRTMA; CRDSWRRTMAF; RDSWRRTMAFV; DSWRRTMAFVQ; SWRRTMAFVQF; WRRTMAFVQFN; RRTMAFVQFNW; RTMAFVQFNWG; TMAFVQFNWGQ; MAFVQFNWGQG; AFVQFNWGQGQ; FVQFNWGQGQD; VQFNWGQGQDS; ARKTCLSCTFL; RKTCLSCTFLP; KTCLSCTFLPE; TCLSCTFLPEV; CLSCTFLPEVM; LSCTFLPEVMV; SCTFLPEVMVW; CTFLPEVMVWL; TFLPEVMVWLH; FLPEVMVWLHS; LPEVMVWLHSM; PEVMVWLHSMG; EVMVWLHSMGK; VMVWLHSMGKQ; MVWLHSMGKQL; VWLHSMGKQLL; WLHSMGKQLLP; LHSMGKQLLPV; HSMGKQLLPVS; SMGKQLLPVSH; MGKQLLPVSHA; GKQLLPVSHAL; KQLLPVSHALS; QLLPVSHALSF; LLPVSHALSFL; LPVSHALSFLR; PVSHALSFLRS; VSHALSFLRSW; SHALSFLRSWF; HALSFLRSWFG; ALSFLRSWFGC; LSFLRSWFGCI; SFLRSWFGCIP; FLRSWFGCIPL; AAPPCGLFFYN; APPCGLFFYNI; EAEAASASTLS; AEAASASTLSL; EAASASTLSLK; GLAKLFGEIPI; LAKLFGEIPIL; AKLFGEIPILL; KLFGEIPILLQ; LFGEIPILLQF; FGEIPILLQFL; GEIPILLQFLQ BK virus complementary reading frame 2 8 mers: WIKFLTGK; IKFLTGKN; KFLTGKNP; FLTGKNPW; LTGKNPWS; TGKNPWSS; GKNPWSSW; KNPWSSWT; NPWSSWTF; ALKELPGE; LKELPGEI; KELPGEIF; ELPGEIFP; GSVRNFTL; SVRNFTLT; VRNFTLTK; RNFTLTKG; NFTLTKGA; FTLTKGAT; TLTKGATR; LTKGATRI; TKGATRIK; ILCIKKWS; LCIKKWSR; CIKKWSRM; LISLILEP; ISLILEPG; SLILEPGV; LILEPGVA; ILEPGVAQ; LEPGVAQR; EPGVAQRF; PGVAQRFV; GVAQRFVL; VAQRFVLI; AQRFVLIF; QRFVLIFL; RFVLIFLF; FVLIFLFA; VLIFLFAQ; LIFLFAQI; IFLFAQIP; FLFAQIPC; LFAQIPCT; FAQIPCTA; AQIPCTAR; QIPCTARN; IPCTARNG; PCTARNGL; CTARNGLF; TARNGLFV; ARNGLFVP; RNGLFVPK; NGLFVPKS; GLFVPKSL; LFVPKSLL; FVPKSLLC; VPKSLLCT; PKSLLCTA; KSLLCTAL; SLLCTALA; LLCTALAC; LCTALACY; CTALACYV; TALACYVS; ALACYVSL; LACYVSLD; IATALTAS; ATALTASH; TALTASHS; ALTASHSG; LTASHSGL; TASHSGLA; LKKLCNGG; KKLCNGGS; KLCNGGSK; LEKLPSEI; SFKVTNLY; FKVTNLYL; KVTNLYLD; VTNLYLDK; VIIFFIGA; IIFFIGAN; IFFIGANL; FFIGANLW; FIGANLWN; IGANLWNR; GANLWNRR; ANLWNRRV; NLWNRRVG; LWNRRVGV; WNRRVGVL; NRRVGVLV; RRVGVLVE; RVGVLVEF; VGVLVEFL; RSNSRFST; SNSRFSTL; NSRFSTLN; SRFSTLNT; RFSTLNTT; FSTLNTTQ; STLNTTQK; TLNTTQKK; LNTTQKKK; NTTQKKKK; TTQKKKKG; TQKKKKGR; QKKKKGRR; KKKKGRRP; NPCLLCCV; PCLLCCVY; CLLCCVYY; KTYGKIFC; TYGKIFCN; YGKIFCNF; GKIFCNFY; YYILFNST; FLSKAVYL; RSIPYYRR; SIPYYRRK; IPYYRRKH; PYYRRKHS; YYRRKHSR; YRRKHSRG; RRKHSRGL; RKHSRGLK; KHSRGLKG; HSRGLKGA; RNKAGVLE; NKAGVLEI; KAGVLEIN; AGVLEINY; GCVFIIRY; CVFIIRYV; VFIIRYVF; FIIRYVFR; IIRYVFRI; IRYVFRIS; RYVFRISI; YVFRISIQ; VFRISIQC; FRISIQCR; RISIQCRG; ISIQCRGV; KVSEKRPA; VSEKRPAL; SEKRPALS; EKRPALSL; KALCKCYY; ALCKCYYF; LCKCYYFC; CKCYYFCR; KCYYFCRK; KSKKYLSA; SKKYLSAS; KKYLSASS; KYLSASSR; YLSASSRY; LSASSRYS; SASSRYSF; ASSRYSFS; KKSRYPSY; KSRYPSYD; SRYPSYDQ; RYPSYDQG; YPSYDQGR; PSYDQGRN; SYDQGRNA; YDQGRNAN; DQGRNANR; QGRNANRK; GRNANRKI; RNANRKIQ; NANRKIQS; ANRKIQSY; NRKIQSYI; RKIQSYIR; NGFNIWSS; GFNIWSSW; FNIWSSWK; NIWSSWKC; IWSSWKCC; WSSWKCCT; SSWKCCTR; SWKCCTRT; WKCCTRTI; KCCTRTIY; CCTRTIYG; CTRTIYGR; TRTIYGRC; RTIYGRCC; TIYGRCCL; IYGRCCLA; YGRCCLAA; GRCCLAAL; RCCLAALF; CCLAALFA; CLAALFAT; FFALYCFQ; FALYCFQC; ALYCFQCT; WKNNTSCR; KNNTSCRV; NNTSCRVI; NTSCRVIR; TSCRVIRF; SCRVIRFV; CRVIRFVW; RVIRFVWW; SLKCKPTH; LKCKPTHG; KCKPTHGK; CKPTHGKA; KPTHGKAN; PTHGKANL; ARCSYRSV; RCSYRSVH; CSYRSVHG; SYRSVHGC; YRSVHGCF; IKGFAFRT; KGFAFRTW; GFAFRTWN; FAFRTWNK; AFRTWNKQ; FRTWNKQF; RTWNKQFR; TWNKQFRQ; WNKQFRQF; NKQFRQFE; KQFRQFER; QFRQFERL; FRQFERLF; RQFERLFR; QFERLFRW; FERLFRWK; ERLFRWKC; GKFRKETF; KFRKETFK; FRKETFKQ; RKETFKQK; KETFKQKN; ETFKQKNP; TFKQKNPN; FKQKNPNI; KQKNPNIS; QKNPNIST; KNPNISTR; NPNISTRL; PNISTRLG; NISTRLGY; ISTRLGYN; STRLGYNE; AQNIFKKI; QNIFKKIL; NIFKKILT; IFKKILTK; FKKILTKL; KKILTKLR; KILTKLRV; ILTKLRVL; LTKLRVLT; KKNFTKWN; KNFTKWND; NFTKWNDL; FTKWNDLV; TKWNDLVA; KWNDLVAT; WNDLVATA; NDLVATAN; DLVATANL; LVATANLV; DKYVYFFK; KYVYFFKD; YVYFFKDE; VYFFKDEI; YMHGEMYS; YYKRRGFR; YKRRGFRN; RLWTWIKH; IPITMLFP; PITMLFPS; ITMLFPSL; TMLFPSLR; MLFPSLRY; LFPSLRYF; FPSLRYFS; PSLRYFSP; SLRYFSPC; RFPKVRPP; NTTPKITQ; TTPKITQA; KWLIQKQH; WLIQKQHL; LIQKQHLL; IQKQHLLN; QKQHLLNV; KQHLLNVY; QHLLNVYV; HLLNVYVQ; KHLFKAFW; HLFKAFWF; LFKAFWFA; FKAFWFAI; KAFWFAIV; AFWFAIVP; FWFAIVPV; WFAIVPVC; FAIVPVCQ; AIVPVCQY; IVPVCQYI; VPVCQYIL; PVCQYILS; VCQYILSY; CQYILSYL; QYILSYLG; YILSYLGP; ILSYLGPL; LSYLGPLE; SYLGPLEV; YLGPLEVF; LGPLEVFL; GPLEVFLC; PLEVFLCH; LEVFLCHQ; EVFLCHQT; VFLCHQTP; PLLPGIPY; LLPGIPYH; LPGIPYHT; AAHPLSGF; AHPLSGFS; HPLSGFSC; PLSGFSCL; GHLAKRKL; HLAKRKLG; LAKRKLGK; AKRKLGKD; KRKLGKDS; RKLGKDSL; KLGKDSLQ; LGKDSLQI; GKDSLQIF; KDSLQIFF; DSLQIFFS; SLQIFFSG; LQIFFSGG; QIFFSGGS; NILQGLST; ILQGLSTV; LQGLSTVV; QGLSTVVF; GLSTVVFQ; LSTVVFQS; STVVFQSC; TGHKYQQL; GHKYQQLK; HKYQQLKH; KYQQLKHT; YQQLKHTG; QQLKHTGY; QLKHTGYQ; LKHTGYQL; KHTGYQLY; HTGYQLYK; TGYQLYKE; GYQLYKEA; YQLYKEAP; QLYKEAPH; LYKEAPHP; YKEAPHPV; KEAPHPVH; EAPHPVHL; APHPVHLA; PHPVHLAT; HPVHLATL; PVHLATLW; LCWSHEVL; CWSHEVLG; WSHEVLGE; SHEVLGEH; HEVLGEHF; EVLGEHFP; VLGEHFPL; LGEHFPLL; HFHFYWDQ; FHFYWDQV; HFYWDQVP; FYWDQVPS; YWDQVPST; WDQVPSTQ; DQVPSTQL; QVPSTQLD; VPSTQLDK; PSTQLDKH; STQLDKHC; TQLDKHCF; QLDKHCFC; LDKHCFCP; DKHCFCPN; KHCFCPNR; HCFCPNRP; CFCPNRPY; FCPNRPYG; CPNRPYGQ; PNRPYGQY; NRPYGQYS; RPYGQYSL; PYGQYSLP; YGQYSLPG; GQYSLPGT; QYSLPGTG; YSLPGTGL; SLPGTGLL; LPGTGLLG; PGTGLLGF; YHQGTLTC; HQGTLTCN; QGTLTCNS; GTLTCNSL; TLTCNSLA; LTCNSLAL; TCNSLALP; CNSLALPA; NSLALPAF; SLALPAFP; LALPAFPR; ALPAFPRV; LPAFPRVL; PAFPRVLH; AFPRVLHL; FPRVLHLQ; PRVLHLQQ; RVLHLQQR; VLHLQQRS; LHLQQRSG; HLQQRSGN; LQQRSGNY; QQRSGNYC; QRSGNYCL; RSGNYCLE; VFLHHAHA; FLHHAHAL; LHHAHALF; HHAHALFV; HAHALFVT; AHALFVTL; HALFVTLH; ALFVTLHE; LFVTLHEG; PLFVQLQP; LFVQLQPP; FVQLQPPT; VQLQPPTS; QLQPPTSV; LQPPTSVD; QPPTSVDF; PPTSVDFH; PTSVDFHR; TSVDFHRL; SVDFHRLG; VDFHRLGP; DFHRLGPH; FHRLGPHL; HRLGPHLN; RLGPHLNW; LGPHLNWG; GPHLNWGG; PHLNWGGE; HLNWGGEF; LNWGGEFL; NWGGEFLL; WGGEFLLC; GGEFLLCC; GEFLLCCN; EFLLCCNR; FLLCCNRE; LLCCNREA; LCCNREAF; CCNREAFF; CNREAFFS; NREAFFSL; REAFFSLG; EAFFSLGY; AFFSLGYH; FFSLGYHC; SHFQHLAL; HFQHLALD; GFHLDPPF; FHLDPPFL; HLDPPFLG; LDPPFLGL; DPPFLGLG; PPFLGLGS; PFLGLGSI; FLGLGSIL; LGLGSILP; GLGSILPL; LLELLLLL; LELLLLLL; ELLLLLLL; LLLLLLLV; LLLLLLVV; LLLLLVVL; LLLLVVLA; LLLVVLAL; LLVVLALA; LVVLALAR; VVLALARV; VLALARVP; LALARVPL; ALARVPLA; LARVPLAF; ARVPLAFW; RVPLAFWE; VPLAFWEL; PLAFWELP; LAFWELPL; AFWELPLD; FWELPLDT; WELPLDTL; ELPLDTLL; LPLDTLLF; PLDTLLFF; LDTLLFFW; DTLLFFWL; TLLFFWLG; LLFFWLGP; LFFWLGPS; FFWLGPSS; FWLGPSSY; WLGPSSYA; LGPSSYAS; GPSSYASR; PSSYASRA; SSYASRAG; SYASRAGV; YASRAGVT; ASRAGVTV; SRAGVTVP; RAGVTVPY; AGVTVPYR; GVTVPYRP; VTVPYRPR; TVPYRPRS; VPYRPRSK; PYRPRSKG; YRPRSKGN; RPRSKGNI; PRSKGNIH; LAPPGAIV; APPGAIVF; PPGAIVFS; PGAIVFSI; GAIVFSIN; AIVFSINS; IVFSINSP; VFSINSPE; FSINSPEC; SINSPECT; INSPECTL; NSPECTLC; FLKSILCV; LKSILCVT; KSILCVTS; SILCVTSS; ILCVTSSI; LCVTSSIL; CVTSSILS; VTSSILSA; TSSILSAS; SSILSASS; SILSASSI; ILSASSIL; VWPKCTRV; WPKCTRVP; PKCTRVPS; KCTRVPSL; CTRVPSLS; TRVPSLSA; RVPSLSAT; VPSLSATC; PSLSATCL; SLSATCLT; LSATCLTI; SATCLTIE; ATCLTIEG; TCLTIEGL; CLTIEGLI; LTIEGLIG; TIEGLIGE; IEGLIGER; EGLIGERS; GLIGERSE; KFIGAFTI; FIGAFTIV; IGAFTIVQ; GAFTIVQV; AFTIVQVV; FTIVQVVS; TIVQVVSS; IVQVVSSK; VQVVSSKN; QVVSSKNL; VVSSKNLA; VSSKNLAK; SSKNLAKE; SKNLAKES; KNLAKESL; NLAKESLK; LAKESLKN; AKESLKNL; KESLKNLS; ESLKNLSV; SLKNLSVL; LKNLSVLL; KNLSVLLC; NLSVLLCN; LSVLLCNS; SVLLCNSC; VLLCNSCE; LLCNSCEV; LCNSCEVI; CNSCEVIE; NSCEVIEG; SCEVIEGI; CEVIEGIS; EVIEGISS; VIEGISSL; IEGISSLI; EGISSLIT; GISSLITC; ISSLITCH; SSLITCHK; SLITCHKA; LITCHKAW; ITCHKAWE; TCHKAWEI; CHKAWEIV; HKAWEIVA; KAWEIVAN; AWEIVANK; WEIVANKE; EIVANKEG; IVANKEGP; VANKEGPQ; ANKEGPQC; NKEGPQCL; KEGPQCLG; EGPQCLGS; GPQCLGSR; PQCLGSRY; ILLTKVFT; LLTKVFTP; LTKVFTPG; TKVFTPGN; KVFTPGNR; VFTPGNRI; FTPGNRIS; YSSGLNNS; SSGLNNSK; SGLNNSKA; GLNNSKAM; LNNSKAMP; NNSKAMPD; NSKAMPDC; SQSSKNLY; QSSKNLYP; SSKNLYPT; AKELIPLT; KELIPLTV; IKAANPAI; KAANPAIA; AANPAIAP; ANPAIAPG; NPAIAPGA; PAIAPGAP; AIAPGAPA; IAPGAPAI; APGAPAIT; PGAPAITA; GAPAITAY; APAITAYV; GVRPIAAI; VRPIAAIA; RPIAAIAS; PIAAIASE; IAAIASEV; AAIASEVL; AIASEVLV; IASEVLVM; ASEVLVMP; SEVLVMPS; EVLVMPST; VLVMPSTV; LVMPSTVA; VMPSTVAR; MPSTVARD; PSTVARDA; STVARDAI; TSIAAAAS; SIAAAASP; IAAAASPA; AAAASPAA; AAASPAAI; AASPAAIS; ASPAAISA; SPAAISAT; PAAISATE; AAISATEN; AISATENP; ISATENPV; SATENPVA; ATENPVAA; TENPVAAA; ENPVAAAA; NPVAAAAS; PVAAAASD; VAAAASDT; AAAASDTL; AAASDTLA; AASDTLAT; ASDTLATR; SDTLATRS; DTLATRSP; TLATRSPK; LATRSPKS; ATRSPKSA; TRSPKSAR; RSPKSARA; SPKSARAA; PKSARAAP; KSARAAPM; SARAAPMN; ARAAPMNL; RAAPMNLE; AAPMNLEI; APMNLEIQ; PMNLEIQK; MNLEIQKK; NLEIQKKR; LEIQKKRD; EIQKKRDY; IQKKRDYL; QKKRDYLP; KKRDYLPR; KRDYLPRS; RDYLPRSL; DYLPRSLL; YLPRSLLQ; LPRSLLQS; PRSLLQSL; RSLLQSLL; SLLQSLLQ; LLQSLLQQ; LQSLLQQV; QSLLQQVK; SLLQQVKQ; LLQQVKQW; LQQVKQWY; QQVKQWYF; QVKQWYFC; VKQWYFCF; KQWYFCFS; QWYFCFSR; WYFCFSRL; YFCFSRLH; FCFSRLHC; CFSRLHCL; FSRLHCLH; SRLHCLHL; RLHCLHLY; LHCLHLYK; HCLHLYKI; CLHLYKIP; LHLYKIPA; HLYKIPAK; LYKIPAKA; YKIPAKAL; KIPAKALK; KSSELFFL; SSELFFLF; SELFFLFQ; ELFFLFQS; LFFLFQSR; FFLFQSRF; FLFQSRFY; LFQSRFYQ; FQSRFYQL; QSRFYQLS; SRFYQLSL; RFYQLSLK; FYQLSLKL; YQLSLKLV; QLSLKLVV; LSLKLVVT; SLKLVVTA; LKLVVTAG; KLVVTAGA; LVVTAGAE; VVTAGAEP; VTAGAEPW; TAGAEPWP; AGAEPWPL; GAEPWPLS; AEPWPLSS; EPWPLSSL; PWPLSSLT; WPLSSLTG; PLSSLTGD; LSSLTGDK; SSLTGDKA; SLTGDKAK; LTGDKAKI; TGDKAKIP; GDKAKIPR; DKAKIPRL; KAKIPRLA; AKIPRLAK; KIPRLAKH; IPRLAKHV; PRLAKHVC; RLAKHVCH; LAKHVCHA; AKHVCHAL; KHVCHALS; HVCHALSF; VCHALSFL; CHALSFLR; HALSFLRS; ALSFLRSW; LSFLRSWF; SFLRSWFG; FLRSWFGC; LRSWFGCI; RSWFGCIP; SWFGCIPW; WFGCIPWV; FGCIPWVS; GCIPWVSS; CIPWVSSS; IPWVSSSS; PWVSSSSL; GHGLAAFP; HGLAAFPC; GLAAFPCE; LAAFPCES; AAFPCESC; AFPCESCT; FPCESCTF; PCESCTFL; CESCTFLP; ESCTFLPE; SCTFLPEV; CTFLPEVM; TFLPEVMV; FLPEVMVW; LPEVMVWL; PEVMVWLH; EVMVWLHS; VMVWLHSM; MVWLHSMG; VWLHSMGK; WLHSMGKQ; LHSMGKQL; HSMGKQLL; SMGKQLLP; MGKQLLPV; GKQLLPVA; KQLLPVAF; QLLPVAFF; LLPVAFFF; LPVAFFFI; PVAFFFII; VAFFFIIY; AFFFIIYK; FFFIIYKR; FFIIYKRP; FIIYKRPR; IIYKRPRP; IYKRPRPP; YKRPRPPL; KRPRPPLP; RPRPPLPP; PRPPLPPP; RPPLPPPF; PPLPPPFL; PLPPPFLS; LPPPFLSS; PPPFLSSS; PPFLSSSK; PFLSSSKG; FLSSSKGV; LSSSKGVE; SSSKGVEA; SSKGVEAF; SKGVEAFS; KGVEAFSE; GVEAFSEA; QNYLGKSL; NYLGKSLF; YLGKSLFF; LGKSLFFC; GKSLFFCN; KSLFFCNF; SLFFCNFC; LFFCNFCK 9 mers: WIKFLTGKN; IKFLTGKNP; KFLTGKNPW; FLTGKNPWS; LTGKNPWSS; TGKNPWSSW; GKNPWSSWT; KNPWSSWTF; ALKELPGEI; LKELPGEIF; KELPGEIFP; GSVRNFTLT; SVRNFTLTK; VRNFTLTKG; RNFTLTKGA; NFTLTKGAT; FTLTKGATR; TLTKGATRI; LTKGATRIK; ILCIKKWSR; LCIKKWSRM; LISLILEPG; ISLILEPGV; SLILEPGVA; LILEPGVAQ; ILEPGVAQR; LEPGVAQRF; EPGVAQRFV; PGVAQRFVL; GVAQRFVLI; VAQRFVLIF; AQRFVLIFL; QRFVLIFLF; RFVLIFLFA; FVLIFLFAQ; VLIFLFAQI; LIFLFAQIP; IFLFAQIPC; FLFAQIPCT; LFAQIPCTA; FAQIPCTAR; AQIPCTARN; QIPCTARNG; IPCTARNGL; PCTARNGLF; CTARNGLFV; TARNGLFVP; ARNGLFVPK; RNGLFVPKS; NGLFVPKSL; GLFVPKSLL; LFVPKSLLC; FVPKSLLCT; VPKSLLCTA; PKSLLCTAL; KSLLCTALA; SLLCTALAC; LLCTALACY; LCTALACYV; CTALACYVS; TALACYVSL; ALACYVSLD; IATALTASH; ATALTASHS; TALTASHSG; ALTASHSGL; LTASHSGLA; LKKLCNGGS; KKLCNGGSK; SFKVTNLYL; FKVTNLYLD; KVTNLYLDK; VIIFFIGAN; IIFFIGANL; IFFIGANLW; FFIGANLWN; FIGANLWNR; IGANLWNRR; GANLWNRRV; ANLWNRRVG; NLWNRRVGV; LWNRRVGVL; WNRRVGVLV; NRRVGVLVE; RRVGVLVEF; RVGVLVEFL; RSNSRFSTL; SNSRFSTLN; NSRFSTLNT; SRFSTLNTT; RFSTLNTTQ; FSTLNTTQK; STLNTTQKK; TLNTTQKKK; LNTTQKKKK; NTTQKKKKG; TTQKKKKGR; TQKKKKGRR; QKKKKGRRP; NPCLLCCVY; PCLLCCVYY; KTYGKIFCN; TYGKIFCNF; YGKIFCNFY; RSIPYYRRK; SIPYYRRKH; IPYYRRKHS; PYYRRKHSR; YYRRKHSRG; YRRKHSRGL; RRKHSRGLK; RKHSRGLKG; KHSRGLKGA; RNKAGVLEI; NKAGVLEIN; KAGVLEINY; GCVFIIRYV; CVFIIRYVF; VFIIRYVFR; FIIRYVFRI; IIRYVFRIS; IRYVFRISI; RYVFRISIQ; YVFRISIQC; VFRISIQCR; FRISIQCRG; RISIQCRGV; KVSEKRPAL; VSEKRPALS; SEKRPALSL; KALCKCYYF; ALCKCYYFC; LCKCYYFCR; CKCYYFCRK; KSKKYLSAS; SKKYLSASS; KKYLSASSR; KYLSASSRY; YLSASSRYS; LSASSRYSF; SASSRYSFS; KKSRYPSYD; KSRYPSYDQ; SRYPSYDQG; RYPSYDQGR; YPSYDQGRN; PSYDQGRNA; SYDQGRNAN; YDQGRNANR; DQGRNANRK; QGRNANRKI; GRNANRKIQ; RNANRKIQS; NANRKIQSY; ANRKIQSYI; NRKIQSYIR; NGFNIWSSW; GFNIWSSWK; FNIWSSWKC; NIWSSWKCC; IWSSWKCCT; WSSWKCCTR; SSWKCCTRT; SWKCCTRTI; WKCCTRTIY; KCCTRTIYG; CCTRTIYGR; CTRTIYGRC; TRTIYGRCC; RTIYGRCCL; TIYGRCCLA; IYGRCCLAA; YGRCCLAAL; GRCCLAALF; RCCLAALFA; CCLAALFAT; FFALYCFQC; FALYCFQCT; WKNNTSCRV; KNNTSCRVI; NNTSCRVIR; NTSCRVIRF; TSCRVIRFV; SCRVIRFVW; CRVIRFVWW; SLKCKPTHG; LKCKPTHGK; KCKPTHGKA; CKPTHGKAN; KPTHGKANL; ARCSYRSVH; RCSYRSVHG; CSYRSVHGC; SYRSVHGCF; IKGFAFRTW; KGFAFRTWN; GFAFRTWNK; FAFRTWNKQ; AFRTWNKQF; FRTWNKQFR; RTWNKQFRQ; TWNKQFRQF; WNKQFRQFE; NKQFRQFER; KQFRQFERL; QFRQFERLF; FRQFERLFR; RQFERLFRW; QFERLFRWK; FERLFRWKC; GKFRKETFK; KFRKETFKQ; FRKETFKQK; RKETFKQKN; KETFKQKNP; ETFKQKNPN; TFKQKNPNI; FKQKNPNIS; KQKNPNIST; QKNPNISTR; KNPNISTRL; NPNISTRLG; PNISTRLGY; NISTRLGYN; ISTRLGYNE; AQNIFKKIL; QNIFKKILT; NIFKKILTK; IFKKILTKL; FKKILTKLR; KKILTKLRV; KILTKLRVL; ILTKLRVLT; KKNFTKWND; KNFTKWNDL; NFTKWNDLV; FTKWNDLVA; TKWNDLVAT; KWNDLVATA; WNDLVATAN; NDLVATANL; DLVATANLV; DKYVYFFKD; KYVYFFKDE; YVYFFKDEI; YYKRRGFRN; IPITMLFPS; PITMLFPSL; ITMLFPSLR; TMLFPSLRY; MLFPSLRYF; LFPSLRYFS; FPSLRYFSP; PSLRYFSPC; NTTPKITQA; KWLIQKQHL; WLIQKQHLL; LIQKQHLLN; IQKQHLLNV; QKQHLLNVY; KQHLLNVYV; QHLLNVYVQ; KHLFKAFWF; HLFKAFWFA; LFKAFWFAI; FKAFWFAIV; KAFWFAIVP; AFWFAIVPV; FWFAIVPVC; WFAIVPVCQ; FAIVPVCQY; AIVPVCQYI; IVPVCQYIL; VPVCQYILS; PVCQYILSY; VCQYILSYL; CQYILSYLG; QYILSYLGP; YILSYLGPL; ILSYLGPLE; LSYLGPLEV; SYLGPLEVF; YLGPLEVFL; LGPLEVFLC; GPLEVFLCH; PLEVFLCHQ; LEVFLCHQT; EVFLCHQTP; PLLPGIPYH; LLPGIPYHT; AAHPLSGFS; AHPLSGFSC; HPLSGFSCL; GHLAKRKLG; HLAKRKLGK; LAKRKLGKD; AKRKLGKDS; KRKLGKDSL; RKLGKDSLQ; KLGKDSLQI; LGKDSLQIF; GKDSLQIFF; KDSLQIFFS; DSLQIFFSG; SLQIFFSGG; LQIFFSGGS; NILQGLSTV; ILQGLSTVV; LQGLSTVVF; QGLSTVVFQ; GLSTVVFQS; LSTVVFQSC; TGHKYQQLK; GHKYQQLKH; HKYQQLKHT; KYQQLKHTG; YQQLKHTGY; QQLKHTGYQ; QLKHTGYQL; LKHTGYQLY; KHTGYQLYK; HTGYQLYKE; TGYQLYKEA; GYQLYKEAP; YQLYKEAPH; QLYKEAPHP; LYKEAPHPV; YKEAPHPVH; KEAPHPVHL; EAPHPVHLA; APHPVHLAT; PHPVHLATL; HPVHLATLW; LCWSHEVLG; CWSHEVLGE; WSHEVLGEH; SHEVLGEHF; HEVLGEHFP; EVLGEHFPL; VLGEHFPLL; HFHFYWDQV; FHFYWDQVP; HFYWDQVPS; FYWDQVPST; YWDQVPSTQ; WDQVPSTQL; DQVPSTQLD; QVPSTQLDK; VPSTQLDKH; PSTQLDKHC; STQLDKHCF; TQLDKHCFC; QLDKHCFCP; LDKHCFCPN; DKHCFCPNR; KHCFCPNRP; HCFCPNRPY; CFCPNRPYG; FCPNRPYGQ; CPNRPYGQY; PNRPYGQYS; NRPYGQYSL; RPYGQYSLP; PYGQYSLPG; YGQYSLPGT; GQYSLPGTG; QYSLPGTGL; YSLPGTGLL; SLPGTGLLG; LPGTGLLGF; YHQGTLTCN; HQGTLTCNS; QGTLTCNSL; GTLTCNSLA; TLTCNSLAL; LTCNSLALP; TCNSLALPA; CNSLALPAF; NSLALPAFP; SLALPAFPR; LALPAFPRV; ALPAFPRVL; LPAFPRVLH; PAFPRVLHL; AFPRVLHLQ; FPRVLHLQQ; PRVLHLQQR; RVLHLQQRS; VLHLQQRSG; LHLQQRSGN; HLQQRSGNY; LQQRSGNYC; QQRSGNYCL; QRSGNYCLE; VFLHHAHAL; FLHHAHALF; LHHAHALFV; HHAHALFVT; HAHALFVTL; AHALFVTLH; HALFVTLHE; ALFVTLHEG; PLFVQLQPP; LFVQLQPPT; FVQLQPPTS; VQLQPPTSV; QLQPPTSVD; LQPPTSVDF; QPPTSVDFH; PPTSVDFHR; PTSVDFHRL; TSVDFHRLG; SVDFHRLGP; VDFHRLGPH; DFHRLGPHL; FHRLGPHLN; HRLGPHLNW; RLGPHLNWG; LGPHLNWGG; GPHLNWGGE; PHLNWGGEF; HLNWGGEFL; LNWGGEFLL; NWGGEFLLC; WGGEFLLCC; GGEFLLCCN; GEFLLCCNR; EFLLCCNRE; FLLCCNREA; LLCCNREAF; LCCNREAFF; CCNREAFFS; CNREAFFSL; NREAFFSLG; REAFFSLGY; EAFFSLGYH; AFFSLGYHC; SHFQHLALD; GFHLDPPFL; FHLDPPFLG; HLDPPFLGL; LDPPFLGLG; DPPFLGLGS; PPFLGLGSI; PFLGLGSIL; FLGLGSILP; LGLGSILPL; LLELLLLLL; LELLLLLLL; ELLLLLLLV; LLLLLLLVV; LLLLLLVVL; LLLLLVVLA; LLLLVVLAL; LLLVVLALA; LLVVLALAR; LVVLALARV; VVLALARVP; VLALARVPL; LALARVPLA; ALARVPLAF; LARVPLAFW; ARVPLAFWE; RVPLAFWEL; VPLAFWELP; PLAFWELPL; LAFWELPLD; AFWELPLDT; FWELPLDTL; WELPLDTLL; ELPLDTLLF; LPLDTLLFF; PLDTLLFFW; LDTLLFFWL; DTLLFFWLG; TLLFFWLGP; LLFFWLGPS; LFFWLGPSS; FFWLGPSSY; FWLGPSSYA; WLGPSSYAS; LGPSSYASR; GPSSYASRA; PSSYASRAG; SSYASRAGV; SYASRAGVT; YASRAGVTV; ASRAGVTVP; SRAGVTVPY; RAGVTVPYR; AGVTVPYRP; GVTVPYRPR; VTVPYRPRS; TVPYRPRSK; VPYRPRSKG; PYRPRSKGN; YRPRSKGNI; RPRSKGNIH; LAPPGAIVF; APPGAIVFS; PPGAIVFSI; PGAIVFSIN; GAIVFSINS; AIVFSINSP; IVFSINSPE; VFSINSPEC; FSINSPECT; SINSPECTL; INSPECTLC; FLKSILCVT; LKSILCVTS; KSILCVTSS; SILCVTSSI; ILCVTSSIL; LCVTSSILS; CVTSSILSA; VTSSILSAS; TSSILSASS; SSILSASSI; SILSASSIL; VWPKCTRVP; WPKCTRVPS; PKCTRVPSL; KCTRVPSLS; CTRVPSLSA; TRVPSLSAT; RVPSLSATC; VPSLSATCL; PSLSATCLT; SLSATCLTI; LSATCLTIE; SATCLTIEG; ATCLTIEGL; TCLTIEGLI; CLTIEGLIG; LTIEGLIGE; TIEGLIGER; IEGLIGERS; EGLIGERSE; KFIGAFTIV; FIGAFTIVQ; IGAFTIVQV; GAFTIVQVV; AFTIVQVVS; FTIVQVVSS; TIVQVVSSK; IVQVVSSKN; VQVVSSKNL; QVVSSKNLA; VVSSKNLAK; VSSKNLAKE; SSKNLAKES; SKNLAKESL; KNLAKESLK; NLAKESLKN; LAKESLKNL; AKESLKNLS; KESLKNLSV; ESLKNLSVL; SLKNLSVLL; LKNLSVLLC; KNLSVLLCN; NLSVLLCNS; LSVLLCNSC; SVLLCNSCE; VLLCNSCEV; LLCNSCEVI; LCNSCEVIE; CNSCEVIEG; NSCEVIEGI; SCEVIEGIS; CEVIEGISS; EVIEGISSL; VIEGISSLI; IEGISSLIT; EGISSLITC; GISSLITCH; ISSLITCHK; SSLITCHKA; SLITCHKAW; LITCHKAWE; ITCHKAWEI; TCHKAWEIV; CHKAWEIVA; HKAWEIVAN; KAWEIVANK; AWEIVANKE; WEIVANKEG; EIVANKEGP; IVANKEGPQ; VANKEGPQC; ANKEGPQCL; NKEGPQCLG; KEGPQCLGS; EGPQCLGSR; GPQCLGSRY; ILLTKVFTP; LLTKVFTPG; LTKVFTPGN; TKVFTPGNR; KVFTPGNRI; VFTPGNRIS; YSSGLNNSK; SSGLNNSKA; SGLNNSKAM; GLNNSKAMP; LNNSKAMPD; NNSKAMPDC; SQSSKNLYP; QSSKNLYPT; AKELIPLTV; IKAANPAIA; KAANPAIAP; AANPAIAPG; ANPAIAPGA; NPAIAPGAP; PAIAPGAPA; AIAPGAPAI; IAPGAPAIT; APGAPAITA; PGAPAITAY; GAPAITAYV; GVRPIAAIA; VRPIAAIAS; RPIAAIASE; PIAAIASEV; IAAIASEVL; AAIASEVLV; AIASEVLVM; IASEVLVMP; ASEVLVMPS; SEVLVMPST; EVLVMPSTV; VLVMPSTVA; LVMPSTVAR; VMPSTVARD; MPSTVARDA; PSTVARDAI; TSIAAAASP; SIAAAASPA; IAAAASPAA; AAAASPAAI; AAASPAAIS; AASPAAISA; ASPAAISAT; SPAAISATE; PAAISATEN; AAISATENP; AISATENPV; ISATENPVA; SATENPVAA; ATENPVAAA; TENPVAAAA; ENPVAAAAS; NPVAAAASD; PVAAAASDT; VAAAASDTL; AAAASDTLA; AAASDTLAT; AASDTLATR; ASDTLATRS; SDTLATRSP; DTLATRSPK; TLATRSPKS; LATRSPKSA; ATRSPKSAR; TRSPKSARA; RSPKSARAA; SPKSARAAP; PKSARAAPM; KSARAAPMN; SARAAPMNL; ARAAPMNLE; RAAPMNLEI; AAPMNLEIQ; APMNLEIQK; PMNLEIQKK; MNLEIQKKR; NLEIQKKRD; LEIQKKRDY; EIQKKRDYL; IQKKRDYLP; QKKRDYLPR; KKRDYLPRS; KRDYLPRSL; RDYLPRSLL; DYLPRSLLQ; YLPRSLLQS; LPRSLLQSL; PRSLLQSLL; RSLLQSLLQ; SLLQSLLQQ; LLQSLLQQV; LQSLLQQVK; QSLLQQVKQ; SLLQQVKQW; LLQQVKQWY; LQQVKQWYF; QQVKQWYFC; QVKQWYFCF; VKQWYFCFS; KQWYFCFSR; QWYFCFSRL; WYFCFSRLH; YFCFSRLHC; FCFSRLHCL; CFSRLHCLH; FSRLHCLHL; SRLHCLHLY; RLHCLHLYK; LHCLHLYKI; HCLHLYKIP; CLHLYKIPA; LHLYKIPAK; HLYKIPAKA; LYKIPAKAL; YKIPAKALK; KSSELFFLF; SSELFFLFQ; SELFFLFQS; ELFFLFQSR; LFFLFQSRF; FFLFQSRFY; FLFQSRFYQ; LFQSRFYQL; FQSRFYQLS; QSRFYQLSL; SRFYQLSLK; RFYQLSLKL; FYQLSLKLV; YQLSLKLVV; QLSLKLVVT; LSLKLVVTA; SLKLVVTAG; LKLVVTAGA; KLVVTAGAE; LVVTAGAEP; VVTAGAEPW; VTAGAEPWP; TAGAEPWPL; AGAEPWPLS; GAEPWPLSS; AEPWPLSSL; EPWPLSSLT; PWPLSSLTG; WPLSSLTGD; PLSSLTGDK; LSSLTGDKA; SSLTGDKAK; SLTGDKAKI; LTGDKAKIP; TGDKAKIPR; GDKAKIPRL; DKAKIPRLA; KAKIPRLAK; AKIPRLAKH; KIPRLAKHV; IPRLAKHVC; PRLAKHVCH; RLAKHVCHA; LAKHVCHAL; AKHVCHALS; KHVCHALSF; HVCHALSFL; VCHALSFLR; CHALSFLRS; HALSFLRSW; ALSFLRSWF; LSFLRSWFG; SFLRSWFGC; FLRSWFGCI; LRSWFGCIP; RSWFGCIPW; SWFGCIPWV; WFGCIPWVS; FGCIPWVSS; GCIPWVSSS; CIPWVSSSS; IPWVSSSSL; GHGLAAFPC; HGLAAFPCE; GLAAFPCES; LAAFPCESC; AAFPCESCT; AFPCESCTF; FPCESCTFL; PCESCTFLP; CESCTFLPE; ESCTFLPEV; SCTFLPEVM; CTFLPEVMV; TFLPEVMVW; FLPEVMVWL; LPEVMVWLH; PEVMVWLHS; EVMVWLHSM; VMVWLHSMG; MVWLHSMGK; VWLHSMGKQ; WLHSMGKQL; LHSMGKQLL; HSMGKQLLP; SMGKQLLPV; MGKQLLPVA; GKQLLPVAF; KQLLPVAFF; QLLPVAFFF; LLPVAFFFI; LPVAFFFII; PVAFFFIIY; VAFFFIIYK; AFFFIIYKR; FFFIIYKRP; FFIIYKRPR; FIIYKRPRP; IIYKRPRPP; IYKRPRPPL; YKRPRPPLP; KRPRPPLPP; RPRPPLPPP; PRPPLPPPF; RPPLPPPFL; PPLPPPFLS; PLPPPFLSS; LPPPFLSSS; PPPFLSSSK; PPFLSSSKG; PFLSSSKGV; FLSSSKGVE; LSSSKGVEA; SSSKGVEAF; SSKGVEAFS; SKGVEAFSE; KGVEAFSEA; QNYLGKSLF; NYLGKSLFF; YLGKSLFFC; LGKSLFFCN; GKSLFFCNF; KSLFFCNFC; SLFFCNFCK 10 mers: WIKFLTGKNP; IKFLTGKNPW; KFLTGKNPWS; FLTGKNPWSS; LTGKNPWSSW; TGKNPWSSWT; GKNPWSSWTF; ALKELPGEIF; LKELPGEIFP; GSVRNFTLTK; SVRNFTLTKG; VRNFTLTKGA; RNFTLTKGAT; NFTLTKGATR; FTLTKGATRI; TLTKGATRIK; ILCIKKWSRM; LISLILEPGV; ISLILEPGVA; SLILEPGVAQ; LILEPGVAQR; ILEPGVAQRF; LEPGVAQRFV; EPGVAQRFVL; PGVAQRFVLI; GVAQRFVLIF; VAQRFVLIFL; AQRFVLIFLF; QRFVLIFLFA; RFVLIFLFAQ; FVLIFLFAQI; VLIFLFAQIP; LIFLFAQIPC; IFLFAQIPCT; FLFAQIPCTA; LFAQIPCTAR; FAQIPCTARN; AQIPCTARNG; QIPCTARNGL; IPCTARNGLF; PCTARNGLFV; CTARNGLFVP; TARNGLFVPK; ARNGLFVPKS; RNGLFVPKSL; NGLFVPKSLL; GLFVPKSLLC; LFVPKSLLCT; FVPKSLLCTA; VPKSLLCTAL; PKSLLCTALA; KSLLCTALAC; SLLCTALACY; LLCTALACYV; LCTALACYVS; CTALACYVSL; TALACYVSLD; IATALTASHS; ATALTASHSG; TALTASHSGL; ALTASHSGLA; LKKLCNGGSK; SFKVTNLYLD; FKVTNLYLDK; VIIFFIGANL; IIFFIGANLW; IFFIGANLWN; FFIGANLWNR; FIGANLWNRR; IGANLWNRRV; GANLWNRRVG; ANLWNRRVGV; NLWNRRVGVL; LWNRRVGVLV; WNRRVGVLVE; NRRVGVLVEF; RRVGVLVEFL; RSNSRFSTLN; SNSRFSTLNT; NSRFSTLNTT; SRFSTLNTTQ; RFSTLNTTQK; FSTLNTTQKK; STLNTTQKKK; TLNTTQKKKK; LNTTQKKKKG; NTTQKKKKGR; TTQKKKKGRR; TQKKKKGRRP; NPCLLCCVYY; KTYGKIFCNF; TYGKIFCNFY; RSIPYYRRKH; SIPYYRRKHS; IPYYRRKHSR; PYYRRKHSRG; YYRRKHSRGL; YRRKHSRGLK; RRKHSRGLKG; RKHSRGLKGA; RNKAGVLEIN; NKAGVLEINY; GCVFIIRYVF; CVFIIRYVFR; VFIIRYVFRI; FIIRYVFRIS; IIRYVFRISI; IRYVFRISIQ; RYVFRISIQC; YVFRISIQCR; VFRISIQCRG; FRISIQCRGV; KVSEKRPALS; VSEKRPALSL; KALCKCYYFC; ALCKCYYFCR; LCKCYYFCRK; KSKKYLSASS; SKKYLSASSR; KKYLSASSRY; KYLSASSRYS; YLSASSRYSF; LSASSRYSFS; KKSRYPSYDQ; KSRYPSYDQG; SRYPSYDQGR; RYPSYDQGRN; YPSYDQGRNA; PSYDQGRNAN; SYDQGRNANR; YDQGRNANRK; DQGRNANRKI; QGRNANRKIQ; GRNANRKIQS; RNANRKIQSY; NANRKIQSYI; ANRKIQSYIR; NGFNIWSSWK; GFNIWSSWKC; FNIWSSWKCC; NIWSSWKCCT; IWSSWKCCTR; WSSWKCCTRT; SSWKCCTRTI; SWKCCTRTIY; WKCCTRTIYG; KCCTRTIYGR; CCTRTIYGRC; CTRTIYGRCC; TRTIYGRCCL; RTIYGRCCLA; TIYGRCCLAA; IYGRCCLAAL; YGRCCLAALF; GRCCLAALFA; RCCLAALFAT; FFALYCFQCT; WKNNTSCRVI; KNNTSCRVIR; NNTSCRVIRF; NTSCRVIRFV; TSCRVIRFVW; SCRVIRFVWW; SLKCKPTHGK; LKCKPTHGKA; KCKPTHGKAN; CKPTHGKANL; ARCSYRSVHG; RCSYRSVHGC; CSYRSVHGCF; IKGFAFRTWN; KGFAFRTWNK; GFAFRTWNKQ; FAFRTWNKQF; AFRTWNKQFR; FRTWNKQFRQ; RTWNKQFRQF; TWNKQFRQFE; WNKQFRQFER; NKQFRQFERL; KQFRQFERLF; QFRQFERLFR; FRQFERLFRW; RQFERLFRWK; QFERLFRWKC; GKFRKETFKQ; KFRKETFKQK; FRKETFKQKN; RKETFKQKNP; KETFKQKNPN; ETFKQKNPNI; TFKQKNPNIS; FKQKNPNIST; KQKNPNISTR; QKNPNISTRL; KNPNISTRLG; NPNISTRLGY; PNISTRLGYN; NISTRLGYNE; AQNIFKKILT; QNIFKKILTK; NIFKKILTKL; IFKKILTKLR; FKKILTKLRV; KKILTKLRVL; KILTKLRVLT; KKNFTKWNDL; KNFTKWNDLV; NFTKWNDLVA; FTKWNDLVAT; TKWNDLVATA; KWNDLVATAN; WNDLVATANL; NDLVATANLV; DKYVYFFKDE; KYVYFFKDEI; IPITMLFPSL; PITMLFPSLR; ITMLFPSLRY; TMLFPSLRYF; MLFPSLRYFS; LFPSLRYFSP; FPSLRYFSPC; KWLIQKQHLL; WLIQKQHLLN; LIQKQHLLNV; IQKQHLLNVY; QKQHLLNVYV; KQHLLNVYVQ; KHLFKAFWFA; HLFKAFWFAI; LFKAFWFAIV; FKAFWFAIVP; KAFWFAIVPV; AFWFAIVPVC; FWFAIVPVCQ; WFAIVPVCQY; FAIVPVCQYI; AIVPVCQYIL; IVPVCQYILS; VPVCQYILSY; PVCQYILSYL; VCQYILSYLG; CQYILSYLGP; QYILSYLGPL; YILSYLGPLE; ILSYLGPLEV; LSYLGPLEVF; SYLGPLEVFL; YLGPLEVFLC; LGPLEVFLCH; GPLEVFLCHQ; PLEVFLCHQT; LEVFLCHQTP; PLLPGIPYHT; AAHPLSGFSC; AHPLSGFSCL; GHLAKRKLGK; HLAKRKLGKD; LAKRKLGKDS; AKRKLGKDSL; KRKLGKDSLQ; RKLGKDSLQI; KLGKDSLQIF; LGKDSLQIFF; GKDSLQIFFS; KDSLQIFFSG; DSLQIFFSGG; SLQIFFSGGS; NILQGLSTVV; ILQGLSTVVF; LQGLSTVVFQ; QGLSTVVFQS; GLSTVVFQSC; TGHKYQQLKH; GHKYQQLKHT; HKYQQLKHTG; KYQQLKHTGY; YQQLKHTGYQ; QQLKHTGYQL; QLKHTGYQLY; LKHTGYQLYK; KHTGYQLYKE; HTGYQLYKEA; TGYQLYKEAP; GYQLYKEAPH; YQLYKEAPHP; QLYKEAPHPV; LYKEAPHPVH; YKEAPHPVHL; KEAPHPVHLA; EAPHPVHLAT; APHPVHLATL; PHPVHLATLW; LCWSHEVLGE; CWSHEVLGEH; WSHEVLGEHF; SHEVLGEHFP; HEVLGEHFPL; EVLGEHFPLL; HFHFYWDQVP; FHFYWDQVPS; HFYWDQVPST; FYWDQVPSTQ; YWDQVPSTQL; WDQVPSTQLD; DQVPSTQLDK; QVPSTQLDKH; VPSTQLDKHC; PSTQLDKHCF; STQLDKHCFC; TQLDKHCFCP; QLDKHCFCPN; LDKHCFCPNR; DKHCFCPNRP; KHCFCPNRPY; HCFCPNRPYG; CFCPNRPYGQ; FCPNRPYGQY; CPNRPYGQYS; PNRPYGQYSL; NRPYGQYSLP; RPYGQYSLPG; PYGQYSLPGT; YGQYSLPGTG; GQYSLPGTGL; QYSLPGTGLL; YSLPGTGLLG; SLPGTGLLGF; YHQGTLTCNS; HQGTLTCNSL; QGTLTCNSLA; GTLTCNSLAL; TLTCNSLALP; LTCNSLALPA; TCNSLALPAF; CNSLALPAFP; NSLALPAFPR; SLALPAFPRV; LALPAFPRVL; ALPAFPRVLH; LPAFPRVLHL; PAFPRVLHLQ; AFPRVLHLQQ; FPRVLHLQQR; PRVLHLQQRS; RVLHLQQRSG; VLHLQQRSGN; LHLQQRSGNY; HLQQRSGNYC; LQQRSGNYCL; QQRSGNYCLE; VFLHHAHALF; FLHHAHALFV; LHHAHALFVT; HHAHALFVTL; HAHALFVTLH; AHALFVTLHE; HALFVTLHEG; PLFVQLQPPT; LFVQLQPPTS; FVQLQPPTSV; VQLQPPTSVD; QLQPPTSVDF; LQPPTSVDFH; QPPTSVDFHR; PPTSVDFHRL; PTSVDFHRLG; TSVDFHRLGP; SVDFHRLGPH; VDFHRLGPHL; DFHRLGPHLN; FHRLGPHLNW; HRLGPHLNWG; RLGPHLNWGG; LGPHLNWGGE; GPHLNWGGEF; PHLNWGGEFL; HLNWGGEFLL; LNWGGEFLLC; NWGGEFLLCC; WGGEFLLCCN; GGEFLLCCNR; GEFLLCCNRE; EFLLCCNREA; FLLCCNREAF; LLCCNREAFF; LCCNREAFFS; CCNREAFFSL; CNREAFFSLG; NREAFFSLGY; REAFFSLGYH; EAFFSLGYHC; GFHLDPPFLG; FHLDPPFLGL; HLDPPFLGLG; LDPPFLGLGS; DPPFLGLGSI; PPFLGLGSIL; PFLGLGSILP; FLGLGSILPL; LLELLLLLLL; LELLLLLLLV; ELLLLLLLVV; LLLLLLLVVL; LLLLLLVVLA; LLLLLVVLAL; LLLLVVLALA; LLLVVLALAR; LLVVLALARV; LVVLALARVP; VVLALARVPL; VLALARVPLA; LALARVPLAF; ALARVPLAFW; LARVPLAFWE; ARVPLAFWEL; RVPLAFWELP; VPLAFWELPL; PLAFWELPLD; LAFWELPLDT; AFWELPLDTL; FWELPLDTLL; WELPLDTLLF; ELPLDTLLFF; LPLDTLLFFW; PLDTLLFFWL; LDTLLFFWLG; DTLLFFWLGP; TLLFFWLGPS; LLFFWLGPSS; LFFWLGPSSY; FFWLGPSSYA; FWLGPSSYAS; WLGPSSYASR; LGPSSYASRA; GPSSYASRAG; PSSYASRAGV; SSYASRAGVT; SYASRAGVTV; YASRAGVTVP; ASRAGVTVPY; SRAGVTVPYR; RAGVTVPYRP; AGVTVPYRPR; GVTVPYRPRS; VTVPYRPRSK; TVPYRPRSKG; VPYRPRSKGN; PYRPRSKGNI; YRPRSKGNIH; LAPPGAIVFS; APPGAIVFSI; PPGAIVFSIN; PGAIVFSINS; GAIVFSINSP; AIVFSINSPE; IVFSINSPEC; VFSINSPECT; FSINSPECTL; SINSPECTLC; FLKSILCVTS; LKSILCVTSS; KSILCVTSSI; SILCVTSSIL; ILCVTSSILS; LCVTSSILSA; CVTSSILSAS; VTSSILSASS; TSSILSASSI; SSILSASSIL; VWPKCTRVPS; WPKCTRVPSL; PKCTRVPSLS; KCTRVPSLSA; CTRVPSLSAT; TRVPSLSATC; RVPSLSATCL; VPSLSATCLT; PSLSATCLTI; SLSATCLTIE; LSATCLTIEG; SATCLTIEGL; ATCLTIEGLI; TCLTIEGLIG; CLTIEGLIGE; LTIEGLIGER; TIEGLIGERS; IEGLIGERSE; KFIGAFTIVQ; FIGAFTIVQV; IGAFTIVQVV; GAFTIVQVVS; AFTIVQVVSS; FTIVQVVSSK; TIVQVVSSKN; IVQVVSSKNL; VQVVSSKNLA; QVVSSKNLAK; VVSSKNLAKE; VSSKNLAKES; SSKNLAKESL; SKNLAKESLK; KNLAKESLKN; NLAKESLKNL; LAKESLKNLS; AKESLKNLSV; KESLKNLSVL; ESLKNLSVLL; SLKNLSVLLC; LKNLSVLLCN; KNLSVLLCNS; NLSVLLCNSC; LSVLLCNSCE; SVLLCNSCEV; VLLCNSCEVI; LLCNSCEVIE; LCNSCEVIEG; CNSCEVIEGI; NSCEVIEGIS; SCEVIEGISS; CEVIEGISSL; EVIEGISSLI; VIEGISSLIT; IEGISSLITC; EGISSLITCH; GISSLITCHK; ISSLITCHKA; SSLITCHKAW; SLITCHKAWE; LITCHKAWEI; ITCHKAWEIV; TCHKAWEIVA; CHKAWEIVAN; HKAWEIVANK; KAWEIVANKE; AWEIVANKEG; WEIVANKEGP; EIVANKEGPQ; IVANKEGPQC; VANKEGPQCL; ANKEGPQCLG; NKEGPQCLGS; KEGPQCLGSR; EGPQCLGSRY; ILLTKVFTPG; LLTKVFTPGN; LTKVFTPGNR; TKVFTPGNRI; KVFTPGNRIS; YSSGLNNSKA; SSGLNNSKAM; SGLNNSKAMP; GLNNSKAMPD; LNNSKAMPDC; SQSSKNLYPT; IKAANPAIAP; KAANPAIAPG; AANPAIAPGA; ANPAIAPGAP; NPAIAPGAPA; PAIAPGAPAI; AIAPGAPAIT; IAPGAPAITA; APGAPAITAY; PGAPAITAYV; GVRPIAAIAS; VRPIAAIASE; RPIAAIASEV; PIAAIASEVL; IAAIASEVLV; AAIASEVLVM; AIASEVLVMP; IASEVLVMPS; ASEVLVMPST; SEVLVMPSTV; EVLVMPSTVA; VLVMPSTVAR; LVMPSTVARD; VMPSTVARDA; MPSTVARDAI; TSIAAAASPA; SIAAAASPAA; IAAAASPAAI; AAAASPAAIS; AAASPAAISA; AASPAAISAT; ASPAAISATE; SPAAISATEN; PAAISATENP; AAISATENPV; AISATENPVA; ISATENPVAA; SATENPVAAA; ATENPVAAAA; TENPVAAAAS; ENPVAAAASD; NPVAAAASDT; PVAAAASDTL; VAAAASDTLA; AAAASDTLAT; AAASDTLATR; AASDTLATRS; ASDTLATRSP; SDTLATRSPK; DTLATRSPKS; TLATRSPKSA; LATRSPKSAR; ATRSPKSARA; TRSPKSARAA; RSPKSARAAP; SPKSARAAPM; PKSARAAPMN; KSARAAPMNL; SARAAPMNLE; ARAAPMNLEI; RAAPMNLEIQ; AAPMNLEIQK; APMNLEIQKK; PMNLEIQKKR; MNLEIQKKRD; NLEIQKKRDY; LEIQKKRDYL; EIQKKRDYLP; IQKKRDYLPR; QKKRDYLPRS; KKRDYLPRSL; KRDYLPRSLL; RDYLPRSLLQ; DYLPRSLLQS; YLPRSLLQSL; LPRSLLQSLL; PRSLLQSLLQ; RSLLQSLLQQ; SLLQSLLQQV; LLQSLLQQVK; LQSLLQQVKQ; QSLLQQVKQW; SLLQQVKQWY; LLQQVKQWYF; LQQVKQWYFC; QQVKQWYFCF; QVKQWYFCFS; VKQWYFCFSR; KQWYFCFSRL; QWYFCFSRLH; WYFCFSRLHC; YFCFSRLHCL; FCFSRLHCLH; CFSRLHCLHL; FSRLHCLHLY; SRLHCLHLYK; RLHCLHLYKI; LHCLHLYKIP; HCLHLYKIPA; CLHLYKIPAK; LHLYKIPAKA; HLYKIPAKAL; LYKIPAKALK; KSSELFFLFQ; SSELFFLFQS; SELFFLFQSR; ELFFLFQSRF; LFFLFQSRFY; FFLFQSRFYQ; FLFQSRFYQL; LFQSRFYQLS; FQSRFYQLSL; QSRFYQLSLK; SRFYQLSLKL; RFYQLSLKLV; FYQLSLKLVV; YQLSLKLVVT; QLSLKLVVTA; LSLKLVVTAG; SLKLVVTAGA; LKLVVTAGAE; KLVVTAGAEP; LVVTAGAEPW; VVTAGAEPWP; VTAGAEPWPL; TAGAEPWPLS; AGAEPWPLSS; GAEPWPLSSL; AEPWPLSSLT; EPWPLSSLTG; PWPLSSLTGD; WPLSSLTGDK; PLSSLTGDKA; LSSLTGDKAK; SSLTGDKAKI; SLTGDKAKIP; LTGDKAKIPR; TGDKAKIPRL; GDKAKIPRLA; DKAKIPRLAK; KAKIPRLAKH; AKIPRLAKHV; KIPRLAKHVC; IPRLAKHVCH; PRLAKHVCHA; RLAKHVCHAL; LAKHVCHALS; AKHVCHALSF; KHVCHALSFL; HVCHALSFLR; VCHALSFLRS; CHALSFLRSW; HALSFLRSWF; ALSFLRSWFG; LSFLRSWFGC; SFLRSWFGCI; FLRSWFGCIP; LRSWFGCIPW; RSWFGCIPWV; SWFGCIPWVS; WFGCIPWVSS; FGCIPWVSSS; GCIPWVSSSS; CIPWVSSSSL; GHGLAAFPCE; HGLAAFPCES; GLAAFPCESC; LAAFPCESCT; AAFPCESCTF; AFPCESCTFL; FPCESCTFLP; PCESCTFLPE; CESCTFLPEV; ESCTFLPEVM; SCTFLPEVMV; CTFLPEVMVW; TFLPEVMVWL; FLPEVMVWLH; LPEVMVWLHS; PEVMVWLHSM; EVMVWLHSMG; VMVWLHSMGK; MVWLHSMGKQ; VWLHSMGKQL; WLHSMGKQLL; LHSMGKQLLP; HSMGKQLLPV; SMGKQLLPVA; MGKQLLPVAF; GKQLLPVAFF; KQLLPVAFFF; QLLPVAFFFI; LLPVAFFFII; LPVAFFFIIY; PVAFFFIIYK; VAFFFIIYKR; AFFFIIYKRP; FFFIIYKRPR; FFIIYKRPRP; FIIYKRPRPP; IIYKRPRPPL; IYKRPRPPLP; YKRPRPPLPP; KRPRPPLPPP; RPRPPLPPPF; PRPPLPPPFL; RPPLPPPFLS; PPLPPPFLSS; PLPPPFLSSS; LPPPFLSSSK; PPPFLSSSKG; PPFLSSSKGV; PFLSSSKGVE; FLSSSKGVEA; LSSSKGVEAF; SSSKGVEAFS; SSKGVEAFSE; SKGVEAFSEA; QNYLGKSLFF; NYLGKSLFFC; YLGKSLFFCN; LGKSLFFCNF; GKSLFFCNFC; KSLFFCNFCK 11 mers: WIKFLTGKNPW; IKFLTGKNPWS; KFLTGKNPWSS; FLTGKNPWSSW; LTGKNPWSSWT; TGKNPWSSWTF; ALKELPGEIFP; GSVRNFTLTKG; SVRNFTLTKGA; VRNFTLTKGAT; RNFTLTKGATR; NFTLTKGATRI; FTLTKGATRIK; LISLILEPGVA; ISLILEPGVAQ; SLILEPGVAQR; LILEPGVAQRF; ILEPGVAQRFV; LEPGVAQRFVL; EPGVAQRFVLI; PGVAQRFVLIF; GVAQRFVLIFL; VAQRFVLIFLF; AQRFVLIFLFA; QRFVLIFLFAQ; RFVLIFLFAQI; FVLIFLFAQIP; VLIFLFAQIPC; LIFLFAQIPCT; IFLFAQIPCTA; FLFAQIPCTAR; LFAQIPCTARN; FAQIPCTARNG; AQIPCTARNGL; QIPCTARNGLF; IPCTARNGLFV; PCTARNGLFVP; CTARNGLFVPK; TARNGLFVPKS; ARNGLFVPKSL; RNGLFVPKSLL; NGLFVPKSLLC; GLFVPKSLLCT; LFVPKSLLCTA; FVPKSLLCTAL; VPKSLLCTALA; PKSLLCTALAC; KSLLCTALACY; SLLCTALACYV; LLCTALACYVS; LCTALACYVSL; CTALACYVSLD; IATALTASHSG; ATALTASHSGL; TALTASHSGLA; SFKVTNLYLDK; VIIFFIGANLW; IIFFIGANLWN; IFFIGANLWNR; FFIGANLWNRR; FIGANLWNRRV; IGANLWNRRVG; GANLWNRRVGV; ANLWNRRVGVL; NLWNRRVGVLV; LWNRRVGVLVE; WNRRVGVLVEF; NRRVGVLVEFL; RSNSRFSTLNT; SNSRFSTLNTT; NSRFSTLNTTQ; SRFSTLNTTQK; RFSTLNTTQKK; FSTLNTTQKKK; STLNTTQKKKK; TLNTTQKKKKG; LNTTQKKKKGR; NTTQKKKKGRR; TTQKKKKGRRP; KTYGKIFCNFY; RSIPYYRRKHS; SIPYYRRKHSR; IPYYRRKHSRG; PYYRRKHSRGL; YYRRKHSRGLK; YRRKHSRGLKG; RRKHSRGLKGA; RNKAGVLEINY; GCVFIIRYVFR; CVFIIRYVFRI; VFIIRYVFRIS; FIIRYVFRISI; IIRYVFRISIQ; IRYVFRISIQC; RYVFRISIQCR; YVFRISIQCRG; VFRISIQCRGV; KVSEKRPALSL; KALCKCYYFCR; ALCKCYYFCRK; KSKKYLSASSR; SKKYLSASSRY; KKYLSASSRYS; KYLSASSRYSF; YLSASSRYSFS; KKSRYPSYDQG; KSRYPSYDQGR; SRYPSYDQGRN; RYPSYDQGRNA; YPSYDQGRNAN; PSYDQGRNANR; SYDQGRNANRK; YDQGRNANRKI; DQGRNANRKIQ; QGRNANRKIQS; GRNANRKIQSY; RNANRKIQSYI; NANRKIQSYIR; NGFNIWSSWKC; GFNIWSSWKCC; FNIWSSWKCCT; NIWSSWKCCTR; IWSSWKCCTRT; WSSWKCCTRTI; SSWKCCTRTIY; SWKCCTRTIYG; WKCCTRTIYGR; KCCTRTIYGRC; CCTRTIYGRCC; CTRTIYGRCCL; TRTIYGRCCLA; RTIYGRCCLAA; TIYGRCCLAAL; IYGRCCLAALF; YGRCCLAALFA; GRCCLAALFAT; WKNNTSCRVIR; KNNTSCRVIRF; NNTSCRVIRFV; NTSCRVIRFVW; TSCRVIRFVWW; SLKCKPTHGKA; LKCKPTHGKAN; KCKPTHGKANL; ARCSYRSVHGC; RCSYRSVHGCF; IKGFAFRTWNK; KGFAFRTWNKQ; GFAFRTWNKQF; FAFRTWNKQFR; AFRTWNKQFRQ; FRTWNKQFRQF; RTWNKQFRQFE; TWNKQFRQFER; WNKQFRQFERL; NKQFRQFERLF; KQFRQFERLFR; QFRQFERLFRW; FRQFERLFRWK; RQFERLFRWKC; GKFRKETFKQK; KFRKETFKQKN; FRKETFKQKNP; RKETFKQKNPN; KETFKQKNPNI; ETFKQKNPNIS; TFKQKNPNIST; FKQKNPNISTR; KQKNPNISTRL; QKNPNISTRLG; KNPNISTRLGY; NPNISTRLGYN; PNISTRLGYNE; AQNIFKKILTK; QNIFKKILTKL; NIFKKILTKLR; IFKKILTKLRV; FKKILTKLRVL; KKILTKLRVLT; KKNFTKWNDLV; KNFTKWNDLVA; NFTKWNDLVAT; FTKWNDLVATA; TKWNDLVATAN; KWNDLVATANL; WNDLVATANLV; DKYVYFFKDEI; IPITMLFPSLR; PITMLFPSLRY; ITMLFPSLRYF; TMLFPSLRYFS; MLFPSLRYFSP; LFPSLRYFSPC; KWLIQKQHLLN; WLIQKQHLLNV; LIQKQHLLNVY; IQKQHLLNVYV; QKQHLLNVYVQ; KHLFKAFWFAI; HLFKAFWFAIV; LFKAFWFAIVP; FKAFWFAIVPV; KAFWFAIVPVC; AFWFAIVPVCQ; FWFAIVPVCQY; WFAIVPVCQYI; FAIVPVCQYIL; AIVPVCQYILS; IVPVCQYILSY; VPVCQYILSYL; PVCQYILSYLG; VCQYILSYLGP; CQYILSYLGPL; QYILSYLGPLE; YILSYLGPLEV; ILSYLGPLEVF; LSYLGPLEVFL; SYLGPLEVFLC; YLGPLEVFLCH; LGPLEVFLCHQ; GPLEVFLCHQT; PLEVFLCHQTP; AAHPLSGFSCL; GHLAKRKLGKD; HLAKRKLGKDS; LAKRKLGKDSL; AKRKLGKDSLQ; KRKLGKDSLQI; RKLGKDSLQIF; KLGKDSLQIFF; LGKDSLQIFFS; GKDSLQIFFSG; KDSLQIFFSGG; DSLQIFFSGGS; NILQGLSTVVF; ILQGLSTVVFQ; LQGLSTVVFQS; QGLSTVVFQSC; TGHKYQQLKHT; GHKYQQLKHTG; HKYQQLKHTGY; KYQQLKHTGYQ; YQQLKHTGYQL; QQLKHTGYQLY; QLKHTGYQLYK; LKHTGYQLYKE; KHTGYQLYKEA; HTGYQLYKEAP; TGYQLYKEAPH; GYQLYKEAPHP; YQLYKEAPHPV; QLYKEAPHPVH; LYKEAPHPVHL; YKEAPHPVHLA; KEAPHPVHLAT; EAPHPVHLATL; APHPVHLATLW; LCWSHEVLGEH; CWSHEVLGEHF; WSHEVLGEHFP; SHEVLGEHFPL; HEVLGEHFPLL; HFHFYWDQVPS; FHFYWDQVPST; HFYWDQVPSTQ; FYWDQVPSTQL; YWDQVPSTQLD; WDQVPSTQLDK; DQVPSTQLDKH; QVPSTQLDKHC; VPSTQLDKHCF; PSTQLDKHCFC; STQLDKHCFCP; TQLDKHCFCPN; QLDKHCFCPNR; LDKHCFCPNRP; DKHCFCPNRPY; KHCFCPNRPYG; HCFCPNRPYGQ; CFCPNRPYGQY; FCPNRPYGQYS; CPNRPYGQYSL; PNRPYGQYSLP; NRPYGQYSLPG; RPYGQYSLPGT; PYGQYSLPGTG; YGQYSLPGTGL; GQYSLPGTGLL; QYSLPGTGLLG; YSLPGTGLLGF; YHQGTLTCNSL; HQGTLTCNSLA; QGTLTCNSLAL; GTLTCNSLALP; TLTCNSLALPA; LTCNSLALPAF; TCNSLALPAFP; CNSLALPAFPR; NSLALPAFPRV; SLALPAFPRVL; LALPAFPRVLH; ALPAFPRVLHL; LPAFPRVLHLQ; PAFPRVLHLQQ; AFPRVLHLQQR; FPRVLHLQQRS; PRVLHLQQRSG; RVLHLQQRSGN; VLHLQQRSGNY; LHLQQRSGNYC; HLQQRSGNYCL; LQQRSGNYCLE; VFLHHAHALFV; FLHHAHALFVT; LHHAHALFVTL; HHAHALFVTLH; HAHALFVTLHE; AHALFVTLHEG; PLFVQLQPPTS; LFVQLQPPTSV; FVQLQPPTSVD; VQLQPPTSVDF; QLQPPTSVDFH; LQPPTSVDFHR; QPPTSVDFHRL; PPTSVDFHRLG; PTSVDFHRLGP; TSVDFHRLGPH; SVDFHRLGPHL; VDFHRLGPHLN; DFHRLGPHLNW; FHRLGPHLNWG; HRLGPHLNWGG; RLGPHLNWGGE; LGPHLNWGGEF; GPHLNWGGEFL; PHLNWGGEFLL; HLNWGGEFLLC; LNWGGEFLLCC; NWGGEFLLCCN; WGGEFLLCCNR; GGEFLLCCNRE; GEFLLCCNREA; EFLLCCNREAF; FLLCCNREAFF; LLCCNREAFFS; LCCNREAFFSL; CCNREAFFSLG; CNREAFFSLGY; NREAFFSLGYH; REAFFSLGYHC; GFHLDPPFLGL; FHLDPPFLGLG; HLDPPFLGLGS; LDPPFLGLGSI; DPPFLGLGSIL; PPFLGLGSILP; PFLGLGSILPL; LLELLLLLLLV; LELLLLLLLVV; ELLLLLLLVVL; LLLLLLLVVLA; LLLLLLVVLAL; LLLLLVVLALA; LLLLVVLALAR; LLLVVLALARV; LLVVLALARVP; LVVLALARVPL; VVLALARVPLA; VLALARVPLAF; LALARVPLAFW; ALARVPLAFWE; LARVPLAFWEL; ARVPLAFWELP; RVPLAFWELPL; VPLAFWELPLD; PLAFWELPLDT; LAFWELPLDTL; AFWELPLDTLL; FWELPLDTLLF; WELPLDTLLFF; ELPLDTLLFFW; LPLDTLLFFWL; PLDTLLFFWLG; LDTLLFFWLGP; DTLLFFWLGPS; TLLFFWLGPSS; LLFFWLGPSSY; LFFWLGPSSYA; FFWLGPSSYAS; FWLGPSSYASR; WLGPSSYASRA; LGPSSYASRAG; GPSSYASRAGV; PSSYASRAGVT; SSYASRAGVTV; SYASRAGVTVP; YASRAGVTVPY; ASRAGVTVPYR; SRAGVTVPYRP; RAGVTVPYRPR; AGVTVPYRPRS; GVTVPYRPRSK; VTVPYRPRSKG; TVPYRPRSKGN; VPYRPRSKGNI; PYRPRSKGNIH; LAPPGAIVFSI; APPGAIVFSIN; PPGAIVFSINS; PGAIVFSINSP; GAIVFSINSPE; AIVFSINSPEC; IVFSINSPECT; VFSINSPECTL; FSINSPECTLC; FLKSILCVTSS; LKSILCVTSSI; KSILCVTSSIL; SILCVTSSILS; ILCVTSSILSA; LCVTSSILSAS; CVTSSILSASS; VTSSILSASSI; TSSILSASSIL; VWPKCTRVPSL; WPKCTRVPSLS; PKCTRVPSLSA; KCTRVPSLSAT; CTRVPSLSATC; TRVPSLSATCL; RVPSLSATCLT; VPSLSATCLTI; PSLSATCLTIE; SLSATCLTIEG; LSATCLTIEGL; SATCLTIEGLI; ATCLTIEGLIG; TCLTIEGLIGE; CLTIEGLIGER; LTIEGLIGERS; TIEGLIGERSE; KFIGAFTIVQV; FIGAFTIVQVV; IGAFTIVQVVS; GAFTIVQVVSS; AFTIVQVVSSK; FTIVQVVSSKN; TIVQVVSSKNL; IVQVVSSKNLA; VQVVSSKNLAK; QVVSSKNLAKE; VVSSKNLAKES; VSSKNLAKESL; SSKNLAKESLK; SKNLAKESLKN; KNLAKESLKNL; NLAKESLKNLS; LAKESLKNLSV; AKESLKNLSVL; KESLKNLSVLL; ESLKNLSVLLC; SLKNLSVLLCN; LKNLSVLLCNS; KNLSVLLCNSC; NLSVLLCNSCE; LSVLLCNSCEV; SVLLCNSCEVI; VLLCNSCEVIE; LLCNSCEVIEG; LCNSCEVIEGI; CNSCEVIEGIS; NSCEVIEGISS; SCEVIEGISSL; CEVIEGISSLI; EVIEGISSLIT; VIEGISSLITC; IEGISSLITCH; EGISSLITCHK; GISSLITCHKA; ISSLITCHKAW; SSLITCHKAWE; SLITCHKAWEI; LITCHKAWEIV; ITCHKAWEIVA; TCHKAWEIVAN; CHKAWEIVANK; HKAWEIVANKE; KAWEIVANKEG; AWEIVANKEGP; WEIVANKEGPQ; EIVANKEGPQC; IVANKEGPQCL; VANKEGPQCLG; ANKEGPQCLGS; NKEGPQCLGSR; KEGPQCLGSRY; ILLTKVFTPGN; LLTKVFTPGNR; LTKVFTPGNRI; TKVFTPGNRIS; YSSGLNNSKAM; SSGLNNSKAMP; SGLNNSKAMPD; GLNNSKAMPDC; IKAANPAIAPG; KAANPAIAPGA; AANPAIAPGAP; ANPAIAPGAPA; NPAIAPGAPAI; PAIAPGAPAIT; AIAPGAPAITA; IAPGAPAITAY; APGAPAITAYV; GVRPIAAIASE; VRPIAAIASEV; RPIAAIASEVL; PIAAIASEVLV; IAAIASEVLVM; AAIASEVLVMP; AIASEVLVMPS; IASEVLVMPST; ASEVLVMPSTV; SEVLVMPSTVA; EVLVMPSTVAR; VLVMPSTVARD; LVMPSTVARDA; VMPSTVARDAI; TSIAAAASPAA; SIAAAASPAAI; IAAAASPAAIS; AAAASPAAISA; AAASPAAISAT; AASPAAISATE; ASPAAISATEN; SPAAISATENP; PAAISATENPV; AAISATENPVA; AISATENPVAA; ISATENPVAAA; SATENPVAAAA; ATENPVAAAAS; TENPVAAAASD; ENPVAAAASDT; NPVAAAASDTL; PVAAAASDTLA; VAAAASDTLAT; AAAASDTLATR; AAASDTLATRS; AASDTLATRSP; ASDTLATRSPK; SDTLATRSPKS; DTLATRSPKSA; TLATRSPKSAR; LATRSPKSARA; ATRSPKSARAA; TRSPKSARAAP; RSPKSARAAPM; SPKSARAAPMN; PKSARAAPMNL; KSARAAPMNLE; SARAAPMNLEI; ARAAPMNLEIQ; RAAPMNLEIQK; AAPMNLEIQKK; APMNLEIQKKR; PMNLEIQKKRD; MNLEIQKKRDY; NLEIQKKRDYL; LEIQKKRDYLP; EIQKKRDYLPR; IQKKRDYLPRS; QKKRDYLPRSL; KKRDYLPRSLL; KRDYLPRSLLQ; RDYLPRSLLQS; DYLPRSLLQSL; YLPRSLLQSLL; LPRSLLQSLLQ; PRSLLQSLLQQ; RSLLQSLLQQV; SLLQSLLQQVK; LLQSLLQQVKQ; LQSLLQQVKQW; QSLLQQVKQWY; SLLQQVKQWYF; LLQQVKQWYFC; LQQVKQWYFCF; QQVKQWYFCFS; QVKQWYFCFSR; VKQWYFCFSRL; KQWYFCFSRLH; QWYFCFSRLHC; WYFCFSRLHCL; YFCFSRLHCLH; FCFSRLHCLHL; CFSRLHCLHLY; FSRLHCLHLYK; SRLHCLHLYKI; RLHCLHLYKIP; LHCLHLYKIPA; HCLHLYKIPAK; CLHLYKIPAKA; LHLYKIPAKAL; HLYKIPAKALK; KSSELFFLFQS; SSELFFLFQSR; SELFFLFQSRF; ELFFLFQSRFY; LFFLFQSRFYQ; FFLFQSRFYQL; FLFQSRFYQLS; LFQSRFYQLSL; FQSRFYQLSLK; QSRFYQLSLKL; SRFYQLSLKLV; RFYQLSLKLVV; FYQLSLKLVVT; YQLSLKLVVTA; QLSLKLVVTAG; LSLKLVVTAGA; SLKLVVTAGAE; LKLVVTAGAEP; KLVVTAGAEPW; LVVTAGAEPWP; VVTAGAEPWPL; VTAGAEPWPLS; TAGAEPWPLSS; AGAEPWPLSSL; GAEPWPLSSLT; AEPWPLSSLTG; EPWPLSSLTGD; PWPLSSLTGDK; WPLSSLTGDKA; PLSSLTGDKAK; LSSLTGDKAKI; SSLTGDKAKIP; SLTGDKAKIPR; LTGDKAKIPRL; TGDKAKIPRLA; GDKAKIPRLAK; DKAKIPRLAKH; KAKIPRLAKHV; AKIPRLAKHVC; KIPRLAKHVCH; IPRLAKHVCHA; PRLAKHVCHAL; RLAKHVCHALS; LAKHVCHALSF; AKHVCHALSFL; KHVCHALSFLR; HVCHALSFLRS; VCHALSFLRSW; CHALSFLRSWF; HALSFLRSWFG; ALSFLRSWFGC; LSFLRSWFGCI; SFLRSWFGCIP; FLRSWFGCIPW; LRSWFGCIPWV; RSWFGCIPWVS; SWFGCIPWVSS; WFGCIPWVSSS; FGCIPWVSSSS; GCIPWVSSSSL; GHGLAAFPCES; HGLAAFPCESC; GLAAFPCESCT; LAAFPCESCTF; AAFPCESCTFL; AFPCESCTFLP; FPCESCTFLPE; PCESCTFLPEV; CESCTFLPEVM; ESCTFLPEVMV; SCTFLPEVMVW; CTFLPEVMVWL; TFLPEVMVWLH; FLPEVMVWLHS; LPEVMVWLHSM; PEVMVWLHSMG; EVMVWLHSMGK; VMVWLHSMGKQ; MVWLHSMGKQL; VWLHSMGKQLL; WLHSMGKQLLP; LHSMGKQLLPV; HSMGKQLLPVA; SMGKQLLPVAF; MGKQLLPVAFF; GKQLLPVAFFF; KQLLPVAFFFI; QLLPVAFFFII; LLPVAFFFIIY; LPVAFFFIIYK; PVAFFFIIYKR; VAFFFIIYKRP; AFFFIIYKRPR; FFFIIYKRPRP; FFIIYKRPRPP; FIIYKRPRPPL; IIYKRPRPPLP; IYKRPRPPLPP; YKRPRPPLPPP; KRPRPPLPPPF; RPRPPLPPPFL; PRPPLPPPFLS; RPPLPPPFLSS; PPLPPPFLSSS; PLPPPFLSSSK; LPPPFLSSSKG; PPPFLSSSKGV; PPFLSSSKGVE; PFLSSSKGVEA; FLSSSKGVEAF; LSSSKGVEAFS; SSSKGVEAFSE; SSKGVEAFSEA; QNYLGKSLFFC; NYLGKSLFFCN; YLGKSLFFCNF; LGKSLFFCNFC; GKSLFFCNFCK BK virus complementary reading frame 3 8 mers: QGRIHGAH; GRIHGAHG; RIHGAHGP; IHGAHGPF; HGAHGPFR; GAHGPFRP; KSCLGKSS; SCLGKSSL; CLGKSSLN; LGKSSLNE; GKSSLNEK; KSSLNEKS; SSLNEKSL; SLNEKSLF; LNEKSLFK; NEKSLFKE; EKSLFKEV; NEENEYFV; KNGAGCKG; NGAGCKGS; GAGCKGSS; AGCKGSSS; GCKGSSSA; FSSLPRYP; SSLPRYPV; SLPRYPVL; LPRYPVLQ; PRYPVLQG; RYPVLQGM; YPVLQGMA; PVLQGMAY; VLQGMAYL; LQGMAYLF; QGMAYLFQ; GMAYLFQK; MAYLFQKA; AYLFQKAF; YLFQKAFC; LFQKAFCA; FQKAFCAL; QKAFCALP; KAFCALPL; AFCALPLH; FCALPLHA; CALPLHAM; ALPLHAMS; LPLHAMSA; KIFKKRAL; IFKKRALG; FKKRALGL; KKRALGLD; KRALGLDR; RALGLDRL; ALGLDRLL; LGLDRLLL; GLDRLLLH; LLHTVVWL; LHTVVWLR; HTVVWLRP; TVVWLRPN; RNSAMVGP; NSAMVGPN; SAMVGPNN; AMVGPNNW; MVGPNNWR; VGPNNWRN; GPNNWRNS; PNNWRNSL; NNWRNSLQ; NWRNSLQR; WRNSLQRS; RNSLQRSK; NSLQRSKA; SLQRSKAL; LQRSKALR; INNKILKG; NNKILKGP; NKILKGPK; VPTYGTEE; PTYGTEEW; TYGTEEWE; YGTEEWES; GTEEWESW; TEEWESWW; EEWESWWS; EWESWWSS; WESWWSSF; ESWWSSFN; SWWSSFNE; WWSSFNEK; WSSFNEKW; SSFNEKWD; SFNEKWDE; FNEKWDED; NEKWDEDL; EKWDEDLF; KWDEDLFC; WDEDLFCH; DEDLFCHE; EDLFCHED; DLFCHEDM; LFCHEDMF; FCHEDMFA; CHEDMFAS; HEDMFASD; EDMFASDE; DMFASDEE; MFASDEEA; FASDEEAT; ASDEEATA; SDEEATAD; DEEATADS; EEATADSQ; EATADSQH; ATADSQHS; TADSQHST; ADSQHSTP; DSQHSTPP; SQHSTPPK; QHSTPPKK; HSTPPKKK; STPPKKKR; TPPKKKRK; PPKKKRKV; PKKKRKVE; KKKRKVED; KKRKVEDP; KRKVEDPK; RKVEDPKD; KVEDPKDF; VEDPKDFP; EDPKDFPS; DPKDFPSD; PKDFPSDL; KDFPSDLH; DFPSDLHQ; FPSDLHQF; PSDLHQFL; SDLHQFLS; DLHQFLSQ; LHQFLSQA; HQFLSQAV; QFLSQAVF; FLSQAVFS; LSQAVFSN; SQAVFSNR; QAVFSNRT; AVFSNRTL; VFSNRTLA; FSNRTLAC; SNRTLACF; NRTLACFA; RTLACFAV; TLACFAVY; LACFAVYT; ACFAVYTT; CFAVYTTK; FAVYTTKE; AVYTTKEK; VYTTKEKA; YTTKEKAQ; TTKEKAQI; TKEKAQIL; KEKAQILY; EKAQILYK; KAQILYKK; AQILYKKL; QILYKKLM; ILYKKLME; LYKKLMEK; YKKLMEKY; KKLMEKYS; KLMEKYSV; LMEKYSVT; MEKYSVTF; EKYSVTFI; KYSVTFIS; YSVTFISR; SVTFISRH; VTFISRHM; TFISRHMC; FISRHMCA; ISRHMCAG; SRHMCAGH; RHMCAGHN; HMCAGHNI; MCAGHNII; CAGHNIIF; AGHNIIFF; GHNIIFFL; HNIIFFLT; NIIFFLTP; IIFFLTPH; IFFLTPHR; FFLTPHRH; FLTPHRHR; LTPHRHRV; TPHRHRVS; PHRHRVSA; HRHRVSAI; RHRVSAIN; HRVSAINN; RVSAINNF; VSAINNFC; SAINNFCQ; AINNFCQK; INNFCQKL; NNFCQKLC; NFCQKLCT; FCQKLCTF; CQKLCTFS; QKLCTFSF; KLCTFSFL; LCTFSFLI; CTFSFLIC; TFSFLICK; FSFLICKG; SFLICKGV; FLICKGVN; LICKGVNK; ICKGVNKE; CKGVNKEY; KGVNKEYL; GVNKEYLL; VNKEYLLY; NKEYLLYS; KEYLLYSA; EYLLYSAL; YLLYSALT; LLYSALTR; LYSALTRD; YSALTRDP; SALTRDPY; ALTRDPYH; LTRDPYHT; TRDPYHTI; RDPYHTIE; DPYHTIEE; PYHTIEES; YHTIEESI; HTIEESIQ; TIEESIQG; IEESIQGG; EESIQGGL; ESIQGGLK; SIQGGLKE; IQGGLKEH; QGGLKEHD; GGLKEHDF; GLKEHDFS; LKEHDFSP; KEHDFSPE; EHDFSPEE; HDFSPEEP; DFSPEEPE; FSPEEPEE; SPEEPEET; PEEPEETK; EEPEETKQ; EPEETKQV; PEETKQVS; EETKQVSW; ETKQVSWK; TKQVSWKL; KQVSWKLI; QVSWKLIT; VSWKLITE; SWKLITEY; WKLITEYA; KLITEYAV; LITEYAVE; ITEYAVET; TEYAVETK; EYAVETKC; YAVETKCE; AVETKCED; VETKCEDV; ETKCEDVF; TKCEDVFL; KCEDVFLL; CEDVFLLL; EDVFLLLG; DVFLLLGM; VFLLLGMY; FLLLGMYL; LLLGMYLE; LLGMYLEF; LGMYLEFQ; GMYLEFQY; MYLEFQYN; YLEFQYNV; LEFQYNVE; EFQYNVEE; FQYNVEEC; QYNVEECK; YNVEECKK; NVEECKKC; VEECKKCQ; EECKKCQK; ECKKCQKK; CKKCQKKD; KKCQKKDQ; KCQKKDQP; CQKKDQPY; QKKDQPYH; KKDQPYHF; KDQPYHFK; DQPYHFKY; QPYHFKYH; PYHFKYHE; YHFKYHEK; HFKYHEKH; FKYHEKHF; KYHEKHFA; YHEKHFAN; HEKHFANA; EKHFANAI; KHFANAII; HFANAIIF; FANAIIFA; ANAIIFAE; NAIIFAES; AIIFAESK; IIFAESKN; IFAESKNQ; FAESKNQK; AESKNQKS; ESKNQKSI; SKNQKSIC; KNQKSICQ; NQKSICQQ; QKSICQQA; KSICQQAV; SICQQAVD; ICQQAVDT; CQQAVDTV; QQAVDTVL; QAVDTVLA; AVDTVLAK; VDTVLAKK; DTVLAKKR; TVLAKKRV; VLAKKRVD; LAKKRVDT; AKKRVDTL; KKRVDTLH; KRVDTLHM; RVDTLHMT; VDTLHMTR; DTLHMTRE; TLHMTREE; LHMTREEM; HMTREEML; MTREEMLT; TREEMLTE; REEMLTER; EEMLTERF; EMLTERFN; MLTERFNH; LTERFNHI; TERFNHIL; ERFNHILD; RFNHILDK; FNHILDKM; NHILDKMD; HILDKMDL; ILDKMDLI; LDKMDLIF; DKMDLIFG; KMDLIFGA; MDLIFGAH; DLIFGAHG; LIFGAHGN; IFGAHGNA; FGAHGNAV; GAHGNAVL; AHGNAVLE; HGNAVLEQ; GNAVLEQY; NAVLEQYM; AVLEQYMA; VLEQYMAG; LEQYMAGV; EQYMAGVA; QYMAGVAW; YMAGVAWL; MAGVAWLH; AGVAWLHC; GVAWLHCL; VAWLHCLL; AWLHCLLP; WLHCLLPK; LHCLLPKM; HCLLPKMD; CLLPKMDS; LLPKMDSV; LPKMDSVI; PKMDSVIF; KMDSVIFD; MDSVIFDF; DSVIFDFL; SVIFDFLH; VIFDFLHC; IFDFLHCI; FDFLHCIV; DFLHCIVF; FLHCIVFN; LHCIVFNV; HCIVFNVP; CIVFNVPK; IVFNVPKR; VFNVPKRR; FNVPKRRY; NVPKRRYW; VPKRRYWL; PKRRYWLF; KRRYWLFK; RRYWLFKG; RYWLFKGP; YWLFKGPI; WLFKGPID; LFKGPIDS; FKGPIDSG; KGPIDSGK; GPIDSGKT; PIDSGKTT; IDSGKTTL; DSGKTTLA; SGKTTLAA; GKTTLAAG; KTTLAAGL; TTLAAGLL; TLAAGLLD; LAAGLLDL; AAGLLDLC; AGLLDLCG; GLLDLCGG; LLDLCGGK; LDLCGGKA; DLCGGKAL; LCGGKALN; CGGKALNV; GGKALNVN; GKALNVNL; KALNVNLP; ALNVNLPM; LNVNLPME; NVNLPMER; VNLPMERL; NLPMERLT; LPMERLTF; PMERLTFE; MERLTFEL; ERLTFELG; RLTFELGV; LTFELGVA; TFELGVAI; FELGVAID; ELGVAIDQ; LGVAIDQY; GVAIDQYM; VAIDQYMV; AIDQYMVV; IDQYMVVF; DQYMVVFE; QYMVVFED; YMVVFEDV; MVVFEDVK; VVFEDVKG; VFEDVKGT; FEDVKGTG; EDVKGTGA; DVKGTGAE; VKGTGAES; KGTGAESK; GTGAESKD; TGAESKDL; GAESKDLP; AESKDLPS; ESKDLPSG; SKDLPSGH; KDLPSGHG; DLPSGHGI; LPSGHGIN; PSGHGINN; SGHGINNL; GHGINNLD; HGINNLDS; GINNLDSL; INNLDSLR; NNLDSLRD; NLDSLRDY; LDSLRDYL; DSLRDYLD; SLRDYLDG; LRDYLDGS; RDYLDGSV; DYLDGSVK; YLDGSVKV; LDGSVKVN; DGSVKVNL; GSVKVNLE; SVKVNLEK; VKVNLEKK; KVNLEKKH; VNLEKKHL; NLEKKHLN; LEKKHLNK; EKKHLNKR; KKHLNKRT; KHLNKRTQ; HLNKRTQI; LNKRTQIF; NKRTQIFP; KRTQIFPP; RTQIFPPG; TQIFPPGL; QIFPPGLV; IFPPGLVT; FPPGLVTM; PPGLVTMN; PGLVTMNE; GLVTMNEY; LVTMNEYP; VTMNEYPV; TMNEYPVP; MNEYPVPK; NEYPVPKT; EYPVPKTL; YPVPKTLQ; PVPKTLQA; VPKTLQAR; PKTLQARF; KTLQARFV; TLQARFVR; LQARFVRQ; QARFVRQI; ARFVRQID; RFVRQIDF; FVRQIDFR; VRQIDFRP; RQIDFRPK; QIDFRPKI; IDFRPKIY; DFRPKIYL; FRPKIYLR; RPKIYLRK; PKIYLRKS; KIYLRKSL; IYLRKSLQ; YLRKSLQN; LRKSLQNS; RKSLQNSE; KSLQNSEF; SLQNSEFL; LQNSEFLL; QNSEFLLE; NSEFLLEK; SEFLLEKR; EFLLEKRI; FLLEKRIL; LLEKRILQ; LEKRILQS; EKRILQSG; KRILQSGM; RILQSGMT; ILQSGMTL; LQSGMTLL; QSGMTLLL; SGMTLLLL; GMTLLLLL; MTLLLLLI; TLLLLLIW; LLLLLIWF; LLLLIWFR; LLLIWFRP; LLIWFRPV; LIWFRPVA; IWFRPVAD; WFRPVADF; FRPVADFA; RPVADFAT; PVADFATD; VADFATDI; ADFATDIQ; DFATDIQS; FATDIQSR; ATDIQSRI; TDIQSRIV; DIQSRIVE; IQSRIVEW; QSRIVEWK; SRIVEWKE; RIVEWKER; IVEWKERL; VEWKERLD; EWKERLDS; WKERLDSE; KERLDSEI; ERLDSEIS; RLDSEISM; LDSEISMY; DSEISMYT; SEISMYTF; EISMYTFS; ISMYTFSR; SMYTFSRM; MYTFSRMK; YTFSRMKY; TFSRMKYN; FSRMKYNI; SRMKYNIC; RMKYNICM; MKYNICMG; KYNICMGK; YNICMGKC; NICMGKCI; ICMGKCIL; CMGKCILD; MGKCILDI; GKCILDIT; KCILDITR; CILDITRE; ILDITREE; LDITREED; DITREEDS; ITREEDSE; TREEDSET; REEDSETE; EEDSETED; EDSETEDS; DSETEDSG; SETEDSGH; ETEDSGHG; TEDSGHGS; EDSGHGSS; DSGHGSST; SGHGSSTE; GHGSSTES; HGSSTESQ; GSSTESQS; SSTESQSQ; STESQSQC; TESQSQCS; ESQSQCSS; SQSQCSSQ; QSQCSSQV; SQCSSQVS; QCSSQVSD; CSSQVSDT; SSQVSDTS; SQVSDTSA; QVSDTSAP; VSDTSAPA; SDTSAPAE; DTSAPAED; TSAPAEDS; SAPAEDSQ; APAEDSQR; PAEDSQRS; AEDSQRSD; EDSQRSDP; DSQRSDPH; SQRSDPHS; QRSDPHSQ; RSDPHSQE; SDPHSQEL; DPHSQELH; PHSQELHL; HSQELHLC; SQELHLCK; QELHLCKG; ELHLCKGF; LHLCKGFQ; HLCKGFQC; LCKGFQCF; CKGFQCFK; KGFQCFKR; GFQCFKRP; FQCFKRPK; QCFKRPKT; CFKRPKTP; FKRPKTPP; KRPKTPPP; RPKTPPPK; HKLKSGLY; KLKSGLYK; LKSGLYKS; KSGLYKSS; SGLYKSSI; GLYKSSIY; MYMYNKST; YMYNKSTC; MYNKSTCL; YNKSTCLK; NKSTCLKH; KSTCLKHF; STCLKHFG; TCLKHFGL; CLKHFGLQ; LKHFGLQL; KHFGLQLS; HFGLQLSL; FGLQLSLF; GLQLSLFV; LQLSLFVN; QLSLFVNI; LSLFVNIS; SLFVNISY; LFVNISYH; FVNISYHI; VNISYHIW; NISYHIWV; ISYHIWVP; SYHIWVPW; YHIWVPWK; HIWVPWKS; IWVPWKSF; WVPWKSFC; VPWKSFCA; PWKSFCAI; WKSFCAIK; KSFCAIKH; SFCAIKHP; FCAIKHPN; CAIKHPNL; AIKHPNLF; IKHPNLFY; KHPNLFYL; HPNLFYLG; PNLFYLGF; NLFYLGFH; LFYLGFHT; FYLGFHTI; YLGFHTIH; LGFHTIHR; GFHTIHRL; FHTIHRLP; HTIHRLPI; TIHRLPIH; IHRLPIHS; HRLPIHSL; RLPIHSLG; LPIHSLGS; PIHSLGSP; IHSLGSPV; HSLGSPVY; SLGSPVYK; LGSPVYKV; GSPVYKVT; QKGNWVRI; KGNWVRIL; GNWVRILY; NWVRILYR; WVRILYRS; VRILYRSF; RILYRSFS; ILYRSFSQ; LYRSFSQA; YRSFSQAD; RSFSQADL; SFSQADLK; FSQADLKI; SQADLKIS; QADLKISC; ADLKISCK; DLKISCKA; LKISCKAS; KISCKASP; ISCKASPL; SCKASPLL; CKASPLLC; KASPLLCS; ASPLLCSR; SPLLCSRA; PLLCSRAV; LLCSRAVS; LCSRAVSK; CSRAVSKQ; SRAVSKQA; RAVSKQAT; AVSKQATN; VSKQATNI; SKQATNIS; KQATNISS; NIQAISFT; IQAISFTK; QAISFTKR; AISFTKRP; ISFTKRPH; SFTKRPHT; FTKRPHTL; TKRPHTLF; KRPHTLFI; QHCGSCVG; HCGSCVGH; CGSCVGHM; GSCVGHMK; SCVGHMKY; CVGHMKYW; VGHMKYWG; GHMKYWGN; HMKYWGNI; MKYWGNIF; KYWGNIFP; YWGNIFPS; WGNIFPSC; GNIFPSCE; NIFPSCES; IFPSCESP; FPSCESPK; PSCESPKI; SCESPKIP; CESPKIPS; ESPKIPSI; SPKIPSIF; PKIPSIFI; KIPSIFIS; IPSIFIST; PSIFISTG; SIFISTGI; IFISTGIR; FISTGIRY; ISTGIRYP; STGIRYPA; TGIRYPAL; GIRYPALN; IRYPALNW; RYPALNWI; YPALNWIS; PALNWISI; ALNWISIV; LNWISIVF; NWISIVFV; WISIVFVQ; ISIVFVQI; SIVFVQIG; IVFVQIGL; VFVQIGLM; FVQIGLMV; VQIGLMVS; QIGLMVSI; IGLMVSIH; GLMVSIHY; LMVSIHYL; MVSIHYLG; VSIHYLGL; SIHYLGLG; IHYLGLGC; HYLGLGCW; YLGLGCWV; LGLGCWVF; GLGCWVFR; LGCWVFRG; GCWVFRGY; CWVFRGYS; WVFRGYST; VFRGYSTI; FRGYSTIR; RGYSTIRV; GYSTIRVL; HSLHFQGF; SLHFQGFS; LHFQGFST; HFQGFSTY; FQGFSTYS; QGFSTYSK; GFSTYSKE; FSTYSKEV; STYSKEVE; TYSKEVEI; YSKEVEIT; SKEVEITA; KEVEITAL; EVEITALN; VEITALNR; EITALNRF; ITALNRFS; TALNRFSS; ALNRFSST; LNRFSSTM; NRFSSTML; RFSSTMLM; FSSTMLMH; SSTMLMHF; STMLMHFL; PCMKVKHA; CMKVKHAS; MKVKHASY; KVKHASYS; VKHASYSN; KHASYSNN; HASYSNNL; ASYSNNLC; SYSNNLCL; YSNNLCLY; SNNLCLYS; NNLCLYSY; NLCLYSYS; LCLYSYSL; CLYSYSLP; LYSYSLPH; YSYSLPHQ; IGEGNSCC; GEGNSCCA; EGNSCCAV; GNSCCAVT; NSCCAVTG; SCCAVTGK; CCAVTGKH; CAVTGKHF; AVTGKHFS; VTGKHFSL; TGKHFSLW; GKHFSLWA; KHFSLWAI; HFSLWAIT; FSLWAITA; SLWAITAK; LWAITAKV; WAITAKVI; AITAKVIF; ITAKVIFS; TAKVIFST; TKAPKVFI; KAPKVFIW; APKVFIWI; PKVFIWIP; KVFIWIPH; VFIWIPHF; FIWIPHFW; IWIPHFWV; EAFYLCNS; AFYLCNSI; FYLCNSIY; YLCNSIYP; LCNSIYPS; CNSIYPSF; NSIYPSFN; SIYPSFNF; FWHLHGFL; WHLHGFLW; HLHGFLWL; LHGFLWLF; HGFLWLFG; GFLWLFGS; FLWLFGSC; LWLFGSCP; WLFGSCPW; LFGSCPWT; FGSCPWTL; GSCPWTLS; SCPWTLSF; CPWTLSFS; PWTLSFSF; WTLSFSFG; TLSFSFGW; LSFSFGWG; SFSFGWGH; FSFGWGHL; SFGWGHLH; FGWGHLHM; GWGHLHML; WGHLHMLQ; GHLHMLQE; HLHMLQEQ; LHMLQEQV; HMLQEQVL; MLQEQVLQ; LQEQVLQS; QEQVLQSR; EQVLQSRT; QVLQSRTG; VLQSRTGL; LQSRTGLE; QSRTGLEV; SRTGLEVK; RTGLEVKA; TGLEVKAT; GLEVKATS; LEVKATSI; EVKATSIE; VKATSIEE; KATSIEEQ; ATSIEEQF; TSIEEQFF; SIEEQFFD; TLLNVHFV; LLNVHFVD; LNVHFVDF; NVHFVDFL; VHFVDFLS; HFVDFLSP; FVDFLSPF; VDFLSPFF; DFLSPFFV; LLLYCQHH; LLYCQHHL; LYCQHHLY; YCQHHLYY; CQHHLYYK; QHHLYYKY; HHLYYKYG; HLYYKYGQ; LYYKYGQN; YYKYGQNV; YKYGQNVH; KYGQNVHG; YGQNVHGY; GQNVHGYL; QNVHGYLP; NVHGYLPF; VHGYLPFQ; HGYLPFQL; GYLPFQLL; YLPFQLLV; GKDQNNIV; KDQNNIVE; DQNNIVEY; QNNIVEYN; NNIVEYNY; NIVEYNYK; IVEYNYKS; VEYNYKSL; KIFLFFSA; IFLFFSAI; FLFFSAIP; LFFSAIPV; FFSAIPVR; FSAIPVRL; QTKKDPNA; QKYLHQET; KYLHQETE; YLHQETEY; LHQETEYH; HQETEYHS; QETEYHST; ETEYHSTH; TEYHSTHL; EYHSTHLG; TIPKPCLI; IPKPCLIA; PKPCLIAD; KPCLIADR; PCLIADRG; CLIADRGL; LIADRGLQ; IADRGLQW; ADRGLQWK; DRGLQWKL; RGLQWKLC; GLQWKLCD; LQWKLCDP; QWKLCDPN; WKLCDPNH; KLCDPNHQ; LCDPNHQR; CDPNHQRT; DPNHQRTY; PNHQRTYT; NHQRTYTL; HQRTYTLL; QRTYTLLE; RTYTLLEL; TYTLLELR; YTLLELRN; QFELKQQT; FELKQQTQ; ELKQQTQQ; PQEHQQLQ; QEHQQLQH; EHQQLQHM; HQQLQHMF; QQLQHMFE; QLQHMFEE; LQHMFEEL; QHMFEELG; HMFEELGL; PLRYLLCP; LRYLLCPL; RYLLCPLQ; QGMQFELL; QQQPPQQQ; QQPPQQQF; QPPQQQFQ; PPQQQFQP; PQQQFQPL; QQQFQPLK; QQFQPLKI; QFQPLKIL; FQPLKILW; QPLKILWQ; PLKILWQQ; LKILWQQQ; KILWQQQP; ILWQQQPQ; LWQQQPQI; WQQQPQIH; QQQPQIHW; QQPQIHWQ; QPQIHWQL; PQIHWQLG; QIHWQLGP; IHWQLGPP; HWQLGPPK; WQLGPPKV; QLGPPKVL; LGPPKVLE; GPPKVLEQ; PPKVLEQH; PKVLEQHP; TWKYKKKG; WKYKKKGI; KYKKKGIT; YKKKGITY; KKKGITYL; KKGITYLG; KGITYLGV; GITYLGVF; ITYLGVFY; TYLGVFYR; YLGVFYRV; LGVFYRVF; GVFYRVFY; VFYRVFYS; FYRVFYSR; SSGTFVFP; SGTFVFPV; GTFVFPVY; TFVFPVYT; FVFPVYTV; VFPVYTVF; FPVYTVFT; PVYTVFTS; VYTVFTST; YTVFTSTK; TVFTSTKF; VFTSTKFQ; FTSTKFQQ; TSTKFQQK; STKFQQKL; NKNKNPLS; KNKNPLSS; NKNPLSSF; KNPLSSFF; NPLSSFFC; PLSSFFCS; LSSFFCSS; SSFFCSSP; SFFCSSPG; FFCSSPGF; FCSSPGFT; CSSPGFTN; SSPGFTNF; SPGFTNFH; QLAQNHGL; LAQNHGLC; AQNHGLCP; QNHGLCPV; LGTRPRFL; GTRPRFLG; TRPRFLGS; RPRFLGSQ; PRFLGSQN; RFLGSQNM; FLGSQNMS; LGSQNMSV; GSQNMSVM; SQNMSVMH; QNMSVMHF; NMSVMHFP; MSVMHFPS; GHGLAAFH; HGLAAFHG; AAPPCESC; APPCESCT; PPCESCTF; PCESCTFL; CESCTFLP; ESCTFLPE; SCTFLPEV; CTFLPEVM; TFLPEVMV; FLPEVMVW; LPEVMVWL; PEVMVWLH; EVMVWLHS; VMVWLHSP; MVWLHSPV; VWLHSPVS; WLHSPVSH; LHSPVSHA; HSPVSHAL; SPVSHALS; PVSHALSF; VSHALSFL; SHALSFLR; HALSFLRS; ALSFLRSW; LSFLRSWF; SFLRSWFG; FLRSWFGC; LRSWFGCI; RSWFGCIP; SWFGCIPW; WFGCIPWV; FGCIPWVS; GCIPWVSS; CIPWVSSS; IPWVSSSS; PWVSSSSL; WVSSSSLW; VSSSSLWP; SSSSLWPF; SSSLWPFF; SSLWPFFL; YIRGRGRL; IRGRGRLC; RGRGRLCL; GRGRLCLH; RGRLCLHP; GRLCLHPF; RLCLHPFS; LCLHPFSQ; CLHPFSQV; LHPFSQVV; HPFSQVVR; PFSQVVRV; FSQVVRVW; SQVVRVWR; QVVRVWRL; VVRVWRLF; VRVWRLFL; RVWRLFLR; VWRLFLRP; WRLFLRPS; RLFLRPSK; LFLRPSKT; FLRPSKTI; LRPSKTIW; RPSKTIWG; PSKTIWGN; SKTIWGNP; KTIWGNPY; TIWGNPYS; IWGNPYSF; WGNPYSFA; GNPYSFAI; NPYSFAIF; PYSFAIFA; YSFAIFAK 9 mers: QGRIHGAHG; GRIHGAHGP; RIHGAHGPF; IHGAHGPFR; HGAHGPFRP; KSCLGKSSL; SCLGKSSLN; CLGKSSLNE; LGKSSLNEK; GKSSLNEKS; KSSLNEKSL; SSLNEKSLF; SLNEKSLFK; LNEKSLFKE; NEKSLFKEV; KNGAGCKGS; NGAGCKGSS; GAGCKGSSS; AGCKGSSSA; FSSLPRYPV; SSLPRYPVL; SLPRYPVLQ; LPRYPVLQG; PRYPVLQGM; RYPVLQGMA; YPVLQGMAY; PVLQGMAYL; VLQGMAYLF; LQGMAYLFQ; QGMAYLFQK; GMAYLFQKA; MAYLFQKAF; AYLFQKAFC; YLFQKAFCA; LFQKAFCAL; FQKAFCALP; QKAFCALPL; KAFCALPLH; AFCALPLHA; FCALPLHAM; CALPLHAMS; ALPLHAMSA; KIFKKRALG; IFKKRALGL; FKKRALGLD; KKRALGLDR; KRALGLDRL; RALGLDRLL; ALGLDRLLL; LGLDRLLLH; LLHTVVWLR; LHTVVWLRP; HTVVWLRPN; RNSAMVGPN; NSAMVGPNN; SAMVGPNNW; AMVGPNNWR; MVGPNNWRN; VGPNNWRNS; GPNNWRNSL; PNNWRNSLQ; NNWRNSLQR; NWRNSLQRS; WRNSLQRSK; RNSLQRSKA; NSLQRSKAL; SLQRSKALR; INNKILKGP; NNKILKGPK; VPTYGTEEW; PTYGTEEWE; TYGTEEWES; YGTEEWESW; GTEEWESWW; TEEWESWWS; EEWESWWSS; EWESWWSSF; WESWWSSFN; ESWWSSFNE; SWWSSFNEK; WWSSFNEKW; WSSFNEKWD; SSFNEKWDE; SFNEKWDED; FNEKWDEDL; NEKWDEDLF; EKWDEDLFC; KWDEDLFCH; WDEDLFCHE; DEDLFCHED; EDLFCHEDM; DLFCHEDMF; LFCHEDMFA; FCHEDMFAS; CHEDMFASD; HEDMFASDE; EDMFASDEE; DMFASDEEA; MFASDEEAT; FASDEEATA; ASDEEATAD; SDEEATADS; DEEATADSQ; EEATADSQH; EATADSQHS; ATADSQHST; TADSQHSTP; ADSQHSTPP; DSQHSTPPK; SQHSTPPKK; QHSTPPKKK; HSTPPKKKR; STPPKKKRK; TPPKKKRKV; PPKKKRKVE; PKKKRKVED; KKKRKVEDP; KKRKVEDPK; KRKVEDPKD; RKVEDPKDF; KVEDPKDFP; VEDPKDFPS; EDPKDFPSD; DPKDFPSDL; PKDFPSDLH; KDFPSDLHQ; DFPSDLHQF; FPSDLHQFL; PSDLHQFLS; SDLHQFLSQ; DLHQFLSQA; LHQFLSQAV; HQFLSQAVF; QFLSQAVFS; FLSQAVFSN; LSQAVFSNR; SQAVFSNRT; QAVFSNRTL; AVFSNRTLA; VFSNRTLAC; FSNRTLACF; SNRTLACFA; NRTLACFAV; RTLACFAVY; TLACFAVYT; LACFAVYTT; ACFAVYTTK; CFAVYTTKE; FAVYTTKEK; AVYTTKEKA; VYTTKEKAQ; YTTKEKAQI; TTKEKAQIL; TKEKAQILY; KEKAQILYK; EKAQILYKK; KAQILYKKL; AQILYKKLM; QILYKKLME; ILYKKLMEK; LYKKLMEKY; YKKLMEKYS; KKLMEKYSV; KLMEKYSVT; LMEKYSVTF; MEKYSVTFI; EKYSVTFIS; KYSVTFISR; YSVTFISRH; SVTFISRHM; VTFISRHMC; TFISRHMCA; FISRHMCAG; ISRHMCAGH; SRHMCAGHN; RHMCAGHNI; HMCAGHNII; MCAGHNIIF; CAGHNIIFF; AGHNIIFFL; GHNIIFFLT; HNIIFFLTP; NIIFFLTPH; IIFFLTPHR; IFFLTPHRH; FFLTPHRHR; FLTPHRHRV; LTPHRHRVS; TPHRHRVSA; PHRHRVSAI; HRHRVSAIN; RHRVSAINN; HRVSAINNF; RVSAINNFC; VSAINNFCQ; SAINNFCQK; AINNFCQKL; INNFCQKLC; NNFCQKLCT; NFCQKLCTF; FCQKLCTFS; CQKLCTFSF; QKLCTFSFL; KLCTFSFLI; LCTFSFLIC; CTFSFLICK; TFSFLICKG; FSFLICKGV; SFLICKGVN; FLICKGVNK; LICKGVNKE; ICKGVNKEY; CKGVNKEYL; KGVNKEYLL; GVNKEYLLY; VNKEYLLYS; NKEYLLYSA; KEYLLYSAL; EYLLYSALT; YLLYSALTR; LLYSALTRD; LYSALTRDP; YSALTRDPY; SALTRDPYH; ALTRDPYHT; LTRDPYHTI; TRDPYHTIE; RDPYHTIEE; DPYHTIEES; PYHTIEESI; YHTIEESIQ; HTIEESIQG; TIEESIQGG; IEESIQGGL; EESIQGGLK; ESIQGGLKE; SIQGGLKEH; IQGGLKEHD; QGGLKEHDF; GGLKEHDFS; GLKEHDFSP; LKEHDFSPE; KEHDFSPEE; EHDFSPEEP; HDFSPEEPE; DFSPEEPEE; FSPEEPEET; SPEEPEETK; PEEPEETKQ; EEPEETKQV; EPEETKQVS; PEETKQVSW; EETKQVSWK; ETKQVSWKL; TKQVSWKLI; KQVSWKLIT; QVSWKLITE; VSWKLITEY; SWKLITEYA; WKLITEYAV; KLITEYAVE; LITEYAVET; ITEYAVETK; TEYAVETKC; EYAVETKCE; YAVETKCED; AVETKCEDV; VETKCEDVF; ETKCEDVFL; TKCEDVFLL; KCEDVFLLL; CEDVFLLLG; EDVFLLLGM; DVFLLLGMY; VFLLLGMYL; FLLLGMYLE; LLLGMYLEF; LLGMYLEFQ; LGMYLEFQY; GMYLEFQYN; MYLEFQYNV; YLEFQYNVE; LEFQYNVEE; EFQYNVEEC; FQYNVEECK; QYNVEECKK; YNVEECKKC; NVEECKKCQ; VEECKKCQK; EECKKCQKK; ECKKCQKKD; CKKCQKKDQ; KKCQKKDQP; KCQKKDQPY; CQKKDQPYH; QKKDQPYHF; KKDQPYHFK; KDQPYHFKY; DQPYHFKYH; QPYHFKYHE; PYHFKYHEK; YHFKYHEKH; HFKYHEKHF; FKYHEKHFA; KYHEKHFAN; YHEKHFANA; HEKHFANAI; EKHFANAII; KHFANAIIF; HFANAIIFA; FANAIIFAE; ANAIIFAES; NAIIFAESK; AIIFAESKN; IIFAESKNQ; IFAESKNQK; FAESKNQKS; AESKNQKSI; ESKNQKSIC; SKNQKSICQ; KNQKSICQQ; NQKSICQQA; QKSICQQAV; KSICQQAVD; SICQQAVDT; ICQQAVDTV; CQQAVDTVL; QQAVDTVLA; QAVDTVLAK; AVDTVLAKK; VDTVLAKKR; DTVLAKKRV; TVLAKKRVD; VLAKKRVDT; LAKKRVDTL; AKKRVDTLH; KKRVDTLHM; KRVDTLHMT; RVDTLHMTR; VDTLHMTRE; DTLHMTREE; TLHMTREEM; LHMTREEML; HMTREEMLT; MTREEMLTE; TREEMLTER; REEMLTERF; EEMLTERFN; EMLTERFNH; MLTERFNHI; LTERFNHIL; TERFNHILD; ERFNHILDK; RFNHILDKM; FNHILDKMD; NHILDKMDL; HILDKMDLI; ILDKMDLIF; LDKMDLIFG; DKMDLIFGA; KMDLIFGAH; MDLIFGAHG; DLIFGAHGN; LIFGAHGNA; IFGAHGNAV; FGAHGNAVL; GAHGNAVLE; AHGNAVLEQ; HGNAVLEQY; GNAVLEQYM; NAVLEQYMA; AVLEQYMAG; VLEQYMAGV; LEQYMAGVA; EQYMAGVAW; QYMAGVAWL; YMAGVAWLH; MAGVAWLHC; AGVAWLHCL; GVAWLHCLL; VAWLHCLLP; AWLHCLLPK; WLHCLLPKM; LHCLLPKMD; HCLLPKMDS; CLLPKMDSV; LLPKMDSVI; LPKMDSVIF; PKMDSVIFD; KMDSVIFDF; MDSVIFDFL; DSVIFDFLH; SVIFDFLHC; VIFDFLHCI; IFDFLHCIV; FDFLHCIVF; DFLHCIVFN; FLHCIVFNV; LHCIVFNVP; HCIVFNVPK; CIVFNVPKR; IVFNVPKRR; VFNVPKRRY; FNVPKRRYW; NVPKRRYWL; VPKRRYWLF; PKRRYWLFK; KRRYWLFKG; RRYWLFKGP; RYWLFKGPI; YWLFKGPID; WLFKGPIDS; LFKGPIDSG; FKGPIDSGK; KGPIDSGKT; GPIDSGKTT; PIDSGKTTL; IDSGKTTLA; DSGKTTLAA; SGKTTLAAG; GKTTLAAGL; KTTLAAGLL; TTLAAGLLD; TLAAGLLDL; LAAGLLDLC; AAGLLDLCG; AGLLDLCGG; GLLDLCGGK; LLDLCGGKA; LDLCGGKAL; DLCGGKALN; LCGGKALNV; CGGKALNVN; GGKALNVNL; GKALNVNLP; KALNVNLPM; ALNVNLPME; LNVNLPMER; NVNLPMERL; VNLPMERLT; NLPMERLTF; LPMERLTFE; PMERLTFEL; MERLTFELG; ERLTFELGV; RLTFELGVA; LTFELGVAI; TFELGVAID; FELGVAIDQ; ELGVAIDQY; LGVAIDQYM; GVAIDQYMV; VAIDQYMVV; AIDQYMVVF; IDQYMVVFE; DQYMVVFED; QYMVVFEDV; YMVVFEDVK; MVVFEDVKG; VVFEDVKGT; VFEDVKGTG; FEDVKGTGA; EDVKGTGAE; DVKGTGAES; VKGTGAESK; KGTGAESKD; GTGAESKDL; TGAESKDLP; GAESKDLPS; AESKDLPSG; ESKDLPSGH; SKDLPSGHG; KDLPSGHGI; DLPSGHGIN; LPSGHGINN; PSGHGINNL; SGHGINNLD; GHGINNLDS; HGINNLDSL; GINNLDSLR; INNLDSLRD; NNLDSLRDY; NLDSLRDYL; LDSLRDYLD; DSLRDYLDG; SLRDYLDGS; LRDYLDGSV; RDYLDGSVK; DYLDGSVKV; YLDGSVKVN; LDGSVKVNL; DGSVKVNLE; GSVKVNLEK; SVKVNLEKK; VKVNLEKKH; KVNLEKKHL; VNLEKKHLN; NLEKKHLNK; LEKKHLNKR; EKKHLNKRT; KKHLNKRTQ; KHLNKRTQI; HLNKRTQIF; LNKRTQIFP; NKRTQIFPP; KRTQIFPPG; RTQIFPPGL; TQIFPPGLV; QIFPPGLVT; IFPPGLVTM; FPPGLVTMN; PPGLVTMNE; PGLVTMNEY; GLVTMNEYP; LVTMNEYPV; VTMNEYPVP; TMNEYPVPK; MNEYPVPKT; NEYPVPKTL; EYPVPKTLQ; YPVPKTLQA; PVPKTLQAR; VPKTLQARF; PKTLQARFV; KTLQARFVR; TLQARFVRQ; LQARFVRQI; QARFVRQID; ARFVRQIDF; RFVRQIDFR; FVRQIDFRP; VRQIDFRPK; RQIDFRPKI; QIDFRPKIY; IDFRPKIYL; DFRPKIYLR; FRPKIYLRK; RPKIYLRKS; PKIYLRKSL; KIYLRKSLQ; IYLRKSLQN; YLRKSLQNS; LRKSLQNSE; RKSLQNSEF; KSLQNSEFL; SLQNSEFLL; LQNSEFLLE; QNSEFLLEK; NSEFLLEKR; SEFLLEKRI; EFLLEKRIL; FLLEKRILQ; LLEKRILQS; LEKRILQSG; EKRILQSGM; KRILQSGMT; RILQSGMTL; ILQSGMTLL; LQSGMTLLL; QSGMTLLLL; SGMTLLLLL; GMTLLLLLI; MTLLLLLIW; TLLLLLIWF; LLLLLIWFR; LLLLIWFRP; LLLIWFRPV; LLIWFRPVA; LIWFRPVAD; IWFRPVADF; WFRPVADFA; FRPVADFAT; RPVADFATD; PVADFATDI; VADFATDIQ; ADFATDIQS; DFATDIQSR; FATDIQSRI; ATDIQSRIV; TDIQSRIVE; DIQSRIVEW; IQSRIVEWK; QSRIVEWKE; SRIVEWKER; RIVEWKERL; IVEWKERLD; VEWKERLDS; EWKERLDSE; WKERLDSEI; KERLDSEIS; ERLDSEISM; RLDSEISMY; LDSEISMYT; DSEISMYTF; SEISMYTFS; EISMYTFSR; ISMYTFSRM; SMYTFSRMK; MYTFSRMKY; YTFSRMKYN; TFSRMKYNI; FSRMKYNIC; SRMKYNICM; RMKYNICMG; MKYNICMGK; KYNICMGKC; YNICMGKCI; NICMGKCIL; ICMGKCILD; CMGKCILDI; MGKCILDIT; GKCILDITR; KCILDITRE; CILDITREE; ILDITREED; LDITREEDS; DITREEDSE; ITREEDSET; TREEDSETE; REEDSETED; EEDSETEDS; EDSETEDSG; DSETEDSGH; SETEDSGHG; ETEDSGHGS; TEDSGHGSS; EDSGHGSST; DSGHGSSTE; SGHGSSTES; GHGSSTESQ; HGSSTESQS; GSSTESQSQ; SSTESQSQC; STESQSQCS; TESQSQCSS; ESQSQCSSQ; SQSQCSSQV; QSQCSSQVS; SQCSSQVSD; QCSSQVSDT; CSSQVSDTS; SSQVSDTSA; SQVSDTSAP; QVSDTSAPA; VSDTSAPAE; SDTSAPAED; DTSAPAEDS; TSAPAEDSQ; SAPAEDSQR; APAEDSQRS; PAEDSQRSD; AEDSQRSDP; EDSQRSDPH; DSQRSDPHS; SQRSDPHSQ; QRSDPHSQE; RSDPHSQEL; SDPHSQELH; DPHSQELHL; PHSQELHLC; HSQELHLCK; SQELHLCKG; QELHLCKGF; ELHLCKGFQ; LHLCKGFQC; HLCKGFQCF; LCKGFQCFK; CKGFQCFKR; KGFQCFKRP; GFQCFKRPK; FQCFKRPKT; QCFKRPKTP; CFKRPKTPP; FKRPKTPPP; KRPKTPPPK; HKLKSGLYK; KLKSGLYKS; LKSGLYKSS; KSGLYKSSI; SGLYKSSIY; MYMYNKSTC; YMYNKSTCL; MYNKSTCLK; YNKSTCLKH; NKSTCLKHF; KSTCLKHFG; STCLKHFGL; TCLKHFGLQ; CLKHFGLQL; LKHFGLQLS; KHFGLQLSL; HFGLQLSLF; FGLQLSLFV; GLQLSLFVN; LQLSLFVNI; QLSLFVNIS; LSLFVNISY; SLFVNISYH; LFVNISYHI; FVNISYHIW; VNISYHIWV; NISYHIWVP; ISYHIWVPW; SYHIWVPWK; YHIWVPWKS; HIWVPWKSF; IWVPWKSFC; WVPWKSFCA; VPWKSFCAI; PWKSFCAIK; WKSFCAIKH; KSFCAIKHP; SFCAIKHPN; FCAIKHPNL; CAIKHPNLF; AIKHPNLFY; IKHPNLFYL; KHPNLFYLG; HPNLFYLGF; PNLFYLGFH; NLFYLGFHT; LFYLGFHTI; FYLGFHTIH; YLGFHTIHR; LGFHTIHRL; GFHTIHRLP; FHTIHRLPI; HTIHRLPIH; TIHRLPIHS; IHRLPIHSL; HRLPIHSLG; RLPIHSLGS; LPIHSLGSP; PIHSLGSPV; IHSLGSPVY; HSLGSPVYK; SLGSPVYKV; LGSPVYKVT; QKGNWVRIL; KGNWVRILY; GNWVRILYR; NWVRILYRS; WVRILYRSF; VRILYRSFS; RILYRSFSQ; ILYRSFSQA; LYRSFSQAD; YRSFSQADL; RSFSQADLK; SFSQADLKI; FSQADLKIS; SQADLKISC; QADLKISCK; ADLKISCKA; DLKISCKAS; LKISCKASP; KISCKASPL; ISCKASPLL; SCKASPLLC; CKASPLLCS; KASPLLCSR; ASPLLCSRA; SPLLCSRAV; PLLCSRAVS; LLCSRAVSK; LCSRAVSKQ; CSRAVSKQA; SRAVSKQAT; RAVSKQATN; AVSKQATNI; VSKQATNIS; SKQATNISS; NIQAISFTK; IQAISFTKR; QAISFTKRP; AISFTKRPH; ISFTKRPHT; SFTKRPHTL; FTKRPHTLF; TKRPHTLFI; QHCGSCVGH; HCGSCVGHM; CGSCVGHMK; GSCVGHMKY; SCVGHMKYW; CVGHMKYWG; VGHMKYWGN; GHMKYWGNI; HMKYWGNIF; MKYWGNIFP; KYWGNIFPS; YWGNIFPSC; WGNIFPSCE; GNIFPSCES; NIFPSCESP; IFPSCESPK; FPSCESPKI; PSCESPKIP; SCESPKIPS; CESPKIPSI; ESPKIPSIF; SPKIPSIFI; PKIPSIFIS; KIPSIFIST; IPSIFISTG; PSIFISTGI; SIFISTGIR; IFISTGIRY; FISTGIRYP; ISTGIRYPA; STGIRYPAL; TGIRYPALN; GIRYPALNW; IRYPALNWI; RYPALNWIS; YPALNWISI; PALNWISIV; ALNWISIVF; LNWISIVFV; NWISIVFVQ; WISIVFVQI; ISIVFVQIG; SIVFVQIGL; IVFVQIGLM; VFVQIGLMV; FVQIGLMVS; VQIGLMVSI; QIGLMVSIH; IGLMVSIHY; GLMVSIHYL; LMVSIHYLG; MVSIHYLGL; VSIHYLGLG; SIHYLGLGC; IHYLGLGCW; HYLGLGCWV; YLGLGCWVF; LGLGCWVFR; GLGCWVFRG; LGCWVFRGY; GCWVFRGYS; CWVFRGYST; WVFRGYSTI; VFRGYSTIR; FRGYSTIRV; RGYSTIRVL; HSLHFQGFS; SLHFQGFST; LHFQGFSTY; HFQGFSTYS; FQGFSTYSK; QGFSTYSKE; GFSTYSKEV; FSTYSKEVE; STYSKEVEI; TYSKEVEIT; YSKEVEITA; SKEVEITAL; KEVEITALN; EVEITALNR; VEITALNRF; EITALNRFS; ITALNRFSS; TALNRFSST; ALNRFSSTM; LNRFSSTML; NRFSSTMLM; RFSSTMLMH; FSSTMLMHF; SSTMLMHFL; PCMKVKHAS; CMKVKHASY; MKVKHASYS; KVKHASYSN; VKHASYSNN; KHASYSNNL; HASYSNNLC; ASYSNNLCL; SYSNNLCLY; YSNNLCLYS; SNNLCLYSY; NNLCLYSYS; NLCLYSYSL; LCLYSYSLP; CLYSYSLPH; LYSYSLPHQ; IGEGNSCCA; GEGNSCCAV; EGNSCCAVT; GNSCCAVTG; NSCCAVTGK; SCCAVTGKH; CCAVTGKHF; CAVTGKHFS; AVTGKHFSL; VTGKHFSLW; TGKHFSLWA; GKHFSLWAI; KHFSLWAIT; HFSLWAITA; FSLWAITAK; SLWAITAKV; LWAITAKVI; WAITAKVIF; AITAKVIFS; ITAKVIFST; TKAPKVFIW; KAPKVFIWI; APKVFIWIP; PKVFIWIPH; KVFIWIPHF; VFIWIPHFW; FIWIPHFWV; EAFYLCNSI; AFYLCNSIY; FYLCNSIYP; YLCNSIYPS; LCNSIYPSF; CNSIYPSFN; NSIYPSFNF; FWHLHGFLW; WHLHGFLWL; HLHGFLWLF; LHGFLWLFG; HGFLWLFGS; GFLWLFGSC; FLWLFGSCP; LWLFGSCPW; WLFGSCPWT; LFGSCPWTL; FGSCPWTLS; GSCPWTLSF; SCPWTLSFS; CPWTLSFSF; PWTLSFSFG; WTLSFSFGW; TLSFSFGWG; LSFSFGWGH; SFSFGWGHL; FSFGWGHLH; SFGWGHLHM; FGWGHLHML; GWGHLHMLQ; WGHLHMLQE; GHLHMLQEQ; HLHMLQEQV; LHMLQEQVL; HMLQEQVLQ; MLQEQVLQS; LQEQVLQSR; QEQVLQSRT; EQVLQSRTG; QVLQSRTGL; VLQSRTGLE; LQSRTGLEV; QSRTGLEVK; SRTGLEVKA; RTGLEVKAT; TGLEVKATS; GLEVKATSI; LEVKATSIE; EVKATSIEE; VKATSIEEQ; KATSIEEQF; ATSIEEQFF; TSIEEQFFD; TLLNVHFVD; LLNVHFVDF; LNVHFVDFL; NVHFVDFLS; VHFVDFLSP; HFVDFLSPF; FVDFLSPFF; VDFLSPFFV; LLLYCQHHL; LLYCQHHLY; LYCQHHLYY; YCQHHLYYK; CQHHLYYKY; QHHLYYKYG; HHLYYKYGQ; HLYYKYGQN; LYYKYGQNV; YYKYGQNVH; YKYGQNVHG; KYGQNVHGY; YGQNVHGYL; GQNVHGYLP; QNVHGYLPF; NVHGYLPFQ; VHGYLPFQL; HGYLPFQLL; GYLPFQLLV; GKDQNNIVE; KDQNNIVEY; DQNNIVEYN; QNNIVEYNY; NNIVEYNYK; NIVEYNYKS; IVEYNYKSL; KIFLFFSAI; IFLFFSAIP; FLFFSAIPV; LFFSAIPVR; FFSAIPVRL; QKYLHQETE; KYLHQETEY; YLHQETEYH; LHQETEYHS; HQETEYHST; QETEYHSTH; ETEYHSTHL; TEYHSTHLG; TIPKPCLIA; IPKPCLIAD; PKPCLIADR; KPCLIADRG; PCLIADRGL; CLIADRGLQ; LIADRGLQW; IADRGLQWK; ADRGLQWKL; DRGLQWKLC; RGLQWKLCD; GLQWKLCDP; LQWKLCDPN; QWKLCDPNH; WKLCDPNHQ; KLCDPNHQR; LCDPNHQRT; CDPNHQRTY; DPNHQRTYT; PNHQRTYTL; NHQRTYTLL; HQRTYTLLE; QRTYTLLEL; RTYTLLELR; TYTLLELRN; QFELKQQTQ; FELKQQTQQ; PQEHQQLQH; QEHQQLQHM; EHQQLQHMF; HQQLQHMFE; QQLQHMFEE; QLQHMFEEL; LQHMFEELG; QHMFEELGL; PLRYLLCPL; LRYLLCPLQ; QQQPPQQQF; QQPPQQQFQ; QPPQQQFQP; PPQQQFQPL; PQQQFQPLK; QQQFQPLKI; QQFQPLKIL; QFQPLKILW; FQPLKILWQ; QPLKILWQQ; PLKILWQQQ; LKILWQQQP; KILWQQQPQ; ILWQQQPQI; LWQQQPQIH; WQQQPQIHW; QQQPQIHWQ; QQPQIHWQL; QPQIHWQLG; PQIHWQLGP; QIHWQLGPP; IHWQLGPPK; HWQLGPPKV; WQLGPPKVL; QLGPPKVLE; LGPPKVLEQ; GPPKVLEQH; PPKVLEQHP; TWKYKKKGI; WKYKKKGIT; KYKKKGITY; YKKKGITYL; KKKGITYLG; KKGITYLGV; KGITYLGVF; GITYLGVFY; ITYLGVFYR; TYLGVFYRV; YLGVFYRVF; LGVFYRVFY; GVFYRVFYS; VFYRVFYSR; SSGTFVFPV; SGTFVFPVY; GTFVFPVYT; TFVFPVYTV; FVFPVYTVF; VFPVYTVFT; FPVYTVFTS; PVYTVFTST; VYTVFTSTK; YTVFTSTKF; TVFTSTKFQ; VFTSTKFQQ; FTSTKFQQK; TSTKFQQKL; NKNKNPLSS; KNKNPLSSF; NKNPLSSFF; KNPLSSFFC; NPLSSFFCS; PLSSFFCSS; LSSFFCSSP; SSFFCSSPG; SFFCSSPGF; FFCSSPGFT; FCSSPGFTN; CSSPGFTNF; SSPGFTNFH; QLAQNHGLC; LAQNHGLCP; AQNHGLCPV; LGTRPRFLG; GTRPRFLGS; TRPRFLGSQ; RPRFLGSQN; PRFLGSQNM; RFLGSQNMS; FLGSQNMSV; LGSQNMSVM; GSQNMSVMH; SQNMSVMHF; QNMSVMHFP; NMSVMHFPS; GHGLAAFHG; AAPPCESCT; APPCESCTF; PPCESCTFL; PCESCTFLP; CESCTFLPE; ESCTFLPEV; SCTFLPEVM; CTFLPEVMV; TFLPEVMVW; FLPEVMVWL; LPEVMVWLH; PEVMVWLHS; EVMVWLHSP; VMVWLHSPV; MVWLHSPVS; VWLHSPVSH; WLHSPVSHA; LHSPVSHAL; HSPVSHALS; SPVSHALSF; PVSHALSFL; VSHALSFLR; SHALSFLRS; HALSFLRSW; ALSFLRSWF; LSFLRSWFG; SFLRSWFGC; FLRSWFGCI; LRSWFGCIP; RSWFGCIPW; SWFGCIPWV; WFGCIPWVS; FGCIPWVSS; GCIPWVSSS; CIPWVSSSS; IPWVSSSSL; PWVSSSSLW; WVSSSSLWP; VSSSSLWPF; SSSSLWPFF; SSSLWPFFL; YIRGRGRLC; IRGRGRLCL; RGRGRLCLH; GRGRLCLHP; RGRLCLHPF; GRLCLHPFS; RLCLHPFSQ; LCLHPFSQV; CLHPFSQVV; LHPFSQVVR; HPFSQVVRV; PFSQVVRVW; FSQVVRVWR; SQVVRVWRL; QVVRVWRLF; VVRVWRLFL; VRVWRLFLR; RVWRLFLRP; VWRLFLRPS; WRLFLRPSK; RLFLRPSKT; LFLRPSKTI; FLRPSKTIW; LRPSKTIWG; RPSKTIWGN; PSKTIWGNP; SKTIWGNPY; KTIWGNPYS; TIWGNPYSF; IWGNPYSFA; WGNPYSFAI; GNPYSFAIF; NPYSFAIFA; PYSFAIFAK 10 mers: QGRIHGAHGP; GRIHGAHGPF; RIHGAHGPFR; IHGAHGPFRP; KSCLGKSSLN; SCLGKSSLNE; CLGKSSLNEK; LGKSSLNEKS; GKSSLNEKSL; KSSLNEKSLF; SSLNEKSLFK; SLNEKSLFKE; LNEKSLFKEV; KNGAGCKGSS; NGAGCKGSSS; GAGCKGSSSA; FSSLPRYPVL; SSLPRYPVLQ; SLPRYPVLQG; LPRYPVLQGM; PRYPVLQGMA; RYPVLQGMAY; YPVLQGMAYL; PVLQGMAYLF; VLQGMAYLFQ; LQGMAYLFQK; QGMAYLFQKA; GMAYLFQKAF; MAYLFQKAFC; AYLFQKAFCA; YLFQKAFCAL; LFQKAFCALP; FQKAFCALPL; QKAFCALPLH; KAFCALPLHA; AFCALPLHAM; FCALPLHAMS; CALPLHAMSA; KIFKKRALGL; IFKKRALGLD; FKKRALGLDR; KKRALGLDRL; KRALGLDRLL; RALGLDRLLL; ALGLDRLLLH; LLHTVVWLRP; LHTVVWLRPN; RNSAMVGPNN; NSAMVGPNNW; SAMVGPNNWR; AMVGPNNWRN; MVGPNNWRNS; VGPNNWRNSL; GPNNWRNSLQ; PNNWRNSLQR; NNWRNSLQRS; NWRNSLQRSK; WRNSLQRSKA; RNSLQRSKAL; NSLQRSKALR; INNKILKGPK; VPTYGTEEWE; PTYGTEEWES; TYGTEEWESW; YGTEEWESWW; GTEEWESWWS; TEEWESWWSS; EEWESWWSSF; EWESWWSSFN; WESWWSSFNE; ESWWSSFNEK; SWWSSFNEKW; WWSSFNEKWD; WSSFNEKWDE; SSFNEKWDED; SFNEKWDEDL; FNEKWDEDLF; NEKWDEDLFC; EKWDEDLFCH; KWDEDLFCHE; WDEDLFCHED; DEDLFCHEDM; EDLFCHEDMF; DLFCHEDMFA; LFCHEDMFAS; FCHEDMFASD; CHEDMFASDE; HEDMFASDEE; EDMFASDEEA; DMFASDEEAT; MFASDEEATA; FASDEEATAD; ASDEEATADS; SDEEATADSQ; DEEATADSQH; EEATADSQHS; EATADSQHST; ATADSQHSTP; TADSQHSTPP; ADSQHSTPPK; DSQHSTPPKK; SQHSTPPKKK; QHSTPPKKKR; HSTPPKKKRK; STPPKKKRKV; TPPKKKRKVE; PPKKKRKVED; PKKKRKVEDP; KKKRKVEDPK; KKRKVEDPKD; KRKVEDPKDF; RKVEDPKDFP; KVEDPKDFPS; VEDPKDFPSD; EDPKDFPSDL; DPKDFPSDLH; PKDFPSDLHQ; KDFPSDLHQF; DFPSDLHQFL; FPSDLHQFLS; PSDLHQFLSQ; SDLHQFLSQA; DLHQFLSQAV; LHQFLSQAVF; HQFLSQAVFS; QFLSQAVFSN; FLSQAVFSNR; LSQAVFSNRT; SQAVFSNRTL; QAVFSNRTLA; AVFSNRTLAC; VFSNRTLACF; FSNRTLACFA; SNRTLACFAV; NRTLACFAVY; RTLACFAVYT; TLACFAVYTT; LACFAVYTTK; ACFAVYTTKE; CFAVYTTKEK; FAVYTTKEKA; AVYTTKEKAQ; VYTTKEKAQI; YTTKEKAQIL; TTKEKAQILY; TKEKAQILYK; KEKAQILYKK; EKAQILYKKL; KAQILYKKLM; AQILYKKLME; QILYKKLMEK; ILYKKLMEKY; LYKKLMEKYS; YKKLMEKYSV; KKLMEKYSVT; KLMEKYSVTF; LMEKYSVTFI; MEKYSVTFIS; EKYSVTFISR; KYSVTFISRH; YSVTFISRHM; SVTFISRHMC; VTFISRHMCA; TFISRHMCAG; FISRHMCAGH; ISRHMCAGHN; SRHMCAGHNI; RHMCAGHNII; HMCAGHNIIF; MCAGHNIIFF; CAGHNIIFFL; AGHNIIFFLT; GHNIIFFLTP; HNIIFFLTPH; NIIFFLTPHR; IIFFLTPHRH; IFFLTPHRHR; FFLTPHRHRV; FLTPHRHRVS; LTPHRHRVSA; TPHRHRVSAI; PHRHRVSAIN; HRHRVSAINN; RHRVSAINNF; HRVSAINNFC; RVSAINNFCQ; VSAINNFCQK; SAINNFCQKL; AINNFCQKLC; INNFCQKLCT; NNFCQKLCTF; NFCQKLCTFS; FCQKLCTFSF; CQKLCTFSFL; QKLCTFSFLI; KLCTFSFLIC; LCTFSFLICK; CTFSFLICKG; TFSFLICKGV; FSFLICKGVN; SFLICKGVNK; FLICKGVNKE; LICKGVNKEY; ICKGVNKEYL; CKGVNKEYLL; KGVNKEYLLY; GVNKEYLLYS; VNKEYLLYSA; NKEYLLYSAL; KEYLLYSALT; EYLLYSALTR; YLLYSALTRD; LLYSALTRDP; LYSALTRDPY; YSALTRDPYH; SALTRDPYHT; ALTRDPYHTI; LTRDPYHTIE; TRDPYHTIEE; RDPYHTIEES; DPYHTIEESI; PYHTIEESIQ; YHTIEESIQG; HTIEESIQGG; TIEESIQGGL; IEESIQGGLK; EESIQGGLKE; ESIQGGLKEH; SIQGGLKEHD; IQGGLKEHDF; QGGLKEHDFS; GGLKEHDFSP; GLKEHDFSPE; LKEHDFSPEE; KEHDFSPEEP; EHDFSPEEPE; HDFSPEEPEE; DFSPEEPEET; FSPEEPEETK; SPEEPEETKQ; PEEPEETKQV; EEPEETKQVS; EPEETKQVSW; PEETKQVSWK; EETKQVSWKL; ETKQVSWKLI; TKQVSWKLIT; KQVSWKLITE; QVSWKLITEY; VSWKLITEYA; SWKLITEYAV; WKLITEYAVE; KLITEYAVET; LITEYAVETK; ITEYAVETKC; TEYAVETKCE; EYAVETKCED; YAVETKCEDV; AVETKCEDVF; VETKCEDVFL; ETKCEDVFLL; TKCEDVFLLL; KCEDVFLLLG; CEDVFLLLGM; EDVFLLLGMY; DVFLLLGMYL; VFLLLGMYLE; FLLLGMYLEF; LLLGMYLEFQ; LLGMYLEFQY; LGMYLEFQYN; GMYLEFQYNV; MYLEFQYNVE; YLEFQYNVEE; LEFQYNVEEC; EFQYNVEECK; FQYNVEECKK; QYNVEECKKC; YNVEECKKCQ; NVEECKKCQK; VEECKKCQKK; EECKKCQKKD; ECKKCQKKDQ; CKKCQKKDQP; KKCQKKDQPY; KCQKKDQPYH; CQKKDQPYHF; QKKDQPYHFK; KKDQPYHFKY; KDQPYHFKYH; DQPYHFKYHE; QPYHFKYHEK; PYHFKYHEKH; YHFKYHEKHF; HFKYHEKHFA; FKYHEKHFAN; KYHEKHFANA; YHEKHFANAI; HEKHFANAII; EKHFANAIIF; KHFANAIIFA; HFANAIIFAE; FANAIIFAES; ANAIIFAESK; NAIIFAESKN; AIIFAESKNQ; IIFAESKNQK; IFAESKNQKS; FAESKNQKSI; AESKNQKSIC; ESKNQKSICQ; SKNQKSICQQ; KNQKSICQQA; NQKSICQQAV; QKSICQQAVD; KSICQQAVDT; SICQQAVDTV; ICQQAVDTVL; CQQAVDTVLA; QQAVDTVLAK; QAVDTVLAKK; AVDTVLAKKR; VDTVLAKKRV; DTVLAKKRVD; TVLAKKRVDT; VLAKKRVDTL; LAKKRVDTLH; AKKRVDTLHM; KKRVDTLHMT; KRVDTLHMTR; RVDTLHMTRE; VDTLHMTREE; DTLHMTREEM; TLHMTREEML; LHMTREEMLT; HMTREEMLTE; MTREEMLTER; TREEMLTERF; REEMLTERFN; EEMLTERFNH; EMLTERFNHI; MLTERFNHIL; LTERFNHILD; TERFNHILDK; ERFNHILDKM; RFNHILDKMD; FNHILDKMDL; NHILDKMDLI; HILDKMDLIF; ILDKMDLIFG; LDKMDLIFGA; DKMDLIFGAH; KMDLIFGAHG; MDLIFGAHGN; DLIFGAHGNA; LIFGAHGNAV; IFGAHGNAVL; FGAHGNAVLE; GAHGNAVLEQ; AHGNAVLEQY; HGNAVLEQYM; GNAVLEQYMA; NAVLEQYMAG; AVLEQYMAGV; VLEQYMAGVA; LEQYMAGVAW; EQYMAGVAWL; QYMAGVAWLH; YMAGVAWLHC; MAGVAWLHCL; AGVAWLHCLL; GVAWLHCLLP; VAWLHCLLPK; AWLHCLLPKM; WLHCLLPKMD; LHCLLPKMDS; HCLLPKMDSV; CLLPKMDSVI; LLPKMDSVIF; LPKMDSVIFD; PKMDSVIFDF; KMDSVIFDFL; MDSVIFDFLH; DSVIFDFLHC; SVIFDFLHCI; VIFDFLHCIV; IFDFLHCIVF; FDFLHCIVFN; DFLHCIVFNV; FLHCIVFNVP; LHCIVFNVPK; HCIVFNVPKR; CIVFNVPKRR; IVFNVPKRRY; VFNVPKRRYW; FNVPKRRYWL; NVPKRRYWLF; VPKRRYWLFK; PKRRYWLFKG; KRRYWLFKGP; RRYWLFKGPI; RYWLFKGPID; YWLFKGPIDS; WLFKGPIDSG; LFKGPIDSGK; FKGPIDSGKT; KGPIDSGKTT; GPIDSGKTTL; PIDSGKTTLA; IDSGKTTLAA; DSGKTTLAAG; SGKTTLAAGL; GKTTLAAGLL; KTTLAAGLLD; TTLAAGLLDL; TLAAGLLDLC; LAAGLLDLCG; AAGLLDLCGG; AGLLDLCGGK; GLLDLCGGKA; LLDLCGGKAL; LDLCGGKALN; DLCGGKALNV; LCGGKALNVN; CGGKALNVNL; GGKALNVNLP; GKALNVNLPM; KALNVNLPME; ALNVNLPMER; LNVNLPMERL; NVNLPMERLT; VNLPMERLTF; NLPMERLTFE; LPMERLTFEL; PMERLTFELG; MERLTFELGV; ERLTFELGVA; RLTFELGVAI; LTFELGVAID; TFELGVAIDQ; FELGVAIDQY; ELGVAIDQYM; LGVAIDQYMV; GVAIDQYMVV; VAIDQYMVVF; AIDQYMVVFE; IDQYMVVFED; DQYMVVFEDV; QYMVVFEDVK; YMVVFEDVKG; MVVFEDVKGT; VVFEDVKGTG; VFEDVKGTGA; FEDVKGTGAE; EDVKGTGAES; DVKGTGAESK; VKGTGAESKD; KGTGAESKDL; GTGAESKDLP; TGAESKDLPS; GAESKDLPSG; AESKDLPSGH; ESKDLPSGHG; SKDLPSGHGI; KDLPSGHGIN; DLPSGHGINN; LPSGHGINNL; PSGHGINNLD; SGHGINNLDS; GHGINNLDSL; HGINNLDSLR; GINNLDSLRD; INNLDSLRDY; NNLDSLRDYL; NLDSLRDYLD; LDSLRDYLDG; DSLRDYLDGS; SLRDYLDGSV; LRDYLDGSVK; RDYLDGSVKV; DYLDGSVKVN; YLDGSVKVNL; LDGSVKVNLE; DGSVKVNLEK; GSVKVNLEKK; SVKVNLEKKH; VKVNLEKKHL; KVNLEKKHLN; VNLEKKHLNK; NLEKKHLNKR; LEKKHLNKRT; EKKHLNKRTQ; KKHLNKRTQI; KHLNKRTQIF; HLNKRTQIFP; LNKRTQIFPP; NKRTQIFPPG; KRTQIFPPGL; RTQIFPPGLV; TQIFPPGLVT; QIFPPGLVTM; IFPPGLVTMN; FPPGLVTMNE; PPGLVTMNEY; PGLVTMNEYP; GLVTMNEYPV; LVTMNEYPVP; VTMNEYPVPK; TMNEYPVPKT; MNEYPVPKTL; NEYPVPKTLQ; EYPVPKTLQA; YPVPKTLQAR; PVPKTLQARF; VPKTLQARFV; PKTLQARFVR; KTLQARFVRQ; TLQARFVRQI; LQARFVRQID; QARFVRQIDF; ARFVRQIDFR; RFVRQIDFRP; FVRQIDFRPK; VRQIDFRPKI; RQIDFRPKIY; QIDFRPKIYL; IDFRPKIYLR; DFRPKIYLRK; FRPKIYLRKS; RPKIYLRKSL; PKIYLRKSLQ; KIYLRKSLQN; IYLRKSLQNS; YLRKSLQNSE; LRKSLQNSEF; RKSLQNSEFL; KSLQNSEFLL; SLQNSEFLLE; LQNSEFLLEK; QNSEFLLEKR; NSEFLLEKRI; SEFLLEKRIL; EFLLEKRILQ; FLLEKRILQS; LLEKRILQSG; LEKRILQSGM; EKRILQSGMT; KRILQSGMTL; RILQSGMTLL; ILQSGMTLLL; LQSGMTLLLL; QSGMTLLLLL; SGMTLLLLLI; GMTLLLLLIW; MTLLLLLIWF; TLLLLLIWFR; LLLLLIWFRP; LLLLIWFRPV; LLLIWFRPVA; LLIWFRPVAD; LIWFRPVADF; IWFRPVADFA; WFRPVADFAT; FRPVADFATD; RPVADFATDI; PVADFATDIQ; VADFATDIQS; ADFATDIQSR; DFATDIQSRI; FATDIQSRIV; ATDIQSRIVE; TDIQSRIVEW; DIQSRIVEWK; IQSRIVEWKE; QSRIVEWKER; SRIVEWKERL; RIVEWKERLD; IVEWKERLDS; VEWKERLDSE; EWKERLDSEI; WKERLDSEIS; KERLDSEISM; ERLDSEISMY; RLDSEISMYT; LDSEISMYTF; DSEISMYTFS; SEISMYTFSR; EISMYTFSRM; ISMYTFSRMK; SMYTFSRMKY; MYTFSRMKYN; YTFSRMKYNI; TFSRMKYNIC; FSRMKYNICM; SRMKYNICMG; RMKYNICMGK; MKYNICMGKC; KYNICMGKCI; YNICMGKCIL; NICMGKCILD; ICMGKCILDI; CMGKCILDIT; MGKCILDITR; GKCILDITRE; KCILDITREE; CILDITREED; ILDITREEDS; LDITREEDSE; DITREEDSET; ITREEDSETE; TREEDSETED; REEDSETEDS; EEDSETEDSG; EDSETEDSGH; DSETEDSGHG; SETEDSGHGS; ETEDSGHGSS; TEDSGHGSST; EDSGHGSSTE; DSGHGSSTES; SGHGSSTESQ; GHGSSTESQS; HGSSTESQSQ; GSSTESQSQC; SSTESQSQCS; STESQSQCSS; TESQSQCSSQ; ESQSQCSSQV; SQSQCSSQVS; QSQCSSQVSD; SQCSSQVSDT; QCSSQVSDTS; CSSQVSDTSA; SSQVSDTSAP; SQVSDTSAPA; QVSDTSAPAE; VSDTSAPAED; SDTSAPAEDS; DTSAPAEDSQ; TSAPAEDSQR; SAPAEDSQRS; APAEDSQRSD; PAEDSQRSDP; AEDSQRSDPH; EDSQRSDPHS; DSQRSDPHSQ; SQRSDPHSQE; QRSDPHSQEL; RSDPHSQELH; SDPHSQELHL; DPHSQELHLC; PHSQELHLCK; HSQELHLCKG; SQELHLCKGF; QELHLCKGFQ; ELHLCKGFQC; LHLCKGFQCF; HLCKGFQCFK; LCKGFQCFKR; CKGFQCFKRP; KGFQCFKRPK; GFQCFKRPKT; FQCFKRPKTP; QCFKRPKTPP; CFKRPKTPPP; FKRPKTPPPK; HKLKSGLYKS; KLKSGLYKSS; LKSGLYKSSI; KSGLYKSSIY; MYMYNKSTCL; YMYNKSTCLK; MYNKSTCLKH; YNKSTCLKHF; NKSTCLKHFG; KSTCLKHFGL; STCLKHFGLQ; TCLKHFGLQL; CLKHFGLQLS; LKHFGLQLSL; KHFGLQLSLF; HFGLQLSLFV; FGLQLSLFVN; GLQLSLFVNI; LQLSLFVNIS; QLSLFVNISY; LSLFVNISYH; SLFVNISYHI; LFVNISYHIW; FVNISYHIWV; VNISYHIWVP; NISYHIWVPW; ISYHIWVPWK; SYHIWVPWKS; YHIWVPWKSF; HIWVPWKSFC; IWVPWKSFCA; WVPWKSFCAI; VPWKSFCAIK; PWKSFCAIKH; WKSFCAIKHP; KSFCAIKHPN; SFCAIKHPNL; FCAIKHPNLF; CAIKHPNLFY; AIKHPNLFYL; IKHPNLFYLG; KHPNLFYLGF; HPNLFYLGFH; PNLFYLGFHT; NLFYLGFHTI; LFYLGFHTIH; FYLGFHTIHR; YLGFHTIHRL; LGFHTIHRLP; GFHTIHRLPI; FHTIHRLPIH; HTIHRLPIHS; TIHRLPIHSL; IHRLPIHSLG; HRLPIHSLGS; RLPIHSLGSP; LPIHSLGSPV; PIHSLGSPVY; IHSLGSPVYK; HSLGSPVYKV; SLGSPVYKVT; QKGNWVRILY; KGNWVRILYR; GNWVRILYRS; NWVRILYRSF; WVRILYRSFS; VRILYRSFSQ; RILYRSFSQA; ILYRSFSQAD; LYRSFSQADL; YRSFSQADLK; RSFSQADLKI; SFSQADLKIS; FSQADLKISC; SQADLKISCK; QADLKISCKA; ADLKISCKAS; DLKISCKASP; LKISCKASPL; KISCKASPLL; ISCKASPLLC; SCKASPLLCS; CKASPLLCSR; KASPLLCSRA; ASPLLCSRAV; SPLLCSRAVS; PLLCSRAVSK; LLCSRAVSKQ; LCSRAVSKQA; CSRAVSKQAT; SRAVSKQATN; RAVSKQATNI; AVSKQATNIS; VSKQATNISS; NIQAISFTKR; IQAISFTKRP; QAISFTKRPH; AISFTKRPHT; ISFTKRPHTL; SFTKRPHTLF; FTKRPHTLFI; QHCGSCVGHM; HCGSCVGHMK; CGSCVGHMKY; GSCVGHMKYW; SCVGHMKYWG; CVGHMKYWGN; VGHMKYWGNI; GHMKYWGNIF; HMKYWGNIFP; MKYWGNIFPS; KYWGNIFPSC; YWGNIFPSCE; WGNIFPSCES; GNIFPSCESP; NIFPSCESPK; IFPSCESPKI; FPSCESPKIP; PSCESPKIPS; SCESPKIPSI; CESPKIPSIF; ESPKIPSIFI; SPKIPSIFIS; PKIPSIFIST; KIPSIFISTG; IPSIFISTGI; PSIFISTGIR; SIFISTGIRY; IFISTGIRYP; FISTGIRYPA; ISTGIRYPAL; STGIRYPALN; TGIRYPALNW; GIRYPALNWI; IRYPALNWIS; RYPALNWISI; YPALNWISIV; PALNWISIVF; ALNWISIVFV; LNWISIVFVQ; NWISIVFVQI; WISIVFVQIG; ISIVFVQIGL; SIVFVQIGLM; IVFVQIGLMV; VFVQIGLMVS; FVQIGLMVSI; VQIGLMVSIH; QIGLMVSIHY; IGLMVSIHYL; GLMVSIHYLG; LMVSIHYLGL; MVSIHYLGLG; VSIHYLGLGC; SIHYLGLGCW; IHYLGLGCWV; HYLGLGCWVF; YLGLGCWVFR; LGLGCWVFRG; GLGCWVFRGY; LGCWVFRGYS; GCWVFRGYST; CWVFRGYSTI; WVFRGYSTIR; VFRGYSTIRV; FRGYSTIRVL; HSLHFQGFST; SLHFQGFSTY; LHFQGFSTYS; HFQGFSTYSK; FQGFSTYSKE; QGFSTYSKEV; GFSTYSKEVE; FSTYSKEVEI; STYSKEVEIT; TYSKEVEITA; YSKEVEITAL; SKEVEITALN; KEVEITALNR; EVEITALNRF; VEITALNRFS; EITALNRFSS; ITALNRFSST; TALNRFSSTM; ALNRFSSTML; LNRFSSTMLM; NRFSSTMLMH; RFSSTMLMHF; FSSTMLMHFL; PCMKVKHASY; CMKVKHASYS; MKVKHASYSN; KVKHASYSNN; VKHASYSNNL; KHASYSNNLC; HASYSNNLCL; ASYSNNLCLY; SYSNNLCLYS; YSNNLCLYSY; SNNLCLYSYS; NNLCLYSYSL; NLCLYSYSLP; LCLYSYSLPH; CLYSYSLPHQ; IGEGNSCCAV; GEGNSCCAVT; EGNSCCAVTG; GNSCCAVTGK; NSCCAVTGKH; SCCAVTGKHF; CCAVTGKHFS; CAVTGKHFSL; AVTGKHFSLW; VTGKHFSLWA; TGKHFSLWAI; GKHFSLWAIT; KHFSLWAITA; HFSLWAITAK; FSLWAITAKV; SLWAITAKVI; LWAITAKVIF; WAITAKVIFS; AITAKVIFST; TKAPKVFIWI; KAPKVFIWIP; APKVFIWIPH; PKVFIWIPHF; KVFIWIPHFW; VFIWIPHFWV; EAFYLCNSIY; AFYLCNSIYP; FYLCNSIYPS; YLCNSIYPSF; LCNSIYPSFN; CNSIYPSFNF; FWHLHGFLWL; WHLHGFLWLF; HLHGFLWLFG; LHGFLWLFGS; HGFLWLFGSC; GFLWLFGSCP; FLWLFGSCPW; LWLFGSCPWT; WLFGSCPWTL; LFGSCPWTLS; FGSCPWTLSF; GSCPWTLSFS; SCPWTLSFSF; CPWTLSFSFG; PWTLSFSFGW; WTLSFSFGWG; TLSFSFGWGH; LSFSFGWGHL; SFSFGWGHLH; FSFGWGHLHM; SFGWGHLHML; FGWGHLHMLQ; GWGHLHMLQE; WGHLHMLQEQ; GHLHMLQEQV; HLHMLQEQVL; LHMLQEQVLQ; HMLQEQVLQS; MLQEQVLQSR; LQEQVLQSRT; QEQVLQSRTG; EQVLQSRTGL; QVLQSRTGLE; VLQSRTGLEV; LQSRTGLEVK; QSRTGLEVKA; SRTGLEVKAT; RTGLEVKATS; TGLEVKATSI; GLEVKATSIE; LEVKATSIEE; EVKATSIEEQ; VKATSIEEQF; KATSIEEQFF; ATSIEEQFFD; TLLNVHFVDF; LLNVHFVDFL; LNVHFVDFLS; NVHFVDFLSP; VHFVDFLSPF; HFVDFLSPFF; FVDFLSPFFV; LLLYCQHHLY; LLYCQHHLYY; LYCQHHLYYK; YCQHHLYYKY; CQHHLYYKYG; QHHLYYKYGQ; HHLYYKYGQN; HLYYKYGQNV; LYYKYGQNVH; YYKYGQNVHG; YKYGQNVHGY; KYGQNVHGYL; YGQNVHGYLP; GQNVHGYLPF; QNVHGYLPFQ; NVHGYLPFQL; VHGYLPFQLL; HGYLPFQLLV; GKDQNNIVEY; KDQNNIVEYN; DQNNIVEYNY; QNNIVEYNYK; NNIVEYNYKS; NIVEYNYKSL; KIFLFFSAIP; IFLFFSAIPV; FLFFSAIPVR; LFFSAIPVRL; QKYLHQETEY; KYLHQETEYH; YLHQETEYHS; LHQETEYHST; HQETEYHSTH; QETEYHSTHL; ETEYHSTHLG; TIPKPCLIAD; IPKPCLIADR; PKPCLIADRG; KPCLIADRGL; PCLIADRGLQ; CLIADRGLQW; LIADRGLQWK; IADRGLQWKL; ADRGLQWKLC; DRGLQWKLCD; RGLQWKLCDP; GLQWKLCDPN; LQWKLCDPNH; QWKLCDPNHQ; WKLCDPNHQR; KLCDPNHQRT; LCDPNHQRTY; CDPNHQRTYT; DPNHQRTYTL; PNHQRTYTLL; NHQRTYTLLE; HQRTYTLLEL; QRTYTLLELR; RTYTLLELRN; QFELKQQTQQ; PQEHQQLQHM; QEHQQLQHMF; EHQQLQHMFE; HQQLQHMFEE; QQLQHMFEEL; QLQHMFEELG; LQHMFEELGL; PLRYLLCPLQ; QQQPPQQQFQ; QQPPQQQFQP; QPPQQQFQPL; PPQQQFQPLK; PQQQFQPLKI; QQQFQPLKIL; QQFQPLKILW; QFQPLKILWQ; FQPLKILWQQ; QPLKILWQQQ; PLKILWQQQP; LKILWQQQPQ; KILWQQQPQI; ILWQQQPQIH; LWQQQPQIHW; WQQQPQIHWQ; QQQPQIHWQL; QQPQIHWQLG; QPQIHWQLGP; PQIHWQLGPP; QIHWQLGPPK; IHWQLGPPKV; HWQLGPPKVL; WQLGPPKVLE; QLGPPKVLEQ; LGPPKVLEQH; GPPKVLEQHP; TWKYKKKGIT; WKYKKKGITY; KYKKKGITYL; YKKKGITYLG; KKKGITYLGV; KKGITYLGVF; KGITYLGVFY; GITYLGVFYR; ITYLGVFYRV; TYLGVFYRVF; YLGVFYRVFY; LGVFYRVFYS; GVFYRVFYSR; SSGTFVFPVY; SGTFVFPVYT; GTFVFPVYTV; TFVFPVYTVF; FVFPVYTVFT; VFPVYTVFTS; FPVYTVFTST; PVYTVFTSTK; VYTVFTSTKF; YTVFTSTKFQ; TVFTSTKFQQ; VFTSTKFQQK; FTSTKFQQKL; NKNKNPLSSF; KNKNPLSSFF; NKNPLSSFFC; KNPLSSFFCS; NPLSSFFCSS; PLSSFFCSSP; LSSFFCSSPG; SSFFCSSPGF; SFFCSSPGFT; FFCSSPGFTN; FCSSPGFTNF; CSSPGFTNFH; QLAQNHGLCP; LAQNHGLCPV; LGTRPRFLGS; GTRPRFLGSQ; TRPRFLGSQN; RPRFLGSQNM; PRFLGSQNMS; RFLGSQNMSV; FLGSQNMSVM; LGSQNMSVMH; GSQNMSVMHF; SQNMSVMHFP; QNMSVMHFPS; AAPPCESCTF; APPCESCTFL; PPCESCTFLP; PCESCTFLPE; CESCTFLPEV; ESCTFLPEVM; SCTFLPEVMV; CTFLPEVMVW; TFLPEVMVWL; FLPEVMVWLH; LPEVMVWLHS; PEVMVWLHSP; EVMVWLHSPV; VMVWLHSPVS; MVWLHSPVSH; VWLHSPVSHA; WLHSPVSHAL; LHSPVSHALS; HSPVSHALSF; SPVSHALSFL; PVSHALSFLR; VSHALSFLRS; SHALSFLRSW; HALSFLRSWF; ALSFLRSWFG; LSFLRSWFGC; SFLRSWFGCI; FLRSWFGCIP; LRSWFGCIPW; RSWFGCIPWV; SWFGCIPWVS; WFGCIPWVSS; FGCIPWVSSS; GCIPWVSSSS; CIPWVSSSSL; IPWVSSSSLW; PWVSSSSLWP; WVSSSSLWPF; VSSSSLWPFF; SSSSLWPFFL; YIRGRGRLCL; IRGRGRLCLH; RGRGRLCLHP; GRGRLCLHPF; RGRLCLHPFS; GRLCLHPFSQ; RLCLHPFSQV; LCLHPFSQVV; CLHPFSQVVR; LHPFSQVVRV; HPFSQVVRVW; PFSQVVRVWR; FSQVVRVWRL; SQVVRVWRLF; QVVRVWRLFL; VVRVWRLFLR; VRVWRLFLRP; RVWRLFLRPS; VWRLFLRPSK; WRLFLRPSKT; RLFLRPSKTI; LFLRPSKTIW; FLRPSKTIWG; LRPSKTIWGN; RPSKTIWGNP; PSKTIWGNPY; SKTIWGNPYS; KTIWGNPYSF; TIWGNPYSFA; IWGNPYSFAI; WGNPYSFAIF; GNPYSFAIFA; NPYSFAIFAK 11 mers: QGRIHGAHGPF; GRIHGAHGPFR; RIHGAHGPFRP; KSCLGKSSLNE; SCLGKSSLNEK; CLGKSSLNEKS; LGKSSLNEKSL; GKSSLNEKSLF; KSSLNEKSLFK; SSLNEKSLFKE; SLNEKSLFKEV; KNGAGCKGSSS; NGAGCKGSSSA; FSSLPRYPVLQ; SSLPRYPVLQG; SLPRYPVLQGM; LPRYPVLQGMA; PRYPVLQGMAY; RYPVLQGMAYL; YPVLQGMAYLF; PVLQGMAYLFQ; VLQGMAYLFQK; LQGMAYLFQKA; QGMAYLFQKAF; GMAYLFQKAFC; MAYLFQKAFCA; AYLFQKAFCAL; YLFQKAFCALP; LFQKAFCALPL; FQKAFCALPLH; QKAFCALPLHA; KAFCALPLHAM; AFCALPLHAMS; FCALPLHAMSA; KIFKKRALGLD; IFKKRALGLDR; FKKRALGLDRL; KKRALGLDRLL; KRALGLDRLLL; RALGLDRLLLH; LLHTVVWLRPN; RNSAMVGPNNW; NSAMVGPNNWR; SAMVGPNNWRN; AMVGPNNWRNS; MVGPNNWRNSL; VGPNNWRNSLQ; GPNNWRNSLQR; PNNWRNSLQRS; NNWRNSLQRSK; NWRNSLQRSKA; WRNSLQRSKAL; RNSLQRSKALR; VPTYGTEEWES; PTYGTEEWESW; TYGTEEWESWW; YGTEEWESWWS; GTEEWESWWSS; TEEWESWWSSF; EEWESWWSSFN; EWESWWSSFNE; WESWWSSFNEK; ESWWSSFNEKW; SWWSSFNEKWD; WWSSFNEKWDE; WSSFNEKWDED; SSFNEKWDEDL; SFNEKWDEDLF; FNEKWDEDLFC; NEKWDEDLFCH; EKWDEDLFCHE; KWDEDLFCHED; WDEDLFCHEDM; DEDLFCHEDMF; EDLFCHEDMFA; DLFCHEDMFAS; LFCHEDMFASD; FCHEDMFASDE; CHEDMFASDEE; HEDMFASDEEA; EDMFASDEEAT; DMFASDEEATA; MFASDEEATAD; FASDEEATADS; ASDEEATADSQ; SDEEATADSQH; DEEATADSQHS; EEATADSQHST; EATADSQHSTP; ATADSQHSTPP; TADSQHSTPPK; ADSQHSTPPKK; DSQHSTPPKKK; SQHSTPPKKKR; QHSTPPKKKRK; HSTPPKKKRKV; STPPKKKRKVE; TPPKKKRKVED; PPKKKRKVEDP; PKKKRKVEDPK; KKKRKVEDPKD; KKRKVEDPKDF; KRKVEDPKDFP; RKVEDPKDFPS; KVEDPKDFPSD; VEDPKDFPSDL; EDPKDFPSDLH; DPKDFPSDLHQ; PKDFPSDLHQF; KDFPSDLHQFL; DFPSDLHQFLS; FPSDLHQFLSQ; PSDLHQFLSQA; SDLHQFLSQAV; DLHQFLSQAVF; LHQFLSQAVFS; HQFLSQAVFSN; QFLSQAVFSNR; FLSQAVFSNRT; LSQAVFSNRTL; SQAVFSNRTLA; QAVFSNRTLAC; AVFSNRTLACF; VFSNRTLACFA; FSNRTLACFAV; SNRTLACFAVY; NRTLACFAVYT; RTLACFAVYTT; TLACFAVYTTK; LACFAVYTTKE; ACFAVYTTKEK; CFAVYTTKEKA; FAVYTTKEKAQ; AVYTTKEKAQI; VYTTKEKAQIL; YTTKEKAQILY; TTKEKAQILYK; TKEKAQILYKK; KEKAQILYKKL; EKAQILYKKLM; KAQILYKKLME; AQILYKKLMEK; QILYKKLMEKY; ILYKKLMEKYS; LYKKLMEKYSV; YKKLMEKYSVT; KKLMEKYSVTF; KLMEKYSVTFI; LMEKYSVTFIS; MEKYSVTFISR; EKYSVTFISRH; KYSVTFISRHM; YSVTFISRHMC; SVTFISRHMCA; VTFISRHMCAG; TFISRHMCAGH; FISRHMCAGHN; ISRHMCAGHNI; SRHMCAGHNII; RHMCAGHNIIF; HMCAGHNIIFF; MCAGHNIIFFL; CAGHNIIFFLT; AGHNIIFFLTP; GHNIIFFLTPH; HNIIFFLTPHR; NIIFFLTPHRH; IIFFLTPHRHR; IFFLTPHRHRV; FFLTPHRHRVS; FLTPHRHRVSA; LTPHRHRVSAI; TPHRHRVSAIN; PHRHRVSAINN; HRHRVSAINNF; RHRVSAINNFC; HRVSAINNFCQ; RVSAINNFCQK; VSAINNFCQKL; SAINNFCQKLC; AINNFCQKLCT; INNFCQKLCTF; NNFCQKLCTFS; NFCQKLCTFSF; FCQKLCTFSFL; CQKLCTFSFLI; QKLCTFSFLIC; KLCTFSFLICK; LCTFSFLICKG; CTFSFLICKGV; TFSFLICKGVN; FSFLICKGVNK; SFLICKGVNKE; FLICKGVNKEY; LICKGVNKEYL; ICKGVNKEYLL; CKGVNKEYLLY; KGVNKEYLLYS; GVNKEYLLYSA; VNKEYLLYSAL; NKEYLLYSALT; KEYLLYSALTR; EYLLYSALTRD; YLLYSALTRDP; LLYSALTRDPY; LYSALTRDPYH; YSALTRDPYHT; SALTRDPYHTI; ALTRDPYHTIE; LTRDPYHTIEE; TRDPYHTIEES; RDPYHTIEESI; DPYHTIEESIQ; PYHTIEESIQG; YHTIEESIQGG; HTIEESIQGGL; TIEESIQGGLK; IEESIQGGLKE; EESIQGGLKEH; ESIQGGLKEHD; SIQGGLKEHDF; IQGGLKEHDFS; QGGLKEHDFSP; GGLKEHDFSPE; GLKEHDFSPEE; LKEHDFSPEEP; KEHDFSPEEPE; EHDFSPEEPEE; HDFSPEEPEET; DFSPEEPEETK; FSPEEPEETKQ; SPEEPEETKQV; PEEPEETKQVS; EEPEETKQVSW; EPEETKQVSWK; PEETKQVSWKL; EETKQVSWKLI; ETKQVSWKLIT; TKQVSWKLITE; KQVSWKLITEY; QVSWKLITEYA; VSWKLITEYAV; SWKLITEYAVE; WKLITEYAVET; KLITEYAVETK; LITEYAVETKC; ITEYAVETKCE; TEYAVETKCED; EYAVETKCEDV; YAVETKCEDVF; AVETKCEDVFL; VETKCEDVFLL; ETKCEDVFLLL; TKCEDVFLLLG; KCEDVFLLLGM; CEDVFLLLGMY; EDVFLLLGMYL; DVFLLLGMYLE; VFLLLGMYLEF; FLLLGMYLEFQ; LLLGMYLEFQY; LLGMYLEFQYN; LGMYLEFQYNV; GMYLEFQYNVE; MYLEFQYNVEE; YLEFQYNVEEC; LEFQYNVEECK; EFQYNVEECKK; FQYNVEECKKC; QYNVEECKKCQ; YNVEECKKCQK; NVEECKKCQKK; VEECKKCQKKD; EECKKCQKKDQ; ECKKCQKKDQP; CKKCQKKDQPY; KKCQKKDQPYH; KCQKKDQPYHF; CQKKDQPYHFK; QKKDQPYHFKY; KKDQPYHFKYH; KDQPYHFKYHE; DQPYHFKYHEK; QPYHFKYHEKH; PYHFKYHEKHF; YHFKYHEKHFA; HFKYHEKHFAN; FKYHEKHFANA; KYHEKHFANAI; YHEKHFANAII; HEKHFANAIIF; EKHFANAIIFA; KHFANAIIFAE; HFANAIIFAES; FANAIIFAESK; ANAIIFAESKN; NAIIFAESKNQ; AIIFAESKNQK; IIFAESKNQKS; IFAESKNQKSI; FAESKNQKSIC; AESKNQKSICQ; ESKNQKSICQQ; SKNQKSICQQA; KNQKSICQQAV; NQKSICQQAVD; QKSICQQAVDT; KSICQQAVDTV; SICQQAVDTVL; ICQQAVDTVLA; CQQAVDTVLAK; QQAVDTVLAKK; QAVDTVLAKKR; AVDTVLAKKRV; VDTVLAKKRVD; DTVLAKKRVDT; TVLAKKRVDTL; VLAKKRVDTLH; LAKKRVDTLHM; AKKRVDTLHMT; KKRVDTLHMTR; KRVDTLHMTRE; RVDTLHMTREE; VDTLHMTREEM; DTLHMTREEML; TLHMTREEMLT; LHMTREEMLTE; HMTREEMLTER; MTREEMLTERF; TREEMLTERFN; REEMLTERFNH; EEMLTERFNHI; EMLTERFNHIL; MLTERFNHILD; LTERFNHILDK; TERFNHILDKM; ERFNHILDKMD; RFNHILDKMDL; FNHILDKMDLI; NHILDKMDLIF; HILDKMDLIFG; ILDKMDLIFGA; LDKMDLIFGAH; DKMDLIFGAHG; KMDLIFGAHGN; MDLIFGAHGNA; DLIFGAHGNAV; LIFGAHGNAVL; IFGAHGNAVLE; FGAHGNAVLEQ; GAHGNAVLEQY; AHGNAVLEQYM; HGNAVLEQYMA; GNAVLEQYMAG; NAVLEQYMAGV; AVLEQYMAGVA; VLEQYMAGVAW; LEQYMAGVAWL; EQYMAGVAWLH; QYMAGVAWLHC; YMAGVAWLHCL; MAGVAWLHCLL; AGVAWLHCLLP; GVAWLHCLLPK; VAWLHCLLPKM; AWLHCLLPKMD; WLHCLLPKMDS; LHCLLPKMDSV; HCLLPKMDSVI; CLLPKMDSVIF; LLPKMDSVIFD; LPKMDSVIFDF; PKMDSVIFDFL; KMDSVIFDFLH; MDSVIFDFLHC; DSVIFDFLHCI; SVIFDFLHCIV; VIFDFLHCIVF; IFDFLHCIVFN; FDFLHCIVFNV; DFLHCIVFNVP; FLHCIVFNVPK; LHCIVFNVPKR; HCIVFNVPKRR; CIVFNVPKRRY; IVFNVPKRRYW; VFNVPKRRYWL; FNVPKRRYWLF; NVPKRRYWLFK; VPKRRYWLFKG; PKRRYWLFKGP; KRRYWLFKGPI; RRYWLFKGPID; RYWLFKGPIDS; YWLFKGPIDSG; WLFKGPIDSGK; LFKGPIDSGKT; FKGPIDSGKTT; KGPIDSGKTTL; GPIDSGKTTLA; PIDSGKTTLAA; IDSGKTTLAAG; DSGKTTLAAGL; SGKTTLAAGLL; GKTTLAAGLLD; KTTLAAGLLDL; TTLAAGLLDLC; TLAAGLLDLCG; LAAGLLDLCGG; AAGLLDLCGGK; AGLLDLCGGKA; GLLDLCGGKAL; LLDLCGGKALN; LDLCGGKALNV; DLCGGKALNVN; LCGGKALNVNL; CGGKALNVNLP; GGKALNVNLPM; GKALNVNLPME; KALNVNLPMER; ALNVNLPMERL; LNVNLPMERLT; NVNLPMERLTF; VNLPMERLTFE; NLPMERLTFEL; LPMERLTFELG; PMERLTFELGV; MERLTFELGVA; ERLTFELGVAI; RLTFELGVAID; LTFELGVAIDQ; TFELGVAIDQY; FELGVAIDQYM; ELGVAIDQYMV; LGVAIDQYMVV; GVAIDQYMVVF; VAIDQYMVVFE; AIDQYMVVFED; IDQYMVVFEDV; DQYMVVFEDVK; QYMVVFEDVKG; YMVVFEDVKGT; MVVFEDVKGTG; VVFEDVKGTGA; VFEDVKGTGAE; FEDVKGTGAES; EDVKGTGAESK; DVKGTGAESKD; VKGTGAESKDL; KGTGAESKDLP; GTGAESKDLPS; TGAESKDLPSG; GAESKDLPSGH; AESKDLPSGHG; ESKDLPSGHGI; SKDLPSGHGIN; KDLPSGHGINN; DLPSGHGINNL; LPSGHGINNLD; PSGHGINNLDS; SGHGINNLDSL; GHGINNLDSLR; HGINNLDSLRD; GINNLDSLRDY; INNLDSLRDYL; NNLDSLRDYLD; NLDSLRDYLDG; LDSLRDYLDGS; DSLRDYLDGSV; SLRDYLDGSVK; LRDYLDGSVKV; RDYLDGSVKVN; DYLDGSVKVNL; YLDGSVKVNLE; LDGSVKVNLEK; DGSVKVNLEKK; GSVKVNLEKKH; SVKVNLEKKHL; VKVNLEKKHLN; KVNLEKKHLNK; VNLEKKHLNKR; NLEKKHLNKRT; LEKKHLNKRTQ; EKKHLNKRTQI; KKHLNKRTQIF; KHLNKRTQIFP; HLNKRTQIFPP; LNKRTQIFPPG; NKRTQIFPPGL; KRTQIFPPGLV; RTQIFPPGLVT; TQIFPPGLVTM; QIFPPGLVTMN; IFPPGLVTMNE; FPPGLVTMNEY; PPGLVTMNEYP; PGLVTMNEYPV; GLVTMNEYPVP; LVTMNEYPVPK; VTMNEYPVPKT; TMNEYPVPKTL; MNEYPVPKTLQ; NEYPVPKTLQA; EYPVPKTLQAR; YPVPKTLQARF; PVPKTLQARFV; VPKTLQARFVR; PKTLQARFVRQ; KTLQARFVRQI; TLQARFVRQID; LQARFVRQIDF; QARFVRQIDFR; ARFVRQIDFRP; RFVRQIDFRPK; FVRQIDFRPKI; VRQIDFRPKIY; RQIDFRPKIYL; QIDFRPKIYLR; IDFRPKIYLRK; DFRPKIYLRKS; FRPKIYLRKSL; RPKIYLRKSLQ; PKIYLRKSLQN; KIYLRKSLQNS; IYLRKSLQNSE; YLRKSLQNSEF; LRKSLQNSEFL; RKSLQNSEFLL; KSLQNSEFLLE; SLQNSEFLLEK; LQNSEFLLEKR; QNSEFLLEKRI; NSEFLLEKRIL; SEFLLEKRILQ; EFLLEKRILQS; FLLEKRILQSG; LLEKRILQSGM; LEKRILQSGMT; EKRILQSGMTL; KRILQSGMTLL; RILQSGMTLLL; ILQSGMTLLLL; LQSGMTLLLLL; QSGMTLLLLLI; SGMTLLLLLIW; GMTLLLLLIWF; MTLLLLLIWFR; TLLLLLIWFRP; LLLLLIWFRPV; LLLLIWFRPVA; LLLIWFRPVAD; LLIWFRPVADF; LIWFRPVADFA; IWFRPVADFAT; WFRPVADFATD; FRPVADFATDI; RPVADFATDIQ; PVADFATDIQS; VADFATDIQSR; ADFATDIQSRI; DFATDIQSRIV; FATDIQSRIVE; ATDIQSRIVEW; TDIQSRIVEWK; DIQSRIVEWKE; IQSRIVEWKER; QSRIVEWKERL; SRIVEWKERLD; RIVEWKERLDS; IVEWKERLDSE; VEWKERLDSEI; EWKERLDSEIS; WKERLDSEISM; KERLDSEISMY; ERLDSEISMYT; RLDSEISMYTF; LDSEISMYTFS; DSEISMYTFSR; SEISMYTFSRM; EISMYTFSRMK; ISMYTFSRMKY; SMYTFSRMKYN; MYTFSRMKYNI; YTFSRMKYNIC; TFSRMKYNICM; FSRMKYNICMG; SRMKYNICMGK; RMKYNICMGKC; MKYNICMGKCI; KYNICMGKCIL; YNICMGKCILD; NICMGKCILDI; ICMGKCILDIT; CMGKCILDITR; MGKCILDITRE; GKCILDITREE; KCILDITREED; CILDITREEDS; ILDITREEDSE; LDITREEDSET; DITREEDSETE; ITREEDSETED; TREEDSETEDS; REEDSETEDSG; EEDSETEDSGH; EDSETEDSGHG; DSETEDSGHGS; SETEDSGHGSS; ETEDSGHGSST; TEDSGHGSSTE; EDSGHGSSTES; DSGHGSSTESQ; SGHGSSTESQS; GHGSSTESQSQ; HGSSTESQSQC; GSSTESQSQCS; SSTESQSQCSS; STESQSQCSSQ; TESQSQCSSQV; ESQSQCSSQVS; SQSQCSSQVSD; QSQCSSQVSDT; SQCSSQVSDTS; QCSSQVSDTSA; CSSQVSDTSAP; SSQVSDTSAPA; SQVSDTSAPAE; QVSDTSAPAED; VSDTSAPAEDS; SDTSAPAEDSQ; DTSAPAEDSQR; TSAPAEDSQRS; SAPAEDSQRSD; APAEDSQRSDP; PAEDSQRSDPH; AEDSQRSDPHS; EDSQRSDPHSQ; DSQRSDPHSQE; SQRSDPHSQEL; QRSDPHSQELH; RSDPHSQELHL; SDPHSQELHLC; DPHSQELHLCK; PHSQELHLCKG; HSQELHLCKGF; SQELHLCKGFQ; QELHLCKGFQC; ELHLCKGFQCF; LHLCKGFQCFK; HLCKGFQCFKR; LCKGFQCFKRP; CKGFQCFKRPK; KGFQCFKRPKT; GFQCFKRPKTP; FQCFKRPKTPP; QCFKRPKTPPP; CFKRPKTPPPK; HKLKSGLYKSS; KLKSGLYKSSI; LKSGLYKSSIY; MYMYNKSTCLK; YMYNKSTCLKH; MYNKSTCLKHF; YNKSTCLKHFG; NKSTCLKHFGL; KSTCLKHFGLQ; STCLKHFGLQL; TCLKHFGLQLS; CLKHFGLQLSL; LKHFGLQLSLF; KHFGLQLSLFV; HFGLQLSLFVN; FGLQLSLFVNI; GLQLSLFVNIS; LQLSLFVNISY; QLSLFVNISYH; LSLFVNISYHI; SLFVNISYHIW; LFVNISYHIWV; FVNISYHIWVP; VNISYHIWVPW; NISYHIWVPWK; ISYHIWVPWKS; SYHIWVPWKSF; YHIWVPWKSFC; HIWVPWKSFCA; IWVPWKSFCAI; WVPWKSFCAIK; VPWKSFCAIKH; PWKSFCAIKHP; WKSFCAIKHPN; KSFCAIKHPNL; SFCAIKHPNLF; FCAIKHPNLFY; CAIKHPNLFYL; AIKHPNLFYLG; IKHPNLFYLGF; KHPNLFYLGFH; HPNLFYLGFHT; PNLFYLGFHTI; NLFYLGFHTIH; LFYLGFHTIHR; FYLGFHTIHRL; YLGFHTIHRLP; LGFHTIHRLPI; GFHTIHRLPIH; FHTIHRLPIHS; HTIHRLPIHSL; TIHRLPIHSLG; IHRLPIHSLGS; HRLPIHSLGSP; RLPIHSLGSPV; LPIHSLGSPVY; PIHSLGSPVYK; IHSLGSPVYKV; HSLGSPVYKVT; QKGNWVRILYR; KGNWVRILYRS; GNWVRILYRSF; NWVRILYRSFS; WVRILYRSFSQ; VRILYRSFSQA; RILYRSFSQAD; ILYRSFSQADL; LYRSFSQADLK; YRSFSQADLKI; RSFSQADLKIS; SFSQADLKISC; FSQADLKISCK; SQADLKISCKA; QADLKISCKAS; ADLKISCKASP; DLKISCKASPL; LKISCKASPLL; KISCKASPLLC; ISCKASPLLCS; SCKASPLLCSR; CKASPLLCSRA; KASPLLCSRAV; ASPLLCSRAVS; SPLLCSRAVSK; PLLCSRAVSKQ; LLCSRAVSKQA; LCSRAVSKQAT; CSRAVSKQATN; SRAVSKQATNI; RAVSKQATNIS; AVSKQATNISS; NIQAISFTKRP; IQAISFTKRPH; QAISFTKRPHT; AISFTKRPHTL; ISFTKRPHTLF; SFTKRPHTLFI; QHCGSCVGHMK; HCGSCVGHMKY; CGSCVGHMKYW; GSCVGHMKYWG; SCVGHMKYWGN; CVGHMKYWGNI; VGHMKYWGNIF; GHMKYWGNIFP; HMKYWGNIFPS; MKYWGNIFPSC; KYWGNIFPSCE; YWGNIFPSCES; WGNIFPSCESP; GNIFPSCESPK; NIFPSCESPKI; IFPSCESPKIP; FPSCESPKIPS; PSCESPKIPSI; SCESPKIPSIF; CESPKIPSIFI; ESPKIPSIFIS; SPKIPSIFIST; PKIPSIFISTG; KIPSIFISTGI; IPSIFISTGIR; PSIFISTGIRY; SIFISTGIRYP; IFISTGIRYPA; FISTGIRYPAL; ISTGIRYPALN; STGIRYPALNW; TGIRYPALNWI; GIRYPALNWIS; IRYPALNWISI; RYPALNWISIV; YPALNWISIVF; PALNWISIVFV; ALNWISIVFVQ; LNWISIVFVQI; NWISIVFVQIG; WISIVFVQIGL; ISIVFVQIGLM; SIVFVQIGLMV; IVFVQIGLMVS; VFVQIGLMVSI; FVQIGLMVSIH; VQIGLMVSIHY; QIGLMVSIHYL; IGLMVSIHYLG; GLMVSIHYLGL; LMVSIHYLGLG; MVSIHYLGLGC; VSIHYLGLGCW; SIHYLGLGCWV; IHYLGLGCWVF; HYLGLGCWVFR; YLGLGCWVFRG; LGLGCWVFRGY; GLGCWVFRGYS; LGCWVFRGYST; GCWVFRGYSTI; CWVFRGYSTIR; WVFRGYSTIRV; VFRGYSTIRVL; HSLHFQGFSTY; SLHFQGFSTYS; LHFQGFSTYSK; HFQGFSTYSKE; FQGFSTYSKEV; QGFSTYSKEVE; GFSTYSKEVEI; FSTYSKEVEIT; STYSKEVEITA; TYSKEVEITAL; YSKEVEITALN; SKEVEITALNR; KEVEITALNRF; EVEITALNRFS; VEITALNRFSS; EITALNRFSST; ITALNRFSSTM; TALNRFSSTML; ALNRFSSTMLM; LNRFSSTMLMH; NRFSSTMLMHF; RFSSTMLMHFL; PCMKVKHASYS; CMKVKHASYSN; MKVKHASYSNN; KVKHASYSNNL; VKHASYSNNLC; KHASYSNNLCL; HASYSNNLCLY; ASYSNNLCLYS; SYSNNLCLYSY; YSNNLCLYSYS; SNNLCLYSYSL; NNLCLYSYSLP; NLCLYSYSLPH; LCLYSYSLPHQ; IGEGNSCCAVT; GEGNSCCAVTG; EGNSCCAVTGK; GNSCCAVTGKH; NSCCAVTGKHF; SCCAVTGKHFS; CCAVTGKHFSL; CAVTGKHFSLW; AVTGKHFSLWA; VTGKHFSLWAI; TGKHFSLWAIT; GKHFSLWAITA; KHFSLWAITAK; HFSLWAITAKV; FSLWAITAKVI; SLWAITAKVIF; LWAITAKVIFS; WAITAKVIFST; TKAPKVFIWIP; KAPKVFIWIPH; APKVFIWIPHF; PKVFIWIPHFW; KVFIWIPHFWV; EAFYLCNSIYP; AFYLCNSIYPS; FYLCNSIYPSF; YLCNSIYPSFN; LCNSIYPSFNF; FWHLHGFLWLF; WHLHGFLWLFG; HLHGFLWLFGS; LHGFLWLFGSC; HGFLWLFGSCP; GFLWLFGSCPW; FLWLFGSCPWT; LWLFGSCPWTL; WLFGSCPWTLS; LFGSCPWTLSF; FGSCPWTLSFS; GSCPWTLSFSF; SCPWTLSFSFG; CPWTLSFSFGW; PWTLSFSFGWG; WTLSFSFGWGH; TLSFSFGWGHL; LSFSFGWGHLH; SFSFGWGHLHM; FSFGWGHLHML; SFGWGHLHMLQ; FGWGHLHMLQE; GWGHLHMLQEQ; WGHLHMLQEQV; GHLHMLQEQVL; HLHMLQEQVLQ; LHMLQEQVLQS; HMLQEQVLQSR; MLQEQVLQSRT; LQEQVLQSRTG; QEQVLQSRTGL; EQVLQSRTGLE; QVLQSRTGLEV; VLQSRTGLEVK; LQSRTGLEVKA; QSRTGLEVKAT; SRTGLEVKATS; RTGLEVKATSI; TGLEVKATSIE; GLEVKATSIEE; LEVKATSIEEQ; EVKATSIEEQF; VKATSIEEQFF; KATSIEEQFFD; TLLNVHFVDFL; LLNVHFVDFLS; LNVHFVDFLSP; NVHFVDFLSPF; VHFVDFLSPFF; HFVDFLSPFFV; LLLYCQHHLYY; LLYCQHHLYYK; LYCQHHLYYKY; YCQHHLYYKYG; CQHHLYYKYGQ; QHHLYYKYGQN; HHLYYKYGQNV; HLYYKYGQNVH; LYYKYGQNVHG; YYKYGQNVHGY; YKYGQNVHGYL; KYGQNVHGYLP; YGQNVHGYLPF; GQNVHGYLPFQ; QNVHGYLPFQL; NVHGYLPFQLL; VHGYLPFQLLV; GKDQNNIVEYN; KDQNNIVEYNY; DQNNIVEYNYK; QNNIVEYNYKS; NNIVEYNYKSL; KIFLFFSAIPV; IFLFFSAIPVR; FLFFSAIPVRL; QKYLHQETEYH; KYLHQETEYHS; YLHQETEYHST; LHQETEYHSTH; HQETEYHSTHL; QETEYHSTHLG; TIPKPCLIADR; IPKPCLIADRG; PKPCLIADRGL; KPCLIADRGLQ; PCLIADRGLQW; CLIADRGLQWK; LIADRGLQWKL; IADRGLQWKLC; ADRGLQWKLCD; DRGLQWKLCDP; RGLQWKLCDPN; GLQWKLCDPNH; LQWKLCDPNHQ; QWKLCDPNHQR; WKLCDPNHQRT; KLCDPNHQRTY; LCDPNHQRTYT; CDPNHQRTYTL; DPNHQRTYTLL; PNHQRTYTLLE; NHQRTYTLLEL; HQRTYTLLELR; QRTYTLLELRN; PQEHQQLQHMF; QEHQQLQHMFE; EHQQLQHMFEE; HQQLQHMFEEL; QQLQHMFEELG; QLQHMFEELGL; QQQPPQQQFQP; QQPPQQQFQPL; QPPQQQFQPLK; PPQQQFQPLKI; PQQQFQPLKIL; QQQFQPLKILW; QQFQPLKILWQ; QFQPLKILWQQ; FQPLKILWQQQ; QPLKILWQQQP; PLKILWQQQPQ; LKILWQQQPQI; KILWQQQPQIH; ILWQQQPQIHW; LWQQQPQIHWQ; WQQQPQIHWQL; QQQPQIHWQLG; QQPQIHWQLGP; QPQIHWQLGPP; PQIHWQLGPPK; QIHWQLGPPKV; IHWQLGPPKVL; HWQLGPPKVLE; WQLGPPKVLEQ; QLGPPKVLEQH; LGPPKVLEQHP; TWKYKKKGITY; WKYKKKGITYL; KYKKKGITYLG; YKKKGITYLGV; KKKGITYLGVF; KKGITYLGVFY; KGITYLGVFYR; GITYLGVFYRV; ITYLGVFYRVF; TYLGVFYRVFY; YLGVFYRVFYS; LGVFYRVFYSR; SSGTFVFPVYT; SGTFVFPVYTV; GTFVFPVYTVF; TFVFPVYTVFT; FVFPVYTVFTS; VFPVYTVFTST; FPVYTVFTSTK; PVYTVFTSTKF; VYTVFTSTKFQ; YTVFTSTKFQQ; TVFTSTKFQQK; VFTSTKFQQKL; NKNKNPLSSFF; KNKNPLSSFFC; NKNPLSSFFCS; KNPLSSFFCSS; NPLSSFFCSSP; PLSSFFCSSPG; LSSFFCSSPGF; SSFFCSSPGFT; SFFCSSPGFTN; FFCSSPGFTNF; FCSSPGFTNFH; QLAQNHGLCPV; LGTRPRFLGSQ; GTRPRFLGSQN; TRPRFLGSQNM; RPRFLGSQNMS; PRFLGSQNMSV; RFLGSQNMSVM; FLGSQNMSVMH; LGSQNMSVMHF; GSQNMSVMHFP; SQNMSVMHFPS; AAPPCESCTFL; APPCESCTFLP; PPCESCTFLPE; PCESCTFLPEV; CESCTFLPEVM; ESCTFLPEVMV; SCTFLPEVMVW; CTFLPEVMVWL; TFLPEVMVWLH; FLPEVMVWLHS; LPEVMVWLHSP; PEVMVWLHSPV; EVMVWLHSPVS; VMVWLHSPVSH; MVWLHSPVSHA; VWLHSPVSHAL; WLHSPVSHALS; LHSPVSHALSF; HSPVSHALSFL; SPVSHALSFLR; PVSHALSFLRS; VSHALSFLRSW; SHALSFLRSWF; HALSFLRSWFG; ALSFLRSWFGC; LSFLRSWFGCI; SFLRSWFGCIP; FLRSWFGCIPW; LRSWFGCIPWV; RSWFGCIPWVS; SWFGCIPWVSS; WFGCIPWVSSS; FGCIPWVSSSS; GCIPWVSSSSL; CIPWVSSSSLW; IPWVSSSSLWP; PWVSSSSLWPF; WVSSSSLWPFF; VSSSSLWPFFL; YIRGRGRLCLH; IRGRGRLCLHP; RGRGRLCLHPF; GRGRLCLHPFS; RGRLCLHPFSQ; GRLCLHPFSQV; RLCLHPFSQVV; LCLHPFSQVVR; CLHPFSQVVRV; LHPFSQVVRVW; HPFSQVVRVWR; PFSQVVRVWRL; FSQVVRVWRLF; SQVVRVWRLFL; QVVRVWRLFLR; VVRVWRLFLRP; VRVWRLFLRPS; RVWRLFLRPSK; VWRLFLRPSKT; WRLFLRPSKTI; RLFLRPSKTIW; LFLRPSKTIWG; FLRPSKTIWGN; LRPSKTIWGNP; RPSKTIWGNPY; PSKTIWGNPYS; SKTIWGNPYSF; KTIWGNPYSFA; TIWGNPYSFAI; IWGNPYSFAIF; WGNPYSFAIFA; GNPYSFAIFAK SEQ ID NOS.: 7-24956

Preferred BK virus fragments of VP2-3 capable of interacting with one or more MHC class 1 molecules are listed in Table J.

TABLE J Prediction of BK virus VP2-3 protein specific MHC class1, 8-, 9-, 10-, 11-mer peptide binders for 42 MHC class 1 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHC/ database. The MHC class 1 molecules for which no binders were found are not listed. pos peptide logscore affinity(nM) Bind Level Protein Name Allele 8-mers 107 KVSTVGLY 0.435 454 WB VP2-3 A0101 140 FVNNIQYL 0.674 33 SB VP2-3 A0201 80 FAALIQTV 0.581 93 WB VP2-3 A0201 195 FLEETTWT 0.576 98 WB VP2-3 A0201 5 ALLGDLVA 0.564 111 WB VP2-3 A0201 43 SLATVEGI 0.559 118 WB VP2-3 A0201 293 MLPLLLGL 0.552 127 WB VP2-3 A0201 40 QIASLATV 0.533 155 WB VP2-3 A0201 61 GLTPQTYA 0.533 155 WB VP2-3 A0201 296 LLLGLYGT 0.529 163 WB VP2-3 A0201 76 AIAGFAAL 0.469 311 WB VP2-3 A0201 89 GISSLAQV 0.456 358 WB VP2-3 A0201 297 LLGLYGTV 0.439 433 WB VP2-3 A0201 132 ILFPGVNT 0.434 457 WB VP2-3 A0201 140 FVNNIQYL 0.869 4 SB VP2-3 A0202 293 MLPLLLGL 0.799 8 SB VP2-3 A0202 80 FAALIQTV 0.745 15 SB VP2-3 A0202 43 SLATVEGI 0.730 18 SB VP2-3 A0202 61 GLTPQTYA 0.709 23 SB VP2-3 A0202 195 FLEETTWT 0.686 29 SB VP2-3 A0202 76 AIAGFAAL 0.667 36 SB VP2-3 A0202 89 GISSLAQV 0.640 49 SB VP2-3 A0202 3 ALALLGDL 0.630 54 WB VP2-3 A0202 297 LLGLYGTV 0.607 69 WB VP2-3 A0202 40 QIASLATV 0.606 71 WB VP2-3 A0202 0 MGAALALL 0.581 92 WB VP2-3 A0202 112 GLYQQSGM 0.575 99 WB VP2-3 A0202 287 RTAPQWML 0.543 139 WB VP2-3 A0202 6 LLGDLVAS 0.539 146 WB VP2-3 A0202 157 FATISQAL 0.530 162 WB VP2-3 A0202 10 LVASVSEA 0.524 173 WB VP2-3 A0202 296 LLLGLYGT 0.477 287 WB VP2-3 A0202 155 SLFATISQ 0.473 298 WB VP2-3 A0202 86 TVTGISSL 0.461 341 WB VP2-3 A0202 62 LTPQTYAV 0.458 352 WB VP2-3 A0202 114 YQQSGMAL 0.445 405 WB VP2-3 A0202 13 SVSEAAAA 0.433 461 WB VP2-3 A0202 18 AAATGFSV 0.427 490 WB VP2-3 A0202 132 ILFPGVNT 0.427 491 WB VP2-3 A0202 43 SLATVEGI 0.798 8 SB VP2-3 A0203 140 FVNNIQYL 0.775 11 SB VP2-3 A0203 297 LLGLYGTV 0.773 11 SB VP2-3 A0203 40 QIASLATV 0.748 15 SB VP2-3 A0203 80 FAALIQTV 0.730 18 SB VP2-3 A0203 61 GLTPQTYA 0.706 24 SB VP2-3 A0203 89 GISSLAQV 0.701 25 SB VP2-3 A0203 76 AIAGFAAL 0.701 25 SB VP2-3 A0203 83 LIQTVTGI 0.666 37 SB VP2-3 A0203 18 AAATGFSV 0.649 44 SB VP2-3 A0203 3 ALALLGDL 0.643 47 SB VP2-3 A0203 112 GLYQQSGM 0.624 58 WB VP2-3 A0203 10 LVASVSEA 0.604 72 WB VP2-3 A0203 114 YQQSGMAL 0.558 119 WB VP2-3 A0203 296 LLLGLYGT 0.552 127 WB VP2-3 A0203 195 FLEETTWT 0.540 144 WB VP2-3 A0203 132 ILFPGVNT 0.534 154 WB VP2-3 A0203 62 LTPQTYAV 0.523 175 WB VP2-3 A0203 69 VIAGAPGA 0.516 187 WB VP2-3 A0203 161 SQALWHVI 0.493 241 WB VP2-3 A0203 86 TVTGISSL 0.464 330 WB VP2-3 A0203 5 ALLGDLVA 0.455 364 WB VP2-3 A0203 13 SVSEAAAA 0.454 368 WB VP2-3 A0203 268 SVHSGEFI 0.440 426 WB VP2-3 A0203 167 VIRDDIPA 0.435 450 WB VP2-3 A0203 297 LLGLYGTV 0.613 66 WB VP2-3 A0204 43 SLATVEGI 0.584 90 WB VP2-3 A0204 140 FVNNIQYL 0.522 175 WB VP2-3 A0204 80 FAALIQTV 0.522 176 WB VP2-3 A0204 287 RTAPQWML 0.509 203 WB VP2-3 A0204 114 YQQSGMAL 0.793 9 SB VP2-3 A0206 80 FAALIQTV 0.748 15 SB VP2-3 A0206 18 AAATGFSV 0.743 16 SB VP2-3 A0206 140 FVNNIQYL 0.719 20 SB VP2-3 A0206 39 VQIASLAT 0.713 22 SB VP2-3 A0206 161 SQALWHVI 0.700 25 SB VP2-3 A0206 40 QIASLATV 0.665 37 SB VP2-3 A0206 75 GAIAGFAA 0.665 37 SB VP2-3 A0206 76 AIAGFAAL 0.657 40 SB VP2-3 A0206 293 MLPLLLGL 0.644 47 SB VP2-3 A0206 94 AQVGYRFF 0.637 50 WB VP2-3 A0206 62 LTPQTYAV 0.598 77 WB VP2-3 A0206 214 IQDYYSNL 0.578 96 WB VP2-3 A0206 201 WTIVNAPI 0.563 112 WB VP2-3 A0206 195 FLEETTWT 0.551 129 WB VP2-3 A0206 296 LLLGLYGT 0.550 129 WB VP2-3 A0206 89 GISSLAQV 0.537 149 WB VP2-3 A0206 5 ALLGDLVA 0.535 153 WB VP2-3 A0206 157 FATISQAL 0.507 207 WB VP2-3 A0206 13 SVSEAAAA 0.502 217 WB VP2-3 A0206 287 RTAPQWML 0.501 221 WB VP2-3 A0206 61 GLTPQTYA 0.499 226 WB VP2-3 A0206 23 FSVAEIAA 0.479 279 WB VP2-3 A0206 297 LLGLYGTV 0.477 286 WB VP2-3 A0206 45 ATVEGITT 0.475 292 WB VP2-3 A0206 4 LALLGDLV 0.460 346 WB VP2-3 A0206 101 FSDWDHKV 0.454 366 WB VP2-3 A0206 10 LVASVSEA 0.443 412 WB VP2-3 A0206 132 ILFPGVNT 0.441 425 WB VP2-3 A0206 247 SIDNADSI 0.437 440 WB VP2-3 A0206 303 TVTPALEA 0.437 443 WB VP2-3 A0206 43 SLATVEGI 0.433 463 WB VP2-3 A0206 35 AAIEVQIA 0.427 493 WB VP2-3 A0206 5 ALLGDLVA 0.884 3 SB VP2-3 A0211 293 MLPLLLGL 0.861 4 SB VP2-3 A0211 61 GLTPQTYA 0.856 4 SB VP2-3 A0211 297 LLGLYGTV 0.852 4 SB VP2-3 A0211 146 YLDPRHWG 0.842 5 SB VP2-3 A0211 89 GISSLAQV 0.841 5 SB VP2-3 A0211 155 SLFATISQ 0.823 6 SB VP2-3 A0211 76 AIAGFAAL 0.819 7 SB VP2-3 A0211 43 SLATVEGI 0.812 7 SB VP2-3 A0211 40 QIASLATV 0.801 8 SB VP2-3 A0211 296 LLLGLYGT 0.762 13 SB VP2-3 A0211 140 FVNNIQYL 0.727 19 SB VP2-3 A0211 132 ILFPGVNT 0.718 21 SB VP2-3 A0211 80 FAALIQTV 0.692 27 SB VP2-3 A0211 195 FLEETTWT 0.687 29 SB VP2-3 A0211 86 TVTGISSL 0.686 29 SB VP2-3 A0211 101 FSDWDHKV 0.685 30 SB VP2-3 A0211 62 LTPQTYAV 0.680 32 SB VP2-3 A0211 18 AAATGFSV 0.673 34 SB VP2-3 A0211 112 GLYQQSGM 0.663 38 SB VP2-3 A0211 287 RTAPQWML 0.657 40 SB VP2-3 A0211 247 SIDNADSI 0.657 40 SB VP2-3 A0211 250 NADSIEEV 0.652 43 SB VP2-3 A0211 262 DLRNKESV 0.628 56 WB VP2-3 A0211 299 GLYGTVTP 0.595 79 WB VP2-3 A0211 6 LLGDLVAS 0.595 79 WB VP2-3 A0211 292 WMLPLLLG 0.555 123 WB VP2-3 A0211 268 SVHSGEFI 0.540 145 WB VP2-3 A0211 303 TVTPALEA 0.519 182 WB VP2-3 A0211 3 ALALLGDL 0.514 191 WB VP2-3 A0211 32 EAAAAIEV 0.514 192 WB VP2-3 A0211 191 SLARFLEE 0.502 217 WB VP2-3 A0211 13 SVSEAAAA 0.493 240 WB VP2-3 A0211 69 VIAGAPGA 0.467 317 WB VP2-3 A0211 4 LALLGDLV 0.450 382 WB VP2-3 A0211 167 VIRDDIPA 0.450 384 WB VP2-3 A0211 293 MLPLLLGL 0.799 8 SB VP2-3 A0212 297 LLGLYGTV 0.778 11 SB VP2-3 A0212 5 ALLGDLVA 0.772 11 SB VP2-3 A0212 76 AIAGFAAL 0.741 16 SB VP2-3 A0212 146 YLDPRHWG 0.731 18 SB VP2-3 A0212 43 SLATVEGI 0.730 18 SB VP2-3 A0212 296 LLLGLYGT 0.725 19 SB VP2-3 A0212 140 FVNNIQYL 0.685 30 SB VP2-3 A0212 40 QIASLATV 0.664 37 SB VP2-3 A0212 112 GLYQQSGM 0.661 39 SB VP2-3 A0212 132 ILFPGVNT 0.661 39 SB VP2-3 A0212 80 FAALIQTV 0.654 42 SB VP2-3 A0212 155 SLFATISQ 0.649 44 SB VP2-3 A0212 62 LTPQTYAV 0.635 51 WB VP2-3 A0212 61 GLTPQTYA 0.635 51 WB VP2-3 A0212 195 FLEETTWT 0.616 63 WB VP2-3 A0212 89 GISSLAQV 0.615 64 WB VP2-3 A0212 262 DLRNKESV 0.607 70 WB VP2-3 A0212 6 LLGDLVAS 0.562 114 WB VP2-3 A0212 114 YQQSGMAL 0.562 114 WB VP2-3 A0212 69 VIAGAPGA 0.521 178 WB VP2-3 A0212 101 FSDWDHKV 0.505 211 WB VP2-3 A0212 18 AAATGFSV 0.490 249 WB VP2-3 A0212 287 RTAPQWML 0.482 270 WB VP2-3 A0212 299 GLYGTVTP 0.463 335 WB VP2-3 A0212 3 ALALLGDL 0.450 383 WB VP2-3 A0212 213 YIQDYYSN 0.440 430 WB VP2-3 A0212 297 LLGLYGTV 0.869 4 SB VP2-3 A0216 61 GLTPQTYA 0.801 8 SB VP2-3 A0216 89 GISSLAQV 0.801 8 SB VP2-3 A0216 40 QIASLATV 0.770 11 SB VP2-3 A0216 262 DLRNKESV 0.743 16 SB VP2-3 A0216 76 AIAGFAAL 0.723 20 SB VP2-3 A0216 155 SLFATISQ 0.689 28 SB VP2-3 A0216 140 FVNNIQYL 0.684 30 SB VP2-3 A0216 293 MLPLLLGL 0.670 35 SB VP2-3 A0216 5 ALLGDLVA 0.656 41 SB VP2-3 A0216 80 FAALIQTV 0.647 45 SB VP2-3 A0216 195 FLEETTWT 0.641 48 SB VP2-3 A0216 43 SLATVEGI 0.614 64 WB VP2-3 A0216 18 AAATGFSV 0.614 65 WB VP2-3 A0216 86 TVTGISSL 0.612 66 WB VP2-3 A0216 112 GLYQQSGM 0.597 78 WB VP2-3 A0216 132 ILFPGVNT 0.596 79 WB VP2-3 A0216 62 LTPQTYAV 0.580 93 WB VP2-3 A0216 250 NADSIEEV 0.545 136 WB VP2-3 A0216 296 LLLGLYGT 0.536 152 WB VP2-3 A0216 146 YLDPRHWG 0.527 167 WB VP2-3 A0216 32 EAAAAIEV 0.507 206 WB VP2-3 A0216 247 SIDNADSI 0.502 219 WB VP2-3 A0216 268 SVHSGEFI 0.451 380 WB VP2-3 A0216 250 NADSIEEV 0.620 61 WB VP2-3 A0219 40 QIASLATV 0.614 65 WB VP2-3 A0219 18 AAATGFSV 0.612 66 WB VP2-3 A0219 293 MLPLLLGL 0.609 68 WB VP2-3 A0219 43 SLATVEGI 0.596 78 WB VP2-3 A0219 146 YLDPRHWG 0.579 95 WB VP2-3 A0219 80 FAALIQTV 0.579 95 WB VP2-3 A0219 296 LLLGLYGT 0.567 108 WB VP2-3 A0219 140 FVNNIQYL 0.565 110 WB VP2-3 A0219 89 GISSLAQV 0.562 114 WB VP2-3 A0219 297 LLGLYGTV 0.543 139 WB VP2-3 A0219 61 GLTPQTYA 0.537 150 WB VP2-3 A0219 76 AIAGFAAL 0.526 168 WB VP2-3 A0219 5 ALLGDLVA 0.523 174 WB VP2-3 A0219 62 LTPQTYAV 0.508 205 WB VP2-3 A0219 86 TVTGISSL 0.502 220 WB VP2-3 A0219 195 FLEETTWT 0.500 223 WB VP2-3 A0219 32 EAAAAIEV 0.455 364 WB VP2-3 A0219 132 ILFPGVNT 0.452 374 WB VP2-3 A0219 114 YQQSGMAL 0.451 378 WB VP2-3 A0219 262 DLRNKESV 0.442 418 WB VP2-3 A0219 107 KVSTVGLY 0.604 72 WB VP2-3 A0301 322 VSRGSSQK 0.592 83 WB VP2-3 A0301 335 ASAKTTNK 0.580 93 WB VP2-3 A0301 239 HVNFGHTY 0.472 302 WB VP2-3 A0301 335 ASAKTTNK 0.732 18 SB VP2-3 A1101 270 HSGEFIEK 0.611 67 WB VP2-3 A1101 257 VTQRMDLR 0.584 90 WB VP2-3 A1101 107 KVSTVGLY 0.575 98 WB VP2-3 A1101 339 TTNKRRSR 0.528 165 WB VP2-3 A1101 92 SLAQVGYR 0.509 202 WB VP2-3 A1101 175 ITSQELQR 0.479 280 WB VP2-3 A1101 91 SSLAQVGY 0.475 293 WB VP2-3 A1101 322 VSRGSSQK 0.474 297 WB VP2-3 A1101 176 TSQELQRR 0.469 312 WB VP2-3 A1101 97 GYRFFSDW 0.582 91 WB VP2-3 A2301 145 QYLDPRHW 0.515 190 WB VP2-3 A2301 133 LFPGVNTF 0.508 205 WB VP2-3 A2301 100 FFSDWDHK 0.478 283 WB VP2-3 A2301 217 YYSNLSPI 0.443 412 WB VP2-3 A2301 194 RFLEETTW 0.435 453 WB VP2-3 A2301 217 YYSNLSPI 0.742 16 SB VP2-3 A2402 133 LFPGVNTF 0.635 51 WB VP2-3 A2402 291 QWMLPLLL 0.529 163 WB VP2-3 A2402 97 GYRFFSDW 0.659 40 SB VP2-3 A2403 194 RFLEETTW 0.644 47 SB VP2-3 A2403 217 YYSNLSPI 0.636 51 WB VP2-3 A2403 133 LFPGVNTF 0.624 58 WB VP2-3 A2403 145 QYLDPRHW 0.611 67 WB VP2-3 A2403 304 VTPALEAY 0.815 7 SB VP2-3 A2602 256 EVTQRMDL 0.685 30 SB VP2-3 A2602 122 ELFNPDEY 0.657 40 SB VP2-3 A2602 287 RTAPQWML 0.612 66 WB VP2-3 A2602 239 HVNFGHTY 0.607 69 WB VP2-3 A2602 107 KVSTVGLY 0.569 105 WB VP2-3 A2602 76 AIAGFAAL 0.544 138 WB VP2-3 A2602 267 ESVHSGEF 0.496 232 WB VP2-3 A2602 158 ATISQALW 0.474 296 WB VP2-3 A2602 140 FVNNIQYL 0.465 324 WB VP2-3 A2602 210 FYNYIQDY 0.674 34 SB VP2-3 A2902 239 HVNFGHTY 0.663 38 SB VP2-3 A2902 123 LFNPDEYY 0.588 86 WB VP2-3 A2902 139 TFVNNIQY 0.582 91 WB VP2-3 A2902 122 ELFNPDEY 0.546 136 WB VP2-3 A2902 211 YNYIQDYY 0.522 177 WB VP2-3 A2902 107 KVSTVGLY 0.502 219 WB VP2-3 A2902 204 VNAPINFY 0.450 383 WB VP2-3 A2902 322 VSRGSSQK 0.699 26 SB VP2-3 A3001 331 KGTRASAK 0.573 101 WB VP2-3 A3001 228 MVRQVAER 0.521 178 WB VP2-3 A3001 342 KRRSRSSR 0.469 312 WB VP2-3 A3001 335 ASAKTTNK 0.448 393 WB VP2-3 A3001 324 RGSSQKAK 0.442 420 WB VP2-3 A3001 107 KVSTVGLY 0.586 88 WB VP2-3 A3002 210 FYNYIQDY 0.499 226 WB VP2-3 A3002 339 TTNKRRSR 0.798 8 SB VP2-3 A3101 228 MVRQVAER 0.756 13 SB VP2-3 A3101 327 SQKAKGTR 0.755 14 SB VP2-3 A3101 257 VTQRMDLR 0.637 50 WB VP2-3 A3101 336 SAKTTNKR 0.631 53 WB VP2-3 A3101 187 FFRDSLAR 0.594 80 WB VP2-3 A3101 92 SLAQVGYR 0.593 81 WB VP2-3 A3101 218 YSNLSPIR 0.579 95 WB VP2-3 A3101 162 QALWHVIR 0.557 120 WB VP2-3 A3101 176 TSQELQRR 0.511 198 WB VP2-3 A3101 179 ELQRRTER 0.476 288 WB VP2-3 A3101 182 RRTERFFR 0.473 299 WB VP2-3 A3101 143 NIQYLDPR 0.430 474 WB VP2-3 A3101 179 ELQRRTER 0.741 16 SB VP2-3 A3301 228 MVRQVAER 0.701 25 SB VP2-3 A3301 187 FFRDSLAR 0.688 29 SB VP2-3 A3301 339 TTNKRRSR 0.662 38 SB VP2-3 A3301 143 NIQYLDPR 0.508 205 WB VP2-3 A3301 228 MVRQVAER 0.823 6 SB VP2-3 A6801 339 TTNKRRSR 0.774 11 SB VP2-3 A6801 175 ITSQELQR 0.722 20 SB VP2-3 A6801 92 SLAQVGYR 0.704 24 SB VP2-3 A6801 218 YSNLSPIR 0.701 25 SB VP2-3 A6801 253 SIEEVTQR 0.642 48 SB VP2-3 A6801 143 NIQYLDPR 0.634 52 WB VP2-3 A6801 162 QALWHVIR 0.599 76 WB VP2-3 A6801 179 ELQRRTER 0.592 82 WB VP2-3 A6801 257 VTQRMDLR 0.581 92 WB VP2-3 A6801 336 SAKTTNKR 0.571 103 WB VP2-3 A6801 176 TSQELQRR 0.567 107 WB VP2-3 A6801 270 HSGEFIEK 0.558 119 WB VP2-3 A6801 239 HVNFGHTY 0.520 180 WB VP2-3 A6801 138 NTFVNNIQ 0.471 305 WB VP2-3 A6801 122 ELFNPDEY 0.441 425 WB VP2-3 A6801 100 FFSDWDHK 0.434 458 WB VP2-3 A6801 32 EAAAAIEV 0.852 4 SB VP2-3 A6802 80 FAALIQTV 0.773 11 SB VP2-3 A6802 86 TVTGISSL 0.765 12 SB VP2-3 A6802 201 WTIVNAPI 0.749 15 SB VP2-3 A6802 55 EAIAAIGL 0.732 18 SB VP2-3 A6802 140 FVNNIQYL 0.714 22 SB VP2-3 A6802 199 TTWTIVNA 0.686 29 SB VP2-3 A6802 62 LTPQTYAV 0.667 36 SB VP2-3 A6802 244 HTYSIDNA 0.652 43 SB VP2-3 A6802 287 RTAPQWML 0.650 44 SB VP2-3 A6802 40 QIASLATV 0.640 49 SB VP2-3 A6802 0 MGAALALL 0.635 51 WB VP2-3 A6802 52 TTSEAIAA 0.624 58 WB VP2-3 A6802 27 EIAAGEAA 0.616 63 WB VP2-3 A6802 21 TGFSVAEI 0.588 86 WB VP2-3 A6802 10 LVASVSEA 0.583 90 WB VP2-3 A6802 18 AAATGFSV 0.561 115 WB VP2-3 A6802 76 AIAGFAAL 0.537 149 WB VP2-3 A6802 53 TSEAIAAI 0.500 223 WB VP2-3 A6802 303 TVTPALEA 0.475 293 WB VP2-3 A6802 185 ERFFRDSL 0.472 301 WB VP2-3 A6802 256 EVTQRMDL 0.455 363 WB VP2-3 A6802 157 FATISQAL 0.452 375 WB VP2-3 A6802 23 FSVAEIAA 0.451 380 WB VP2-3 A6802 13 SVSEAAAA 0.446 400 WB VP2-3 A6802 38 EVQIASLA 0.440 427 WB VP2-3 A6802 43 SLATVEGI 0.440 430 WB VP2-3 A6802 250 NADSIEEV 0.433 460 WB VP2-3 A6802 32 EAAAAIEV 0.788 9 SB VP2-3 A6901 199 TTWTIVNA 0.689 28 SB VP2-3 A6901 201 WTIVNAPI 0.671 35 SB VP2-3 A6901 40 QIASLATV 0.635 52 WB VP2-3 A6901 55 EAIAAIGL 0.619 61 WB VP2-3 A6901 134 FPGVNTFV 0.612 66 WB VP2-3 A6901 80 FAALIQTV 0.611 67 WB VP2-3 A6901 101 FSDWDHKV 0.563 112 WB VP2-3 A6901 27 EIAAGEAA 0.546 135 WB VP2-3 A6901 62 LTPQTYAV 0.541 143 WB VP2-3 A6901 140 FVNNIQYL 0.534 154 WB VP2-3 A6901 244 HTYSIDNA 0.533 156 WB VP2-3 A6901 250 NADSIEEV 0.521 178 WB VP2-3 A6901 52 TTSEAIAA 0.511 198 WB VP2-3 A6901 18 AAATGFSV 0.493 241 WB VP2-3 A6901 287 RTAPQWML 0.476 289 WB VP2-3 A6901 222 SPIRPSMV 0.469 313 WB VP2-3 A6901 289 APQWMLPL 0.773 11 SB VP2-3 B0702 225 RPSMVRQV 0.705 24 SB VP2-3 B0702 222 SPIRPSMV 0.604 72 WB VP2-3 B0702 153 GPSLFATI 0.482 272 WB VP2-3 B0702 134 FPGVNTFV 0.477 287 WB VP2-3 B0702 63 TPQTYAVI 0.476 289 WB VP2-3 B0702 73 APGAIAGF 0.460 343 WB VP2-3 B0702 114 YQQSGMAL 0.579 94 WB VP2-3 B1501 180 LQRRTERF 0.557 120 WB VP2-3 B1501 94 AQVGYRFF 0.550 129 WB VP2-3 B1501 239 HVNFGHTY 0.550 130 WB VP2-3 B1501 203 IVNAPINF 0.498 228 WB VP2-3 B1501 39 VQIASLAT 0.466 321 WB VP2-3 B1501 107 KVSTVGLY 0.464 331 WB VP2-3 B1501 161 SQALWHVI 0.446 400 WB VP2-3 B1501 127 DEYYDILF 0.753 14 SB VP2-3 B1801 37 IEVQIASL 0.745 15 SB VP2-3 B1801 233 AEREGTHV 0.477 286 WB VP2-3 B1801 182 RRTERFFR 0.519 182 WB VP2-3 B2705 342 KRRSRSSR 0.514 192 WB VP2-3 B2705 259 QRMDLRNK 0.511 197 WB VP2-3 B2705 320 RRVSRGSS 0.459 349 WB VP2-3 B2705 294 LPLLLGLY 0.729 18 SB VP2-3 B3501 16 EAAAATGF 0.672 34 SB VP2-3 B3501 239 HVNFGHTY 0.639 49 SB VP2-3 B3501 206 APINFYNY 0.606 71 WB VP2-3 B3501 157 FATISQAL 0.598 77 WB VP2-3 B3501 289 APQWMLPL 0.579 95 WB VP2-3 B3501 139 TFVNNIQY 0.501 221 WB VP2-3 B3501 93 LAQVGYRF 0.486 261 WB VP2-3 B3501 123 LFNPDEYY 0.476 289 WB VP2-3 B3501 73 APGAIAGF 0.469 313 WB VP2-3 B3501 114 YQQSGMAL 0.547 134 WB VP2-3 B3901 37 IEVQIASL 0.623 59 WB VP2-3 B4001 272 GEFIEKTI 0.558 118 WB VP2-3 B4001 127 DEYYDILF 0.459 346 WB VP2-3 B4001 235 REGTHVNF 0.445 404 WB VP2-3 B4001 233 AEREGTHV 0.430 476 WB VP2-3 B4001 235 REGTHVNF 0.564 111 WB VP2-3 B4002 197 EETTWTIV 0.485 263 WB VP2-3 B4002 272 GEFIEKTI 0.467 318 WB VP2-3 B4002 26 AEIAAGEA 0.493 240 WB VP2-3 B4403 235 REGTHVNF 0.426 497 WB VP2-3 B4403 26 AEIAAGEA 0.624 58 WB VP2-3 B4501 233 AEREGTHV 0.483 269 WB VP2-3 B4501 197 EETTWTIV 0.443 413 WB VP2-3 B4501 153 GPSLFATI 0.494 238 WB VP2-3 B5101 63 TPQTYAVI 0.493 241 WB VP2-3 B5101 294 LPLLLGLY 0.483 269 WB VP2-3 B5101 134 FPGVNTFV 0.466 321 WB VP2-3 B5101 222 SPIRPSMV 0.440 427 WB VP2-3 B5101 206 APINFYNY 0.677 32 SB VP2-3 B5301 134 FPGVNTFV 0.594 81 WB VP2-3 B5301 63 TPQTYAVI 0.488 254 WB VP2-3 B5301 153 GPSLFATI 0.467 320 WB VP2-3 B5301 134 FPGVNTFV 0.703 24 SB VP2-3 B5401 294 LPLLLGLY 0.526 168 WB VP2-3 B5401 80 FAALIQTV 0.437 443 WB VP2-3 B5401 158 ATISQALW 0.681 31 SB VP2-3 B5801 194 RFLEETTW 0.580 93 WB VP2-3 B5801 287 RTAPQWML 0.551 129 WB VP2-3 B5801 203 IVNAPINF 0.463 332 WB VP2-3 B5801 9-mers 138 NTFVNNIQY 0.453 373 WB VP2-3 A0101 195 FLEETTWTI 0.822 6 SB VP2-3 A0201 6 LLGDLVASV 0.810 7 SB VP2-3 A0201 292 WMLPLLLGL 0.786 10 SB VP2-3 A0201 213 YIQDYYSNL 0.758 13 SB VP2-3 A0201 61 GLTPQTYAV 0.678 32 SB VP2-3 A0201 82 ALIQTVTGI 0.643 47 SB VP2-3 A0201 299 GLYGTVTPA 0.622 59 WB VP2-3 A0201 159 TISQALWHV 0.608 69 WB VP2-3 A0201 39 VQIASLATV 0.593 81 WB VP2-3 A0201 296 LLLGLYGTV 0.532 157 WB VP2-3 A0201 155 SLFATISQA 0.509 203 WB VP2-3 A0201 3 ALALLGDLV 0.509 203 WB VP2-3 A0201 76 AIAGFAALI 0.477 288 WB VP2-3 A0201 17 AAAATGFSV 0.471 307 WB VP2-3 A0201 100 FFSDWDHKV 0.465 327 WB VP2-3 A0201 191 SLARFLEET 0.427 492 WB VP2-3 A0201 61 GLTPQTYAV 0.877 3 SB VP2-3 A0202 6 LLGDLVASV 0.801 8 SB VP2-3 A0202 195 FLEETTWTI 0.800 8 SB VP2-3 A0202 3 ALALLGDLV 0.789 9 SB VP2-3 A0202 213 YIQDYYSNL 0.759 13 SB VP2-3 A0202 159 TISQALWHV 0.692 27 SB VP2-3 A0202 155 SLFATISQA 0.675 33 SB VP2-3 A0202 292 WMLPLLLGL 0.671 35 SB VP2-3 A0202 299 GLYGTVTPA 0.656 41 SB VP2-3 A0202 82 ALIQTVTGI 0.656 41 SB VP2-3 A0202 191 SLARFLEET 0.649 44 SB VP2-3 A0202 10 LVASVSEAA 0.578 96 WB VP2-3 A0202 52 TTSEAIAAI 0.559 118 WB VP2-3 A0202 76 AIAGFAALI 0.550 130 WB VP2-3 A0202 296 LLLGLYGTV 0.537 149 WB VP2-3 A0202 39 VQIASLATV 0.505 211 WB VP2-3 A0202 33 AAAAIEVQI 0.497 231 WB VP2-3 A0202 220 NLSPIRPSM 0.483 269 WB VP2-3 A0202 80 FAALIQTVT 0.482 272 WB VP2-3 A0202 112 GLYQQSGMA 0.457 356 WB VP2-3 A0202 75 GAIAGFAAL 0.449 388 WB VP2-3 A0202 17 AAAATGFSV 0.447 396 WB VP2-3 A0202 65 QTYAVIAGA 0.445 405 WB VP2-3 A0202 36 AIEVQIASL 0.443 413 WB VP2-3 A0202 136 GVNTFVNNI 0.436 444 WB VP2-3 A0202 132 ILFPGVNTF 0.435 454 WB VP2-3 A0202 100 FFSDWDHKV 0.428 488 WB VP2-3 A0202 6 LLGDLVASV 0.941 1 SB VP2-3 A0203 299 GLYGTVTPA 0.900 2 SB VP2-3 A0203 61 GLTPQTYAV 0.878 3 SB VP2-3 A0203 82 ALIQTVTGI 0.870 4 SB VP2-3 A0203 39 VQIASLATV 0.845 5 SB VP2-3 A0203 213 YIQDYYSNL 0.840 5 SB VP2-3 A0203 292 WMLPLLLGL 0.787 10 SB VP2-3 A0203 296 LLLGLYGTV 0.779 10 SB VP2-3 A0203 195 FLEETTWTI 0.757 13 SB VP2-3 A0203 112 GLYQQSGMA 0.739 16 SB VP2-3 A0203 155 SLFATISQA 0.730 18 SB VP2-3 A0203 65 QTYAVIAGA 0.690 28 SB VP2-3 A0203 3 ALALLGDLV 0.687 29 SB VP2-3 A0203 69 VIAGAPGAI 0.670 35 SB VP2-3 A0203 136 GVNTFVNNI 0.666 37 SB VP2-3 A0203 76 AIAGFAALI 0.664 37 SB VP2-3 A0203 191 SLARFLEET 0.663 38 SB VP2-3 A0203 159 TISQALWHV 0.608 69 WB VP2-3 A0203 85 QTVTGISSL 0.606 70 WB VP2-3 A0203 52 TTSEAIAAI 0.586 88 WB VP2-3 A0203 167 VIRDDIPAI 0.553 125 WB VP2-3 A0203 17 AAAATGFSV 0.540 145 WB VP2-3 A0203 75 GAIAGFAAL 0.515 190 WB VP2-3 A0203 10 LVASVSEAA 0.487 258 WB VP2-3 A0203 18 AAATGFSVA 0.483 269 WB VP2-3 A0203 20 ATGFSVAEI 0.460 344 WB VP2-3 A0203 79 GFAALIQTV 0.447 396 WB VP2-3 A0203 220 NLSPIRPSM 0.428 485 WB VP2-3 A0203 6 LLGDLVASV 0.693 27 SB VP2-3 A0204 195 FLEETTWTI 0.675 33 SB VP2-3 A0204 61 GLTPQTYAV 0.670 35 SB VP2-3 A0204 82 ALIQTVTGI 0.615 64 WB VP2-3 A0204 155 SLFATISQA 0.590 84 WB VP2-3 A0204 296 LLLGLYGTV 0.582 91 WB VP2-3 A0204 100 FFSDWDHKV 0.570 104 WB VP2-3 A0204 17 AAAATGFSV 0.494 238 WB VP2-3 A0204 292 WMLPLLLGL 0.493 241 WB VP2-3 A0204 213 YIQDYYSNL 0.491 246 WB VP2-3 A0204 299 GLYGTVTPA 0.468 317 WB VP2-3 A0204 159 TISQALWHV 0.463 333 WB VP2-3 A0204 191 SLARFLEET 0.455 365 WB VP2-3 A0204 39 VQIASLATV 0.928 2 SB VP2-3 A0206 292 WMLPLLLGL 0.907 2 SB VP2-3 A0206 195 FLEETTWTI 0.894 3 SB VP2-3 A0206 61 GLTPQTYAV 0.849 5 SB VP2-3 A0206 159 TISQALWHV 0.830 6 SB VP2-3 A0206 6 LLGDLVASV 0.811 7 SB VP2-3 A0206 75 GAIAGFAAL 0.805 8 SB VP2-3 A0206 68 AVIAGAPGA 0.768 12 SB VP2-3 A0206 17 AAAATGFSV 0.719 20 SB VP2-3 A0206 82 ALIQTVTGI 0.701 25 SB VP2-3 A0206 296 LLLGLYGTV 0.688 29 SB VP2-3 A0206 45 ATVEGITTT 0.678 32 SB VP2-3 A0206 94 AQVGYRFFS 0.625 57 WB VP2-3 A0206 146 YLDPRHWGP 0.622 59 WB VP2-3 A0206 213 YIQDYYSNL 0.593 81 WB VP2-3 A0206 52 TTSEAIAAI 0.579 94 WB VP2-3 A0206 10 LVASVSEAA 0.547 133 WB VP2-3 A0206 129 YYDILFPGV 0.545 137 WB VP2-3 A0206 288 TAPQWMLPL 0.544 139 WB VP2-3 A0206 114 YQQSGMALE 0.542 141 WB VP2-3 A0206 246 YSIDNADSI 0.520 180 WB VP2-3 A0206 18 AAATGFSVA 0.517 186 WB VP2-3 A0206 299 GLYGTVTPA 0.516 189 WB VP2-3 A0206 85 QTVTGISSL 0.511 198 WB VP2-3 A0206 76 AIAGFAALI 0.511 198 WB VP2-3 A0206 29 AAGEAAAAI 0.508 205 WB VP2-3 A0206 132 ILFPGVNTF 0.505 210 WB VP2-3 A0206 230 RQVAEREGT 0.497 230 WB VP2-3 A0206 3 ALALLGDLV 0.496 234 WB VP2-3 A0206 65 QTYAVIAGA 0.478 282 WB VP2-3 A0206 5 ALLGDLVAS 0.462 337 WB VP2-3 A0206 167 VIRDDIPAI 0.444 409 WB VP2-3 A0206 115 QQSGMALEL 0.438 437 WB VP2-3 A0206 61 GLTPQTYAV 0.969 1 SB VP2-3 A0211 6 LLGDLVASV 0.968 1 SB VP2-3 A0211 296 LLLGLYGTV 0.950 1 SB VP2-3 A0211 292 WMLPLLLGL 0.944 1 SB VP2-3 A0211 195 FLEETTWTI 0.936 2 SB VP2-3 A0211 159 TISQALWHV 0.904 2 SB VP2-3 A0211 155 SLFATISQA 0.891 3 SB VP2-3 A0211 299 GLYGTVTPA 0.884 3 SB VP2-3 A0211 100 FFSDWDHKV 0.872 4 SB VP2-3 A0211 146 YLDPRHWGP 0.871 4 SB VP2-3 A0211 3 ALALLGDLV 0.860 4 SB VP2-3 A0211 213 YIQDYYSNL 0.850 5 SB VP2-3 A0211 220 NLSPIRPSM 0.829 6 SB VP2-3 A0211 132 ILFPGVNTF 0.826 6 SB VP2-3 A0211 76 AIAGFAALI 0.816 7 SB VP2-3 A0211 191 SLARFLEET 0.802 8 SB VP2-3 A0211 82 ALIQTVTGI 0.775 11 SB VP2-3 A0211 129 YYDILFPGV 0.734 17 SB VP2-3 A0211 92 SLAQVGYRF 0.679 32 SB VP2-3 A0211 79 GFAALIQTV 0.662 38 SB VP2-3 A0211 5 ALLGDLVAS 0.660 39 SB VP2-3 A0211 112 GLYQQSGMA 0.658 40 SB VP2-3 A0211 17 AAAATGFSV 0.657 41 SB VP2-3 A0211 295 PLLLGLYGT 0.632 53 WB VP2-3 A0211 133 LFPGVNTFV 0.594 80 WB VP2-3 A0211 167 VIRDDIPAI 0.594 81 WB VP2-3 A0211 253 SIEEVTQRM 0.567 108 WB VP2-3 A0211 86 TVTGISSLA 0.472 303 WB VP2-3 A0211 288 TAPQWMLPL 0.472 304 WB VP2-3 A0211 27 EIAAGEAAA 0.450 383 WB VP2-3 A0211 6 LLGDLVASV 0.931 2 SB VP2-3 A0212 61 GLTPQTYAV 0.924 2 SB VP2-3 A0212 296 LLLGLYGTV 0.910 2 SB VP2-3 A0212 292 WMLPLLLGL 0.910 2 SB VP2-3 A0212 213 YIQDYYSNL 0.894 3 SB VP2-3 A0212 195 FLEETTWTI 0.892 3 SB VP2-3 A0212 146 YLDPRHWGP 0.842 5 SB VP2-3 A0212 100 FFSDWDHKV 0.833 6 SB VP2-3 A0212 299 GLYGTVTPA 0.769 12 SB VP2-3 A0212 159 TISQALWHV 0.717 21 SB VP2-3 A0212 132 ILFPGVNTF 0.716 21 SB VP2-3 A0212 167 VIRDDIPAI 0.698 26 SB VP2-3 A0212 155 SLFATISQA 0.679 32 SB VP2-3 A0212 82 ALIQTVTGI 0.678 32 SB VP2-3 A0212 191 SLARFLEET 0.662 38 SB VP2-3 A0212 3 ALALLGDLV 0.654 42 SB VP2-3 A0212 129 YYDILFPGV 0.650 43 SB VP2-3 A0212 220 NLSPIRPSM 0.622 59 WB VP2-3 A0212 5 ALLGDLVAS 0.593 82 WB VP2-3 A0212 79 GFAALIQTV 0.532 157 WB VP2-3 A0212 133 LFPGVNTFV 0.528 164 WB VP2-3 A0212 295 PLLLGLYGT 0.485 261 WB VP2-3 A0212 27 EIAAGEAAA 0.471 306 WB VP2-3 A0212 17 AAAATGFSV 0.450 383 WB VP2-3 A0212 76 AIAGFAALI 0.448 393 WB VP2-3 A0212 253 SIEEVTQRM 0.430 475 WB VP2-3 A0212 6 LLGDLVASV 0.934 2 SB VP2-3 A0216 61 GLTPQTYAV 0.916 2 SB VP2-3 A0216 296 LLLGLYGTV 0.886 3 SB VP2-3 A0216 159 TISQALWHV 0.864 4 SB VP2-3 A0216 195 FLEETTWTI 0.847 5 SB VP2-3 A0216 155 SLFATISQA 0.847 5 SB VP2-3 A0216 299 GLYGTVTPA 0.835 5 SB VP2-3 A0216 213 YIQDYYSNL 0.801 8 SB VP2-3 A0216 100 FFSDWDHKV 0.789 9 SB VP2-3 A0216 133 LFPGVNTFV 0.782 10 SB VP2-3 A0216 292 WMLPLLLGL 0.764 12 SB VP2-3 A0216 3 ALALLGDLV 0.763 12 SB VP2-3 A0216 191 SLARFLEET 0.721 20 SB VP2-3 A0216 82 ALIQTVTGI 0.677 33 SB VP2-3 A0216 220 NLSPIRPSM 0.650 44 SB VP2-3 A0216 76 AIAGFAALI 0.635 51 WB VP2-3 A0216 17 AAAATGFSV 0.610 67 WB VP2-3 A0216 132 ILFPGVNTF 0.584 90 WB VP2-3 A0216 112 GLYQQSGMA 0.570 104 WB VP2-3 A0216 92 SLAQVGYRF 0.552 127 WB VP2-3 A0216 79 GFAALIQTV 0.522 176 WB VP2-3 A0216 6 LLGDLVASV 0.930 2 SB VP2-3 A0219 292 WMLPLLLGL 0.899 2 SB VP2-3 A0219 61 GLTPQTYAV 0.888 3 SB VP2-3 A0219 195 FLEETTWTI 0.848 5 SB VP2-3 A0219 159 TISQALWHV 0.840 5 SB VP2-3 A0219 100 FFSDWDHKV 0.782 10 SB VP2-3 A0219 213 YIQDYYSNL 0.736 17 SB VP2-3 A0219 296 LLLGLYGTV 0.726 19 SB VP2-3 A0219 146 YLDPRHWGP 0.682 31 SB VP2-3 A0219 82 ALIQTVTGI 0.643 47 SB VP2-3 A0219 17 AAAATGFSV 0.629 55 WB VP2-3 A0219 155 SLFATISQA 0.603 73 WB VP2-3 A0219 299 GLYGTVTPA 0.564 111 WB VP2-3 A0219 295 PLLLGLYGT 0.553 125 WB VP2-3 A0219 129 YYDILFPGV 0.529 163 WB VP2-3 A0219 220 NLSPIRPSM 0.528 164 WB VP2-3 A0219 167 VIRDDIPAI 0.507 208 WB VP2-3 A0219 132 ILFPGVNTF 0.504 214 WB VP2-3 A0219 3 ALALLGDLV 0.475 291 WB VP2-3 A0219 321 RVSRGSSQK 0.719 20 SB VP2-3 A0301 334 RASAKTTNK 0.651 43 SB VP2-3 A0301 203 IVNAPINFY 0.555 123 WB VP2-3 A0301 293 MLPLLLGLY 0.473 299 WB VP2-3 A0301 334 RASAKTTNK 0.729 18 SB VP2-3 A1101 321 RVSRGSSQK 0.724 19 SB VP2-3 A1101 91 SSLAQVGYR 0.688 29 SB VP2-3 A1101 203 IVNAPINFY 0.666 37 SB VP2-3 A1101 99 RFFSDWDHK 0.496 234 WB VP2-3 A1101 158 ATISQALWH 0.460 345 WB VP2-3 A1101 161 SQALWHVIR 0.457 356 WB VP2-3 A1101 174 AITSQELQR 0.448 392 WB VP2-3 A1101 139 TFVNNIQYL 0.584 90 WB VP2-3 A2301 187 FFRDSLARF 0.577 97 WB VP2-3 A2301 113 LYQQSGMAL 0.564 111 WB VP2-3 A2301 132 ILFPGVNTF 0.521 178 WB VP2-3 A2301 300 LYGTVTPAL 0.518 183 WB VP2-3 A2301 216 DYYSNLSPI 0.482 271 WB VP2-3 A2301 310 AYEDGPNQK 0.478 283 WB VP2-3 A2301 202 TIVNAPINF 0.466 322 WB VP2-3 A2301 99 RFFSDWDHK 0.466 323 WB VP2-3 A2301 92 SLAQVGYRF 0.459 348 WB VP2-3 A2301 300 LYGTVTPAL 0.661 39 SB VP2-3 A2402 216 DYYSNLSPI 0.637 50 WB VP2-3 A2402 156 LFATISQAL 0.560 116 WB VP2-3 A2402 113 LYQQSGMAL 0.530 160 WB VP2-3 A2402 200 TWTIVNAPI 0.452 374 WB VP2-3 A2402 113 LYQQSGMAL 0.743 16 SB VP2-3 A2403 139 TFVNNIQYL 0.591 83 WB VP2-3 A2403 187 FFRDSLARF 0.572 102 WB VP2-3 A2403 300 LYGTVTPAL 0.502 218 WB VP2-3 A2403 292 WMLPLLLGL 0.426 498 WB VP2-3 A2403 122 ELFNPDEYY 0.557 120 WB VP2-3 A2601 303 TVTPALEAY 0.843 5 SB VP2-3 A2602 203 IVNAPINFY 0.823 6 SB VP2-3 A2602 122 ELFNPDEYY 0.792 9 SB VP2-3 A2602 85 QTVTGISSL 0.778 11 SB VP2-3 A2602 213 YIQDYYSNL 0.629 55 WB VP2-3 A2602 293 MLPLLLGLY 0.578 96 WB VP2-3 A2602 179 ELQRRTERF 0.551 128 WB VP2-3 A2602 36 AIEVQIASL 0.518 183 WB VP2-3 A2602 138 NTFVNNIQY 0.503 215 WB VP2-3 A2602 187 FFRDSLARF 0.468 316 WB VP2-3 A2602 202 TIVNAPINF 0.447 398 WB VP2-3 A2602 62 LTPQTYAVI 0.442 416 WB VP2-3 A2602 210 FYNYIQDYY 0.765 12 SB VP2-3 A2902 122 ELFNPDEYY 0.716 21 SB VP2-3 A2902 138 NTFVNNIQY 0.580 94 WB VP2-3 A2902 203 IVNAPINFY 0.465 327 WB VP2-3 A2902 209 NFYNYIQDY 0.457 357 WB VP2-3 A2902 293 MLPLLLGLY 0.446 402 WB VP2-3 A2902 99 RFFSDWDHK 0.765 12 SB VP2-3 A3001 321 RVSRGSSQK 0.639 49 SB VP2-3 A3001 334 RASAKTTNK 0.593 81 WB VP2-3 A3001 186 RFFRDSLAR 0.501 222 WB VP2-3 A3001 329 KAKGTRASA 0.446 401 WB VP2-3 A3001 210 FYNYIQDYY 0.594 80 WB VP2-3 A3002 203 IVNAPINFY 0.508 205 WB VP2-3 A3002 293 MLPLLLGLY 0.466 321 WB VP2-3 A3002 338 KTTNKRRSR 0.829 6 SB VP2-3 A3101 316 NQKKRRVSR 0.804 8 SB VP2-3 A3101 227 SMVRQVAER 0.772 11 SB VP2-3 A3101 186 RFFRDSLAR 0.765 12 SB VP2-3 A3101 91 SSLAQVGYR 0.756 13 SB VP2-3 A3101 161 SQALWHVIR 0.641 48 SB VP2-3 A3101 326 SSQKAKGTR 0.632 53 WB VP2-3 A3101 334 RASAKTTNK 0.583 91 WB VP2-3 A3101 217 YYSNLSPIR 0.570 105 WB VP2-3 A3101 336 SAKTTNKRR 0.537 149 WB VP2-3 A3101 99 RFFSDWDHK 0.504 214 WB VP2-3 A3101 335 ASAKTTNKR 0.479 280 WB VP2-3 A3101 321 RVSRGSSQK 0.435 453 WB VP2-3 A3101 256 EVTQRMDLR 0.709 23 SB VP2-3 A3301 316 NQKKRRVSR 0.703 24 SB VP2-3 A3301 252 DSIEEVTQR 0.585 89 WB VP2-3 A3301 341 NKRRSRSSR 0.463 333 WB VP2-3 A3301 256 EVTQRMDLR 0.844 5 SB VP2-3 A6801 252 DSIEEVTQR 0.787 10 SB VP2-3 A6801 138 NTFVNNIQY 0.711 22 SB VP2-3 A6801 175 ITSQELQRR 0.650 44 SB VP2-3 A6801 279 IAPGGANQR 0.616 63 WB VP2-3 A6801 217 YYSNLSPIR 0.607 70 WB VP2-3 A6801 91 SSLAQVGYR 0.605 71 WB VP2-3 A6801 227 SMVRQVAER 0.599 76 WB VP2-3 A6801 335 ASAKTTNKR 0.531 160 WB VP2-3 A6801 122 ELFNPDEYY 0.510 201 WB VP2-3 A6801 210 FYNYIQDYY 0.503 217 WB VP2-3 A6801 174 AITSQELQR 0.462 338 WB VP2-3 A6801 142 NNIQYLDPR 0.461 341 WB VP2-3 A6801 326 SSQKAKGTR 0.457 357 WB VP2-3 A6801 321 RVSRGSSQK 0.456 360 WB VP2-3 A6801 303 TVTPALEAY 0.454 367 WB VP2-3 A6801 161 SQALWHVIR 0.451 379 WB VP2-3 A6801 203 IVNAPINFY 0.449 388 WB VP2-3 A6801 338 KTTNKRRSR 0.428 487 WB VP2-3 A6801 336 SAKTTNKRR 0.427 493 WB VP2-3 A6801 65 QTYAVIAGA 0.846 5 SB VP2-3 A6802 52 TTSEAIAAI 0.827 6 SB VP2-3 A6802 86 TVTGISSLA 0.764 12 SB VP2-3 A6802 10 LVASVSEAA 0.709 23 SB VP2-3 A6802 198 ETTWTIVNA 0.691 28 SB VP2-3 A6802 85 QTVTGISSL 0.677 32 SB VP2-3 A6802 16 EAAAATGFS 0.649 44 SB VP2-3 A6802 267 ESVHSGEFI 0.602 73 WB VP2-3 A6802 27 EIAAGEAAA 0.596 79 WB VP2-3 A6802 17 AAAATGFSV 0.574 100 WB VP2-3 A6802 249 DNADSIEEV 0.562 114 WB VP2-3 A6802 166 HVIRDDIPA 0.561 115 WB VP2-3 A6802 159 TISQALWHV 0.550 130 WB VP2-3 A6802 88 TGISSLAQV 0.536 151 WB VP2-3 A6802 48 EGITTTSEA 0.535 152 WB VP2-3 A6802 246 YSIDNADSI 0.523 174 WB VP2-3 A6802 76 AIAGFAALI 0.521 177 WB VP2-3 A6802 55 EAIAAIGLT 0.484 267 WB VP2-3 A6802 80 FAALIQTVT 0.481 273 WB VP2-3 A6802 152 WGPSLFATI 0.478 284 WB VP2-3 A6802 33 AAAAIEVQI 0.458 353 WB VP2-3 A6802 288 TAPQWMLPL 0.443 416 WB VP2-3 A6802 51 TTTSEAIAA 0.433 463 WB VP2-3 A6802 65 QTYAVIAGA 0.710 23 SB VP2-3 A6901 198 ETTWTIVNA 0.703 24 SB VP2-3 A6901 52 TTSEAIAAI 0.684 30 SB VP2-3 A6901 159 TISQALWHV 0.622 59 WB VP2-3 A6901 292 WMLPLLLGL 0.604 72 WB VP2-3 A6901 17 AAAATGFSV 0.601 74 WB VP2-3 A6901 27 EIAAGEAAA 0.579 94 WB VP2-3 A6901 195 FLEETTWTI 0.570 104 WB VP2-3 A6901 288 TAPQWMLPL 0.545 137 WB VP2-3 A6901 6 LLGDLVASV 0.506 209 WB VP2-3 A6901 296 LLLGLYGTV 0.472 301 WB VP2-3 A6901 100 FFSDWDHKV 0.429 484 WB VP2-3 A6901 225 RPSMVRQVA 0.705 24 SB VP2-3 B0702 172 IPAITSQEL 0.628 55 WB VP2-3 B0702 148 DPRHWGPSL 0.610 67 WB VP2-3 B0702 289 APQWMLPLL 0.598 77 WB VP2-3 B0702 314 GPNQKKRRV 0.530 162 WB VP2-3 B0702 206 APINFYNYI 0.475 294 WB VP2-3 B0702 132 ILFPGVNTF 0.606 70 WB VP2-3 B1501 203 IVNAPINFY 0.578 96 WB VP2-3 B1501 180 LQRRTERFF 0.558 118 WB VP2-3 B1501 115 QQSGMALEL 0.503 216 WB VP2-3 B1501 39 VQIASLATV 0.477 287 WB VP2-3 B1501 122 ELFNPDEYY 0.439 432 WB VP2-3 B1501 92 SLAQVGYRF 0.428 489 WB VP2-3 B1501 184 TERFFRDSL 0.622 59 WB VP2-3 B1801 292 WMLPLLLGL 0.590 84 WB VP2-3 B1801 148 DPRHWGPSL 0.584 90 WB VP2-3 B1801 54 SEAIAAIGL 0.546 135 WB VP2-3 B1801 255 EEVTQRMDL 0.451 380 WB VP2-3 B1801 15 SEAAAATGF 0.435 449 WB VP2-3 B1801 320 RRVSRGSSQ 0.507 206 WB VP2-3 B2705 303 TVTPALEAY 0.686 29 SB VP2-3 B3501 172 IPAITSQEL 0.611 67 WB VP2-3 B3501 125 NPDEYYDIL 0.606 71 WB VP2-3 B3501 238 THVNFGHTY 0.550 130 WB VP2-3 B3501 156 LFATISQAL 0.521 178 WB VP2-3 B3501 67 YAVIAGAPG 0.510 199 WB VP2-3 B3501 288 TAPQWMLPL 0.508 204 WB VP2-3 B3501 289 APQWMLPLL 0.499 225 WB VP2-3 B3501 132 ILFPGVNTF 0.484 265 WB VP2-3 B3501 80 FAALIQTVT 0.470 310 WB VP2-3 B3501 63 TPQTYAVIA 0.453 372 WB VP2-3 B3501 28 IAAGEAAAA 0.446 400 WB VP2-3 B3501 134 FPGVNTFVN 0.445 405 WB VP2-3 B3501 205 NAPINFYNY 0.437 442 WB VP2-3 B3501 13 SVSEAAAAT 0.433 461 WB VP2-3 B3501 75 GAIAGFAAL 0.429 483 WB VP2-3 B3501 54 SEAIAAIGL 0.703 24 SB VP2-3 B4001 31 GEAAAAIEV 0.632 53 WB VP2-3 B4001 255 EEVTQRMDL 0.542 141 WB VP2-3 B4001 15 SEAAAATGF 0.509 202 WB VP2-3 B4001 184 TERFFRDSL 0.467 319 WB VP2-3 B4001 266 KESVHSGEF 0.574 99 WB VP2-3 B4002 255 EEVTQRMDL 0.532 158 WB VP2-3 B4002 272 GEFIEKTIA 0.496 232 WB VP2-3 B4002 15 SEAAAATGF 0.495 235 WB VP2-3 B4002 54 SEAIAAIGL 0.445 405 WB VP2-3 B4002 54 SEAIAAIGL 0.492 243 WB VP2-3 B4403 15 SEAAAATGF 0.476 288 WB VP2-3 B4403 26 AEIAAGEAA 0.466 322 WB VP2-3 B4403 26 AEIAAGEAA 0.639 49 SB VP2-3 B4501 255 EEVTQRMDL 0.521 178 WB VP2-3 B4501 31 GEAAAAIEV 0.456 361 WB VP2-3 B4501 197 EETTWTIVN 0.432 464 WB VP2-3 B4501 206 APINFYNYI 0.497 230 WB VP2-3 B5101 294 LPLLLGLYG 0.451 381 WB VP2-3 B5101 206 APINFYNYI 0.608 69 WB VP2-3 B5301 289 APQWMLPLL 0.545 136 WB VP2-3 B5301 157 FATISQALW 0.522 176 WB VP2-3 B5301 206 APINFYNYI 0.614 64 WB VP2-3 B5401 73 APGAIAGFA 0.573 100 WB VP2-3 B5401 119 MALELFNPD 0.511 199 WB VP2-3 B5401 134 FPGVNTFVN 0.502 218 WB VP2-3 B5401 294 LPLLLGLYG 0.488 254 WB VP2-3 B5401 63 TPQTYAVIA 0.478 282 WB VP2-3 B5401 80 FAALIQTVT 0.464 329 WB VP2-3 B5401 157 FATISQALW 0.723 19 SB VP2-3 B5801 90 ISSLAQVGY 0.546 136 WB VP2-3 B5801 96 VGYRFFSDW 0.481 274 WB VP2-3 B5801 10-mers 237 GTHVNFGHTY 0.517 185 WB VP2-3 A0101 5 ALLGDLVASV 0.820 6 SB VP2-3 A0201 132 ILFPGVNTFV 0.785 10 SB VP2-3 A0201 299 GLYGTVTPAL 0.721 20 SB VP2-3 A0201 195 FLEETTWTIV 0.703 24 SB VP2-3 A0201 155 SLFATISQAL 0.632 53 WB VP2-3 A0201 114 YQQSGMALEL 0.529 162 WB VP2-3 A0201 158 ATISQALWHV 0.476 288 WB VP2-3 A0201 199 TTWTIVNAPI 0.473 298 WB VP2-3 A0201 61 GLTPQTYAVI 0.471 305 WB VP2-3 A0201 112 GLYQQSGMAL 0.455 364 WB VP2-3 A0201 260 RMDLRNKESV 0.442 418 WB VP2-3 A0201 220 NLSPIRPSMV 0.436 445 WB VP2-3 A0201 163 ALWHVIRDDI 0.430 476 WB VP2-3 A0201 132 ILFPGVNTFV 0.798 8 SB VP2-3 A0202 5 ALLGDLVASV 0.785 10 SB VP2-3 A0202 155 SLFATISQAL 0.742 16 SB VP2-3 A0202 299 GLYGTVTPAL 0.680 32 SB VP2-3 A0202 112 GLYQQSGMAL 0.654 42 SB VP2-3 A0202 195 FLEETTWTIV 0.589 85 WB VP2-3 A0202 3 ALALLGDLVA 0.583 91 WB VP2-3 A0202 191 SLARFLEETT 0.557 120 WB VP2-3 A0202 114 YQQSGMALEL 0.554 124 WB VP2-3 A0202 296 LLLGLYGTVT 0.537 149 WB VP2-3 A0202 138 NTFVNNIQYL 0.525 170 WB VP2-3 A0202 220 NLSPIRPSMV 0.519 182 WB VP2-3 A0202 158 ATISQALWHV 0.501 222 WB VP2-3 A0202 10 LVASVSEAAA 0.479 280 WB VP2-3 A0202 61 GLTPQTYAVI 0.466 322 WB VP2-3 A0202 124 FNPDEYYDIL 0.461 342 WB VP2-3 A0202 295 PLLLGLYGTV 0.450 382 WB VP2-3 A0202 260 RMDLRNKESV 0.447 397 WB VP2-3 A0202 293 MLPLLLGLYG 0.427 492 WB VP2-3 A0202 2 AALALLGDLV 0.426 498 WB VP2-3 A0202 132 ILFPGVNTFV 0.888 3 SB VP2-3 A0203 5 ALLGDLVASV 0.868 4 SB VP2-3 A0203 195 FLEETTWTIV 0.820 7 SB VP2-3 A0203 299 GLYGTVTPAL 0.803 8 SB VP2-3 A0203 220 NLSPIRPSMV 0.788 9 SB VP2-3 A0203 112 GLYQQSGMAL 0.756 14 SB VP2-3 A0203 61 GLTPQTYAVI 0.703 24 SB VP2-3 A0203 155 SLFATISQAL 0.700 25 SB VP2-3 A0203 239 HVNFGHTYSI 0.663 38 SB VP2-3 A0203 287 RTAPQWMLPL 0.629 55 WB VP2-3 A0203 260 RMDLRNKESV 0.533 156 WB VP2-3 A0203 191 SLARFLEETT 0.530 161 WB VP2-3 A0203 68 AVIAGAPGAI 0.529 163 WB VP2-3 A0203 158 ATISQALWHV 0.516 187 WB VP2-3 A0203 24 SVAEIAAGEA 0.513 193 WB VP2-3 A0203 114 YQQSGMALEL 0.513 194 WB VP2-3 A0203 35 AAIEVQIASL 0.509 203 WB VP2-3 A0203 295 PLLLGLYGTV 0.503 217 WB VP2-3 A0203 69 VIAGAPGAIA 0.490 248 WB VP2-3 A0203 3 ALALLGDLVA 0.472 303 WB VP2-3 A0203 10 LVASVSEAAA 0.471 304 WB VP2-3 A0203 75 GAIAGFAALI 0.453 373 WB VP2-3 A0203 85 QTVTGISSLA 0.440 425 WB VP2-3 A0203 43 SLATVEGITT 0.431 473 WB VP2-3 A0203 132 ILFPGVNTFV 0.738 17 SB VP2-3 A0204 195 FLEETTWTIV 0.686 30 SB VP2-3 A0204 5 ALLGDLVASV 0.678 32 SB VP2-3 A0204 155 SLFATISQAL 0.630 54 WB VP2-3 A0204 158 ATISQALWHV 0.567 108 WB VP2-3 A0204 299 GLYGTVTPAL 0.485 263 WB VP2-3 A0204 112 GLYQQSGMAL 0.468 317 WB VP2-3 A0204 287 RTAPQWMLPL 0.457 356 WB VP2-3 A0204 5 ALLGDLVASV 0.873 3 SB VP2-3 A0206 195 FLEETTWTIV 0.869 4 SB VP2-3 A0206 132 ILFPGVNTFV 0.865 4 SB VP2-3 A0206 114 YQQSGMALEL 0.803 8 SB VP2-3 A0206 158 ATISQALWHV 0.779 10 SB VP2-3 A0206 35 AAIEVQIASL 0.711 22 SB VP2-3 A0206 75 GAIAGFAALI 0.649 44 SB VP2-3 A0206 287 RTAPQWMLPL 0.626 57 WB VP2-3 A0206 299 GLYGTVTPAL 0.599 76 WB VP2-3 A0206 68 AVIAGAPGAI 0.591 83 WB VP2-3 A0206 67 YAVIAGAPGA 0.588 86 WB VP2-3 A0206 84 IQTVTGISSL 0.569 105 WB VP2-3 A0206 2 AALALLGDLV 0.550 129 WB VP2-3 A0206 94 AQVGYRFFSD 0.537 150 WB VP2-3 A0206 146 YLDPRHWGPS 0.525 169 WB VP2-3 A0206 260 RMDLRNKESV 0.525 170 WB VP2-3 A0206 166 HVIRDDIPAI 0.513 193 WB VP2-3 A0206 288 TAPQWMLPLL 0.507 208 WB VP2-3 A0206 155 SLFATISQAL 0.500 223 WB VP2-3 A0206 39 VQIASLATVE 0.488 254 WB VP2-3 A0206 24 SVAEIAAGEA 0.488 255 WB VP2-3 A0206 194 RFLEETTWTI 0.480 276 WB VP2-3 A0206 10 LVASVSEAAA 0.470 309 WB VP2-3 A0206 112 GLYQQSGMAL 0.466 322 WB VP2-3 A0206 220 NLSPIRPSMV 0.460 344 WB VP2-3 A0206 159 TISQALWHVI 0.458 353 WB VP2-3 A0206 17 AAAATGFSVA 0.457 354 WB VP2-3 A0206 45 ATVEGITTTS 0.454 365 WB VP2-3 A0206 231 QVAEREGTHV 0.453 371 WB VP2-3 A0206 78 AGFAALIQTV 0.448 394 WB VP2-3 A0206 115 QQSGMALELF 0.438 437 WB VP2-3 A0206 81 AALIQTVTGI 0.433 460 WB VP2-3 A0206 61 GLTPQTYAVI 0.432 466 WB VP2-3 A0206 132 ILFPGVNTFV 0.975 1 SB VP2-3 A0211 5 ALLGDLVASV 0.972 1 SB VP2-3 A0211 155 SLFATISQAL 0.940 1 SB VP2-3 A0211 299 GLYGTVTPAL 0.939 1 SB VP2-3 A0211 195 FLEETTWTIV 0.931 2 SB VP2-3 A0211 260 RMDLRNKESV 0.912 2 SB VP2-3 A0211 220 NLSPIRPSMV 0.891 3 SB VP2-3 A0211 295 PLLLGLYGTV 0.885 3 SB VP2-3 A0211 112 GLYQQSGMAL 0.864 4 SB VP2-3 A0211 61 GLTPQTYAVI 0.850 5 SB VP2-3 A0211 146 YLDPRHWGPS 0.740 16 SB VP2-3 A0211 191 SLARFLEETT 0.737 17 SB VP2-3 A0211 128 EYYDILFPGV 0.731 18 SB VP2-3 A0211 159 TISQALWHVI 0.674 34 SB VP2-3 A0211 102 SDWDHKVSTV 0.641 48 SB VP2-3 A0211 292 WMLPLLLGLY 0.638 50 WB VP2-3 A0211 163 ALWHVIRDDI 0.620 60 WB VP2-3 A0211 3 ALALLGDLVA 0.616 63 WB VP2-3 A0211 92 SLAQVGYRFF 0.615 64 WB VP2-3 A0211 158 ATISQALWHV 0.598 77 WB VP2-3 A0211 99 RFFSDWDHKV 0.596 79 WB VP2-3 A0211 287 RTAPQWMLPL 0.585 89 WB VP2-3 A0211 78 AGFAALIQTV 0.570 105 WB VP2-3 A0211 43 SLATVEGITT 0.568 107 WB VP2-3 A0211 223 PIRPSMVRQV 0.566 109 WB VP2-3 A0211 296 LLLGLYGTVT 0.548 133 WB VP2-3 A0211 38 EVQIASLATV 0.532 158 WB VP2-3 A0211 114 YQQSGMALEL 0.530 162 WB VP2-3 A0211 194 RFLEETTWTI 0.518 184 WB VP2-3 A0211 239 HVNFGHTYSI 0.510 199 WB VP2-3 A0211 24 SVAEIAAGEA 0.497 230 WB VP2-3 A0211 171 DIPAITSQEL 0.484 265 WB VP2-3 A0211 231 QVAEREGTHV 0.484 265 WB VP2-3 A0211 288 TAPQWMLPLL 0.470 310 WB VP2-3 A0211 16 EAAAATGFSV 0.464 330 WB VP2-3 A0211 87 VTGISSLAQV 0.454 366 WB VP2-3 A0211 6 LLGDLVASVS 0.453 372 WB VP2-3 A0211 35 AAIEVQIASL 0.437 439 WB VP2-3 A0211 132 ILFPGVNTFV 0.943 1 SB VP2-3 A0212 5 ALLGDLVASV 0.935 2 SB VP2-3 A0212 195 FLEETTWTIV 0.906 2 SB VP2-3 A0212 299 GLYGTVTPAL 0.904 2 SB VP2-3 A0212 155 SLFATISQAL 0.880 3 SB VP2-3 A0212 260 RMDLRNKESV 0.826 6 SB VP2-3 A0212 220 NLSPIRPSMV 0.779 10 SB VP2-3 A0212 112 GLYQQSGMAL 0.778 11 SB VP2-3 A0212 295 PLLLGLYGTV 0.757 13 SB VP2-3 A0212 191 SLARFLEETT 0.661 39 SB VP2-3 A0212 61 GLTPQTYAVI 0.654 42 SB VP2-3 A0212 163 ALWHVIRDDI 0.638 50 WB VP2-3 A0212 128 EYYDILFPGV 0.616 63 WB VP2-3 A0212 146 YLDPRHWGPS 0.615 64 WB VP2-3 A0212 114 YQQSGMALEL 0.540 145 WB VP2-3 A0212 296 LLLGLYGTVT 0.537 149 WB VP2-3 A0212 102 SDWDHKVSTV 0.537 150 WB VP2-3 A0212 231 QVAEREGTHV 0.480 278 WB VP2-3 A0212 292 WMLPLLLGLY 0.456 358 WB VP2-3 A0212 158 ATISQALWHV 0.442 419 WB VP2-3 A0212 99 RFFSDWDHKV 0.441 423 WB VP2-3 A0212 213 YIQDYYSNLS 0.431 472 WB VP2-3 A0212 132 ILFPGVNTFV 0.955 1 SB VP2-3 A0216 5 ALLGDLVASV 0.929 2 SB VP2-3 A0216 299 GLYGTVTPAL 0.896 3 SB VP2-3 A0216 195 FLEETTWTIV 0.888 3 SB VP2-3 A0216 220 NLSPIRPSMV 0.866 4 SB VP2-3 A0216 155 SLFATISQAL 0.857 4 SB VP2-3 A0216 295 PLLLGLYGTV 0.819 7 SB VP2-3 A0216 260 RMDLRNKESV 0.787 9 SB VP2-3 A0216 112 GLYQQSGMAL 0.782 10 SB VP2-3 A0216 61 GLTPQTYAVI 0.651 43 SB VP2-3 A0216 191 SLARFLEETT 0.648 45 SB VP2-3 A0216 158 ATISQALWHV 0.620 60 WB VP2-3 A0216 102 SDWDHKVSTV 0.575 99 WB VP2-3 A0216 163 ALWHVIRDDI 0.562 114 WB VP2-3 A0216 231 QVAEREGTHV 0.553 125 WB VP2-3 A0216 128 EYYDILFPGV 0.552 126 WB VP2-3 A0216 38 EVQIASLATV 0.550 130 WB VP2-3 A0216 223 PIRPSMVRQV 0.520 179 WB VP2-3 A0216 43 SLATVEGITT 0.498 229 WB VP2-3 A0216 99 RFFSDWDHKV 0.498 229 WB VP2-3 A0216 171 DIPAITSQEL 0.485 262 WB VP2-3 A0216 87 VTGISSLAQV 0.455 363 WB VP2-3 A0216 16 EAAAATGFSV 0.451 379 WB VP2-3 A0216 114 YQQSGMALEL 0.446 401 WB VP2-3 A0216 78 AGFAALIQTV 0.438 434 WB VP2-3 A0216 3 ALALLGDLVA 0.434 456 WB VP2-3 A0216 59 AIGLTPQTYA 0.433 460 WB VP2-3 A0216 296 LLLGLYGTVT 0.427 492 WB VP2-3 A0216 5 ALLGDLVASV 0.918 2 SB VP2-3 A0219 195 FLEETTWTIV 0.849 5 SB VP2-3 A0219 299 GLYGTVTPAL 0.826 6 SB VP2-3 A0219 220 NLSPIRPSMV 0.768 12 SB VP2-3 A0219 155 SLFATISQAL 0.750 14 SB VP2-3 A0219 260 RMDLRNKESV 0.698 26 SB VP2-3 A0219 295 PLLLGLYGTV 0.664 37 SB VP2-3 A0219 61 GLTPQTYAVI 0.545 137 WB VP2-3 A0219 114 YQQSGMALEL 0.523 175 WB VP2-3 A0219 128 EYYDILFPGV 0.521 177 WB VP2-3 A0219 159 TISQALWHVI 0.498 228 WB VP2-3 A0219 16 EAAAATGFSV 0.480 277 WB VP2-3 A0219 112 GLYQQSGMAL 0.441 424 WB VP2-3 A0219 158 ATISQALWHV 0.439 430 WB VP2-3 A0219 268 SVHSGEFIEK 0.544 139 WB VP2-3 A0301 329 KAKGTRASAK 0.506 208 WB VP2-3 A0301 320 RRVSRGSSQK 0.471 306 WB VP2-3 A0301 202 TIVNAPINFY 0.464 331 WB VP2-3 A0301 292 WMLPLLLGLY 0.456 358 WB VP2-3 A0301 268 SVHSGEFIEK 0.783 10 SB VP2-3 A1101 257 VTQRMDLRNK 0.698 26 SB VP2-3 A1101 160 ISQALWHVIR 0.561 115 WB VP2-3 A1101 329 KAKGTRASAK 0.536 152 WB VP2-3 A1101 202 TIVNAPINFY 0.497 230 WB VP2-3 A1101 90 ISSLAQVGYR 0.464 329 WB VP2-3 A1101 212 NYIQDYYSNL 0.652 43 SB VP2-3 A2301 186 RFFRDSLARF 0.651 43 SB VP2-3 A2301 194 RFLEETTWTI 0.548 132 WB VP2-3 A2301 201 WTIVNAPINF 0.547 135 WB VP2-3 A2301 310 AYEDGPNQKK 0.490 250 WB VP2-3 A2301 245 TYSIDNADSI 0.489 252 WB VP2-3 A2301 91 SSLAQVGYRF 0.461 340 WB VP2-3 A2301 179 ELQRRTERFF 0.429 482 WB VP2-3 A2301 212 NYIQDYYSNL 0.650 44 SB VP2-3 A2402 194 RFLEETTWTI 0.609 69 WB VP2-3 A2402 151 HWGPSLFATI 0.540 145 WB VP2-3 A2402 245 TYSIDNADSI 0.529 162 WB VP2-3 A2402 186 RFFRDSLARF 0.484 266 WB VP2-3 A2402 156 LFATISQALW 0.476 290 WB VP2-3 A2402 194 RFLEETTWTI 0.667 36 SB VP2-3 A2403 186 RFFRDSLARF 0.659 39 SB VP2-3 A2403 212 NYIQDYYSNL 0.619 62 WB VP2-3 A2403 245 TYSIDNADSI 0.461 341 WB VP2-3 A2403 291 QWMLPLLLGL 0.429 481 WB VP2-3 A2403 202 TIVNAPINFY 0.620 60 WB VP2-3 A2601 252 DSIEEVTQRM 0.617 63 WB VP2-3 A2601 202 TIVNAPINFY 0.801 8 SB VP2-3 A2602 302 GTVTPALEAY 0.771 11 SB VP2-3 A2602 287 RTAPQWMLPL 0.760 13 SB VP2-3 A2602 201 WTIVNAPINF 0.744 15 SB VP2-3 A2602 179 ELQRRTERFF 0.735 17 SB VP2-3 A2602 171 DIPAITSQEL 0.532 158 WB VP2-3 A2602 166 HVIRDDIPAI 0.531 159 WB VP2-3 A2602 131 DILFPGVNTF 0.488 253 WB VP2-3 A2602 38 EVQIASLATV 0.471 304 WB VP2-3 A2602 209 NFYNYIQDYY 0.572 102 WB VP2-3 A2902 204 VNAPINFYNY 0.549 131 WB VP2-3 A2902 292 WMLPLLLGLY 0.547 134 WB VP2-3 A2902 329 KAKGTRASAK 0.783 10 SB VP2-3 A3001 322 VSRGSSQKAK 0.757 13 SB VP2-3 A3001 268 SVHSGEFIEK 0.678 32 SB VP2-3 A3001 180 LQRRTERFFR 0.485 263 WB VP2-3 A3001 237 GTHVNFGHTY 0.479 281 WB VP2-3 A3001 89 GISSLAQVGY 0.518 184 WB VP2-3 A3002 292 WMLPLLLGLY 0.511 198 WB VP2-3 A3002 209 NFYNYIQDYY 0.475 292 WB VP2-3 A3002 202 TIVNAPINFY 0.437 443 WB VP2-3 A3002 180 LQRRTERFFR 0.756 14 SB VP2-3 A3101 334 RASAKTTNKR 0.645 46 SB VP2-3 A3101 337 AKTTNKRRSR 0.606 71 WB VP2-3 A3101 160 ISQALWHVIR 0.591 83 WB VP2-3 A3101 174 AITSQELQRR 0.577 97 WB VP2-3 A3101 177 SQELQRRTER 0.543 140 WB VP2-3 A3101 329 KAKGTRASAK 0.520 180 WB VP2-3 A3101 90 ISSLAQVGYR 0.491 246 WB VP2-3 A3101 340 TNKRRSRSSR 0.489 252 WB VP2-3 A3101 226 PSMVRQVAER 0.471 305 WB VP2-3 A3101 335 ASAKTTNKRR 0.455 363 WB VP2-3 A3101 315 PNQKKRRVSR 0.448 393 WB VP2-3 A3101 216 DYYSNLSPIR 0.588 86 WB VP2-3 A3301 180 LQRRTERFFR 0.560 116 WB VP2-3 A3301 160 ISQALWHVIR 0.507 206 WB VP2-3 A3301 278 TIAPGGANQR 0.743 16 SB VP2-3 A6801 309 EAYEDGPNQK 0.741 16 SB VP2-3 A6801 90 ISSLAQVGYR 0.713 22 SB VP2-3 A6801 216 DYYSNLSPIR 0.707 23 SB VP2-3 A6801 268 SVHSGEFIEK 0.645 46 SB VP2-3 A6801 185 ERFFRDSLAR 0.541 142 WB VP2-3 A6801 334 RASAKTTNKR 0.535 152 WB VP2-3 A6801 202 TIVNAPINFY 0.532 158 WB VP2-3 A6801 160 ISQALWHVIR 0.498 228 WB VP2-3 A6801 255 EEVTQRMDLR 0.495 237 WB VP2-3 A6801 209 NFYNYIQDYY 0.464 329 WB VP2-3 A6801 221 LSPIRPSMVR 0.439 434 WB VP2-3 A6801 16 EAAAATGFSV 0.886 3 SB VP2-3 A6802 199 TTWTIVNAPI 0.877 3 SB VP2-3 A6802 32 EAAAAIEVQI 0.797 8 SB VP2-3 A6802 138 NTFVNNIQYL 0.763 12 SB VP2-3 A6802 239 HVNFGHTYSI 0.707 23 SB VP2-3 A6802 287 RTAPQWMLPL 0.692 28 SB VP2-3 A6802 24 SVAEIAAGEA 0.669 36 SB VP2-3 A6802 51 TTTSEAIAAI 0.664 38 SB VP2-3 A6802 205 NAPINFYNYI 0.663 38 SB VP2-3 A6802 27 EIAAGEAAAA 0.642 47 SB VP2-3 A6802 48 EGITTTSEAI 0.641 48 SB VP2-3 A6802 85 QTVTGISSLA 0.637 50 WB VP2-3 A6802 38 EVQIASLATV 0.608 69 WB VP2-3 A6802 171 DIPAITSQEL 0.587 86 WB VP2-3 A6802 10 LVASVSEAAA 0.570 105 WB VP2-3 A6802 128 EYYDILFPGV 0.563 113 WB VP2-3 A6802 220 NLSPIRPSMV 0.549 130 WB VP2-3 A6802 132 ILFPGVNTFV 0.545 138 WB VP2-3 A6802 166 HVIRDDIPAI 0.535 152 WB VP2-3 A6802 155 SLFATISQAL 0.516 188 WB VP2-3 A6802 159 TISQALWHVI 0.500 223 WB VP2-3 A6802 28 IAAGEAAAAI 0.487 257 WB VP2-3 A6802 231 QVAEREGTHV 0.474 296 WB VP2-3 A6802 158 ATISQALWHV 0.457 357 WB VP2-3 A6802 41 IASLATVEGI 0.435 450 WB VP2-3 A6802 16 EAAAATGFSV 0.809 7 SB VP2-3 A6901 199 TTWTIVNAPI 0.775 11 SB VP2-3 A6901 128 EYYDILFPGV 0.674 34 SB VP2-3 A6901 38 EVQIASLATV 0.655 41 SB VP2-3 A6901 138 NTFVNNIQYL 0.647 45 SB VP2-3 A6901 158 ATISQALWHV 0.607 69 WB VP2-3 A6901 32 EAAAAIEVQI 0.603 73 WB VP2-3 A6901 27 EIAAGEAAAA 0.569 105 WB VP2-3 A6901 239 HVNFGHTYSI 0.516 187 WB VP2-3 A6901 287 RTAPQWMLPL 0.511 198 WB VP2-3 A6901 166 HVIRDDIPAI 0.505 210 WB VP2-3 A6901 132 ILFPGVNTFV 0.497 229 WB VP2-3 A6901 231 QVAEREGTHV 0.482 271 WB VP2-3 A6901 5 ALLGDLVASV 0.460 346 WB VP2-3 A6901 51 TTTSEAIAAI 0.451 381 WB VP2-3 A6901 87 VTGISSLAQV 0.440 426 WB VP2-3 A6901 288 TAPQWMLPLL 0.437 441 WB VP2-3 A6901 24 SVAEIAAGEA 0.434 456 WB VP2-3 A6901 289 APQWMLPLLL 0.641 48 SB VP2-3 B0702 225 RPSMVRQVAE 0.621 60 WB VP2-3 B0702 148 DPRHWGPSLF 0.517 185 WB VP2-3 B0702 73 APGAIAGFAA 0.513 194 WB VP2-3 B0702 292 WMLPLLLGLY 0.543 140 WB VP2-3 B1501 115 QQSGMALELF 0.542 141 WB VP2-3 B1501 114 YQQSGMALEL 0.537 150 WB VP2-3 B1501 84 IQTVTGISSL 0.522 176 WB VP2-3 B1501 155 SLFATISQAL 0.494 238 WB VP2-3 B1501 230 RQVAEREGTH 0.480 276 WB VP2-3 B1501 92 SLAQVGYRFF 0.475 291 WB VP2-3 B1501 58 AAIGLTPQTY 0.469 311 WB VP2-3 B1501 237 GTHVNFGHTY 0.447 398 WB VP2-3 B1501 299 GLYGTVTPAL 0.434 457 WB VP2-3 B1501 201 WTIVNAPINF 0.426 497 WB VP2-3 B1501 233 AEREGTHVNF 0.711 22 SB VP2-3 B1801 121 LELFNPDEYY 0.515 189 WB VP2-3 B1801 178 QELQRRTERF 0.507 207 WB VP2-3 B1801 37 IEVQIASLAT 0.487 257 WB VP2-3 B1801 148 DPRHWGPSLF 0.482 273 WB VP2-3 B1801 292 WMLPLLLGLY 0.445 407 WB VP2-3 B1801 320 RRVSRGSSQK 0.631 54 WB VP2-3 B2705 98 YRFFSDWDHK 0.450 383 WB VP2-3 B2705 125 NPDEYYDILF 0.757 13 SB VP2-3 B3501 58 AAIGLTPQTY 0.566 109 WB VP2-3 B3501 148 DPRHWGPSLF 0.544 138 WB VP2-3 B3501 28 IAAGEAAAAI 0.514 192 WB VP2-3 B3501 202 TIVNAPINFY 0.476 289 WB VP2-3 B3501 67 YAVIAGAPGA 0.456 358 WB VP2-3 B3501 292 WMLPLLLGLY 0.447 397 WB VP2-3 B3501 209 NFYNYIQDYY 0.429 480 WB VP2-3 B3501 114 YQQSGMALEL 0.466 323 WB VP2-3 B3901 233 AEREGTHVNF 0.508 204 WB VP2-3 B4001 254 IEEVTQRMDL 0.497 230 WB VP2-3 B4001 266 KESVHSGEFI 0.457 355 WB VP2-3 B4002 233 AEREGTHVNF 0.450 382 WB VP2-3 B4002 26 AEIAAGEAAA 0.461 340 WB VP2-3 B4403 26 AEIAAGEAAA 0.637 50 WB VP2-3 B4501 197 EETTWTIVNA 0.481 273 WB VP2-3 B4501 233 AEREGTHVNF 0.474 297 WB VP2-3 B4501 294 LPLLLGLYGT 0.583 91 WB VP2-3 B5101 289 APQWMLPLLL 0.580 94 WB VP2-3 B5301 125 NPDEYYDILF 0.476 289 WB VP2-3 B5301 294 LPLLLGLYGT 0.816 7 SB VP2-3 B5401 73 APGAIAGFAA 0.666 36 SB VP2-3 B5401 134 FPGVNTFVNN 0.529 163 WB VP2-3 B5401 192 LARFLEETTW 0.441 422 WB VP2-3 B5701 283 GANQRTAPQW 0.661 39 SB VP2-3 B5801 192 LARFLEETTW 0.570 105 WB VP2-3 B5801 201 WTIVNAPINF 0.543 139 WB VP2-3 B5801 156 LFATISQALW 0.490 247 WB VP2-3 B5801 287 RTAPQWMLPL 0.462 337 WB VP2-3 B5801 91 SSLAQVGYRF 0.439 432 WB VP2-3 B5801 11-mers 201 WTIVNAPINFY 0.505 212 WB VP2-3 A0101 146 YLDPRHWGPSL 0.844 5 SB VP2-3 A0201 247 SIDNADSIEEV 0.608 69 WB VP2-3 A0201 157 FATISQALWHV 0.499 226 WB VP2-3 A0201 297 LLGLYGTVTPA 0.443 413 WB VP2-3 A0201 61 GLTPQTYAVIA 0.440 428 WB VP2-3 A0201 80 FAALIQTVTGI 0.740 16 SB VP2-3 A0202 146 YLDPRHWGPSL 0.686 29 SB VP2-3 A0202 297 LLGLYGTVTPA 0.612 66 WB VP2-3 A0202 293 MLPLLLGLYGT 0.607 69 WB VP2-3 A0202 61 GLTPQTYAVIA 0.598 77 WB VP2-3 A0202 24 SVAEIAAGEAA 0.577 96 WB VP2-3 A0202 157 FATISQALWHV 0.572 102 WB VP2-3 A0202 52 TTSEAIAAIGL 0.559 117 WB VP2-3 A0202 40 QIASLATVEGI 0.554 124 WB VP2-3 A0202 287 RTAPQWMLPLL 0.542 142 WB VP2-3 A0202 247 SIDNADSIEEV 0.539 146 WB VP2-3 A0202 92 SLAQVGYRFFS 0.525 170 WB VP2-3 A0202 10 LVASVSEAAAA 0.525 170 WB VP2-3 A0202 59 AIGLTPQTYAV 0.518 183 WB VP2-3 A0202 86 TVTGISSLAQV 0.493 241 WB VP2-3 A0202 43 SLATVEGITTT 0.487 258 WB VP2-3 A0202 3 ALALLGDLVAS 0.480 278 WB VP2-3 A0202 34 AAAIEVQIASL 0.471 305 WB VP2-3 A0202 83 LIQTVTGISSL 0.467 318 WB VP2-3 A0202 1 GAALALLGDLV 0.467 320 WB VP2-3 A0202 244 HTYSIDNADSI 0.466 324 WB VP2-3 A0202 155 SLFATISQALW 0.458 350 WB VP2-3 A0202 274 FIEKTIAPGGA 0.427 490 WB VP2-3 A0202 140 FVNNIQYLDPR 0.427 492 WB VP2-3 A0202 146 YLDPRHWGPSL 0.801 8 SB VP2-3 A0203 297 LLGLYGTVTPA 0.759 13 SB VP2-3 A0203 83 LIQTVTGISSL 0.719 20 SB VP2-3 A0203 293 MLPLLLGLYGT 0.711 22 SB VP2-3 A0203 80 FAALIQTVTGI 0.669 36 SB VP2-3 A0203 43 SLATVEGITTT 0.657 40 SB VP2-3 A0203 59 AIGLTPQTYAV 0.639 49 SB VP2-3 A0203 61 GLTPQTYAVIA 0.610 67 WB VP2-3 A0203 18 AAATGFSVAEI 0.562 114 WB VP2-3 A0203 40 QIASLATVEGI 0.559 118 WB VP2-3 A0203 86 TVTGISSLAQV 0.542 141 WB VP2-3 A0203 287 RTAPQWMLPLL 0.526 168 WB VP2-3 A0203 274 FIEKTIAPGGA 0.518 183 WB VP2-3 A0203 10 LVASVSEAAAA 0.513 193 WB VP2-3 A0203 4 LALLGDLVASV 0.490 248 WB VP2-3 A0203 24 SVAEIAAGEAA 0.488 253 WB VP2-3 A0203 34 AAAIEVQIASL 0.478 283 WB VP2-3 A0203 327 SQKAKGTRASA 0.474 294 WB VP2-3 A0203 247 SIDNADSIEEV 0.455 365 WB VP2-3 A0203 157 FATISQALWHV 0.447 396 WB VP2-3 A0203 101 FSDWDHKVSTV 0.447 398 WB VP2-3 A0203 67 YAVIAGAPGAI 0.430 477 WB VP2-3 A0203 146 YLDPRHWGPSL 0.615 64 WB VP2-3 A0204 29 AAGEAAAAIEV 0.520 180 WB VP2-3 A0204 59 AIGLTPQTYAV 0.517 185 WB VP2-3 A0204 297 LLGLYGTVTPA 0.495 236 WB VP2-3 A0204 247 SIDNADSIEEV 0.488 255 WB VP2-3 A0204 43 SLATVEGITTT 0.466 322 WB VP2-3 A0204 146 YLDPRHWGPSL 0.882 3 SB VP2-3 A0206 214 IQDYYSNLSPI 0.767 12 SB VP2-3 A0206 230 RQVAEREGTHV 0.764 12 SB VP2-3 A0206 157 FATISQALWHV 0.747 15 SB VP2-3 A0206 114 YQQSGMALELF 0.741 16 SB VP2-3 A0206 247 SIDNADSIEEV 0.659 40 SB VP2-3 A0206 29 AAGEAAAAIEV 0.632 53 WB VP2-3 A0206 287 RTAPQWMLPLL 0.614 64 WB VP2-3 A0206 80 FAALIQTVTGI 0.614 65 WB VP2-3 A0206 35 AAIEVQIASLA 0.587 86 WB VP2-3 A0206 37 IEVQIASLATV 0.586 88 WB VP2-3 A0206 24 SVAEIAAGEAA 0.580 93 WB VP2-3 A0206 4 LALLGDLVASV 0.580 94 WB VP2-3 A0206 101 FSDWDHKVSTV 0.577 97 WB VP2-3 A0206 15 SEAAAATGFSV 0.572 102 WB VP2-3 A0206 86 TVTGISSLAQV 0.557 120 WB VP2-3 A0206 59 AIGLTPQTYAV 0.537 150 WB VP2-3 A0206 293 MLPLLLGLYGT 0.536 151 WB VP2-3 A0206 58 AAIGLTPQTYA 0.531 159 WB VP2-3 A0206 10 LVASVSEAAAA 0.524 173 WB VP2-3 A0206 18 AAATGFSVAEI 0.509 203 WB VP2-3 A0206 68 AVIAGAPGAIA 0.503 215 WB VP2-3 A0206 84 IQTVTGISSLA 0.500 223 WB VP2-3 A0206 52 TTSEAIAAIGL 0.457 357 WB VP2-3 A0206 1 GAALALLGDLV 0.454 366 WB VP2-3 A0206 297 LLGLYGTVTPA 0.442 420 WB VP2-3 A0206 13 SVSEAAAATGF 0.441 423 WB VP2-3 A0206 45 ATVEGITTTSE 0.429 481 WB VP2-3 A0206 146 YLDPRHWGPSL 0.969 1 SB VP2-3 A0211 247 SIDNADSIEEV 0.903 2 SB VP2-3 A0211 86 TVTGISSLAQV 0.868 4 SB VP2-3 A0211 61 GLTPQTYAVIA 0.808 7 SB VP2-3 A0211 92 SLAQVGYRFFS 0.759 13 SB VP2-3 A0211 59 AIGLTPQTYAV 0.737 17 SB VP2-3 A0211 122 ELFNPDEYYDI 0.669 35 SB VP2-3 A0211 43 SLATVEGITTT 0.657 40 SB VP2-3 A0211 29 AAGEAAAAIEV 0.644 46 SB VP2-3 A0211 4 LALLGDLVASV 0.626 56 WB VP2-3 A0211 287 RTAPQWMLPLL 0.626 57 WB VP2-3 A0211 131 DILFPGVNTFV 0.620 60 WB VP2-3 A0211 101 FSDWDHKVSTV 0.615 64 WB VP2-3 A0211 157 FATISQALWHV 0.608 69 WB VP2-3 A0211 293 MLPLLLGLYGT 0.597 78 WB VP2-3 A0211 132 ILFPGVNTFVN 0.565 110 WB VP2-3 A0211 297 LLGLYGTVTPA 0.547 134 WB VP2-3 A0211 76 AIAGFAALIQT 0.537 150 WB VP2-3 A0211 292 WMLPLLLGLYG 0.526 167 WB VP2-3 A0211 24 SVAEIAAGEAA 0.526 168 WB VP2-3 A0211 253 SIEEVTQRMDL 0.525 170 WB VP2-3 A0211 296 LLLGLYGTVTP 0.523 174 WB VP2-3 A0211 98 YRFFSDWDHKV 0.515 190 WB VP2-3 A0211 6 LLGDLVASVSE 0.504 213 WB VP2-3 A0211 27 EIAAGEAAAAI 0.496 234 WB VP2-3 A0211 194 RFLEETTWTIV 0.476 288 WB VP2-3 A0211 155 SLFATISQALW 0.468 315 WB VP2-3 A0211 5 ALLGDLVASVS 0.465 325 WB VP2-3 A0211 83 LIQTVTGISSL 0.454 369 WB VP2-3 A0211 77 IAGFAALIQTV 0.449 386 WB VP2-3 A0211 278 TIAPGGANQRT 0.438 437 WB VP2-3 A0211 191 SLARFLEETTW 0.437 444 WB VP2-3 A0211 299 GLYGTVTPALE 0.429 482 WB VP2-3 A0211 146 YLDPRHWGPSL 0.942 1 SB VP2-3 A0212 247 SIDNADSIEEV 0.724 19 SB VP2-3 A0212 59 AIGLTPQTYAV 0.677 32 SB VP2-3 A0212 61 GLTPQTYAVIA 0.591 83 WB VP2-3 A0212 43 SLATVEGITTT 0.566 109 WB VP2-3 A0212 122 ELFNPDEYYDI 0.556 121 WB VP2-3 A0212 4 LALLGDLVASV 0.541 143 WB VP2-3 A0212 293 MLPLLLGLYGT 0.513 194 WB VP2-3 A0212 6 LLGDLVASVSE 0.507 207 WB VP2-3 A0212 83 LIQTVTGISSL 0.499 226 WB VP2-3 A0212 253 SIEEVTQRMDL 0.493 242 WB VP2-3 A0212 292 WMLPLLLGLYG 0.489 251 WB VP2-3 A0212 92 SLAQVGYRFFS 0.479 281 WB VP2-3 A0212 86 TVTGISSLAQV 0.475 292 WB VP2-3 A0212 157 FATISQALWHV 0.435 454 WB VP2-3 A0212 132 ILFPGVNTFVN 0.434 457 WB VP2-3 A0212 213 YIQDYYSNLSP 0.433 464 WB VP2-3 A0212 98 YRFFSDWDHKV 0.432 468 WB VP2-3 A0212 296 LLLGLYGTVTP 0.431 473 WB VP2-3 A0212 146 YLDPRHWGPSL 0.908 2 SB VP2-3 A0216 247 SIDNADSIEEV 0.852 4 SB VP2-3 A0216 86 TVTGISSLAQV 0.811 7 SB VP2-3 A0216 59 AIGLTPQTYAV 0.755 14 SB VP2-3 A0216 29 AAGEAAAAIEV 0.714 22 SB VP2-3 A0216 92 SLAQVGYRFFS 0.674 34 SB VP2-3 A0216 131 DILFPGVNTFV 0.671 35 SB VP2-3 A0216 43 SLATVEGITTT 0.635 52 WB VP2-3 A0216 61 GLTPQTYAVIA 0.633 53 WB VP2-3 A0216 297 LLGLYGTVTPA 0.621 60 WB VP2-3 A0216 83 LIQTVTGISSL 0.526 169 WB VP2-3 A0216 157 FATISQALWHV 0.524 172 WB VP2-3 A0216 122 ELFNPDEYYDI 0.508 205 WB VP2-3 A0216 4 LALLGDLVASV 0.499 225 WB VP2-3 A0216 77 IAGFAALIQTV 0.459 350 WB VP2-3 A0216 76 AIAGFAALIQT 0.458 351 WB VP2-3 A0216 146 YLDPRHWGPSL 0.941 1 SB VP2-3 A0219 247 SIDNADSIEEV 0.699 26 SB VP2-3 A0219 86 TVTGISSLAQV 0.670 35 SB VP2-3 A0219 59 AIGLTPQTYAV 0.566 109 WB VP2-3 A0219 4 LALLGDLVASV 0.537 149 WB VP2-3 A0219 157 FATISQALWHV 0.530 161 WB VP2-3 A0219 83 LIQTVTGISSL 0.499 225 WB VP2-3 A0219 332 GTRASAKTTNK 0.622 59 WB VP2-3 A0301 321 RVSRGSSQKAK 0.580 93 WB VP2-3 A0301 203 IVNAPINFYNY 0.501 220 WB VP2-3 A0301 339 TTNKRRSRSSR 0.487 258 WB VP2-3 A0301 203 IVNAPINFYNY 0.678 32 SB VP2-3 A1101 339 TTNKRRSRSSR 0.651 43 SB VP2-3 A1101 277 KTIAPGGANQR 0.634 52 WB VP2-3 A1101 321 RVSRGSSQKAK 0.626 57 WB VP2-3 A1101 332 GTRASAKTTNK 0.606 70 WB VP2-3 A1101 89 GISSLAQVGYR 0.521 177 WB VP2-3 A1101 136 GVNTFVNNIQY 0.517 185 WB VP2-3 A1101 159 TISQALWHVIR 0.481 274 WB VP2-3 A1101 176 TSQELQRRTER 0.476 289 WB VP2-3 A1101 140 FVNNIQYLDPR 0.469 313 WB VP2-3 A1101 267 ESVHSGEFIEK 0.437 442 WB VP2-3 A1101 200 TWTIVNAPINF 0.630 54 WB VP2-3 A2301 97 GYRFFSDWDHK 0.623 59 WB VP2-3 A2301 113 LYQQSGMALEL 0.597 77 WB VP2-3 A2301 186 RFFRDSLARFL 0.449 389 WB VP2-3 A2301 200 TWTIVNAPINF 0.612 66 WB VP2-3 A2402 113 LYQQSGMALEL 0.533 156 WB VP2-3 A2402 113 LYQQSGMALEL 0.750 14 SB VP2-3 A2403 186 RFFRDSLARFL 0.485 263 WB VP2-3 A2403 91 SSLAQVGYRFF 0.459 347 WB VP2-3 A2403 201 WTIVNAPINFY 0.672 34 SB VP2-3 A2601 109 STVGLYQQSGM 0.619 61 WB VP2-3 A2601 201 WTIVNAPINFY 0.930 2 SB VP2-3 A2602 109 STVGLYQQSGM 0.769 12 SB VP2-3 A2602 27 EIAAGEAAAAI 0.765 12 SB VP2-3 A2602 287 RTAPQWMLPLL 0.678 32 SB VP2-3 A2602 203 IVNAPINFYNY 0.672 34 SB VP2-3 A2602 13 SVSEAAAATGF 0.566 109 WB VP2-3 A2602 88 TGISSLAQVGY 0.498 228 WB VP2-3 A2602 291 QWMLPLLLGLY 0.553 126 WB VP2-3 A2902 203 IVNAPINFYNY 0.517 185 WB VP2-3 A2902 236 EGTHVNFGHTY 0.485 262 WB VP2-3 A2902 208 INFYNYIQDYY 0.471 304 WB VP2-3 A2902 136 GVNTFVNNIQY 0.468 317 WB VP2-3 A2902 319 KRRVSRGSSQK 0.802 8 SB VP2-3 A3001 332 GTRASAKTTNK 0.790 9 SB VP2-3 A3001 97 GYRFFSDWDHK 0.743 16 SB VP2-3 A3001 321 RVSRGSSQKAK 0.684 30 SB VP2-3 A3001 203 IVNAPINFYNY 0.460 345 WB VP2-3 A3002 339 TTNKRRSRSSR 0.837 5 SB VP2-3 A3101 277 KTIAPGGANQR 0.682 31 SB VP2-3 A3101 334 RASAKTTNKRR 0.664 37 SB VP2-3 A3101 336 SAKTTNKRRSR 0.656 41 SB VP2-3 A3101 140 FVNNIQYLDPR 0.655 41 SB VP2-3 A3101 176 TSQELQRRTER 0.645 46 SB VP2-3 A3101 179 ELQRRTERFFR 0.636 51 WB VP2-3 A3101 225 RPSMVRQVAER 0.580 94 WB VP2-3 A3101 324 RGSSQKAKGTR 0.569 105 WB VP2-3 A3101 89 GISSLAQVGYR 0.567 108 WB VP2-3 A3101 159 TISQALWHVIR 0.483 268 WB VP2-3 A3101 332 GTRASAKTTNK 0.446 401 WB VP2-3 A3101 220 NLSPIRPSMVR 0.432 465 WB VP2-3 A3101 179 ELQRRTERFFR 0.812 7 SB VP2-3 A3301 339 TTNKRRSRSSR 0.738 17 SB VP2-3 A3301 140 FVNNIQYLDPR 0.519 181 WB VP2-3 A3301 176 TSQELQRRTER 0.516 188 WB VP2-3 A3301 220 NLSPIRPSMVR 0.506 210 WB VP2-3 A3301 159 TISQALWHVIR 0.465 326 WB VP2-3 A3301 339 TTNKRRSRSSR 0.848 5 SB VP2-3 A6801 140 FVNNIQYLDPR 0.795 9 SB VP2-3 A6801 159 TISQALWHVIR 0.758 13 SB VP2-3 A6801 256 EVTQRMDLRNK 0.719 20 SB VP2-3 A6801 179 ELQRRTERFFR 0.714 22 SB VP2-3 A6801 309 EAYEDGPNQKK 0.713 22 SB VP2-3 A6801 267 ESVHSGEFIEK 0.706 24 SB VP2-3 A6801 220 NLSPIRPSMVR 0.687 29 SB VP2-3 A6801 250 NADSIEEVTQR 0.655 41 SB VP2-3 A6801 176 TSQELQRRTER 0.647 45 SB VP2-3 A6801 201 WTIVNAPINFY 0.600 75 WB VP2-3 A6801 89 GISSLAQVGYR 0.591 83 WB VP2-3 A6801 277 KTIAPGGANQR 0.588 86 WB VP2-3 A6801 172 IPAITSQELQR 0.515 190 WB VP2-3 A6801 225 RPSMVRQVAER 0.438 438 WB VP2-3 A6801 215 QDYYSNLSPIR 0.437 444 WB VP2-3 A6801 198 ETTWTIVNAPI 0.863 4 SB VP2-3 A6802 86 TVTGISSLAQV 0.804 8 SB VP2-3 A6802 16 EAAAATGFSVA 0.777 11 SB VP2-3 A6802 80 FAALIQTVTGI 0.761 13 SB VP2-3 A6802 27 EIAAGEAAAAI 0.759 13 SB VP2-3 A6802 244 HTYSIDNADSI 0.756 13 SB VP2-3 A6802 52 TTSEAIAAIGL 0.729 18 SB VP2-3 A6802 24 SVAEIAAGEAA 0.724 19 SB VP2-3 A6802 40 QIASLATVEGI 0.649 44 SB VP2-3 A6802 32 EAAAAIEVQIA 0.633 52 WB VP2-3 A6802 10 LVASVSEAAAA 0.605 71 WB VP2-3 A6802 131 DILFPGVNTFV 0.561 115 WB VP2-3 A6802 287 RTAPQWMLPLL 0.551 129 WB VP2-3 A6802 259 QRMDLRNKESV 0.550 129 WB VP2-3 A6802 122 ELFNPDEYYDI 0.549 131 WB VP2-3 A6802 46 TVEGITTTSEA 0.537 150 WB VP2-3 A6802 157 FATISQALWHV 0.500 223 WB VP2-3 A6802 109 STVGLYQQSGM 0.495 235 WB VP2-3 A6802 204 VNAPINFYNYI 0.467 319 WB VP2-3 A6802 18 AAATGFSVAEI 0.465 326 WB VP2-3 A6802 23 FSVAEIAAGEA 0.463 333 WB VP2-3 A6802 15 SEAAAATGFSV 0.457 356 WB VP2-3 A6802 98 YRFFSDWDHKV 0.453 371 WB VP2-3 A6802 50 ITTTSEAIAAI 0.442 419 WB VP2-3 A6802 67 YAVIAGAPGAI 0.439 430 WB VP2-3 A6802 0 MGAALALLGDL 0.426 497 WB VP2-3 A6802 198 ETTWTIVNAPI 0.765 12 SB VP2-3 A6901 27 EIAAGEAAAAI 0.722 20 SB VP2-3 A6901 131 DILFPGVNTFV 0.706 23 SB VP2-3 A6901 157 FATISQALWHV 0.625 58 WB VP2-3 A6901 52 TTSEAIAAIGL 0.581 93 WB VP2-3 A6901 244 HTYSIDNADSI 0.559 117 WB VP2-3 A6901 86 TVTGISSLAQV 0.494 237 WB VP2-3 A6901 24 SVAEIAAGEAA 0.491 245 WB VP2-3 A6901 67 YAVIAGAPGAI 0.465 326 WB VP2-3 A6901 146 YLDPRHWGPSL 0.462 338 WB VP2-3 A6901 29 AAGEAAAAIEV 0.456 360 WB VP2-3 A6901 101 FSDWDHKVSTV 0.443 416 WB VP2-3 A6901 294 LPLLLGLYGTV 0.439 433 WB VP2-3 A6901 40 QIASLATVEGI 0.436 448 WB VP2-3 A6901 287 RTAPQWMLPLL 0.433 459 WB VP2-3 A6901 73 APGAIAGFAAL 0.671 35 SB VP2-3 B0702 222 SPIRPSMVRQV 0.530 162 WB VP2-3 B0702 67 YAVIAGAPGAI 0.489 251 WB VP2-3 B0702 114 YQQSGMALELF 0.567 108 WB VP2-3 B1501 201 WTIVNAPINFY 0.536 151 WB VP2-3 B1501 203 IVNAPINFYNY 0.501 221 WB VP2-3 B1501 13 SVSEAAAATGF 0.500 223 WB VP2-3 B1501 264 RNKESVHSGEF 0.488 254 WB VP2-3 B1501 57 IAAIGLTPQTY 0.455 361 WB VP2-3 B1501 37 IEVQIASLATV 0.605 71 WB VP2-3 B1801 127 DEYYDILFPGV 0.591 83 WB VP2-3 B1801 178 QELQRRTERFF 0.466 323 WB VP2-3 B1801 130 YDILFPGVNTF 0.426 495 WB VP2-3 B1801 182 RRTERFFRDSL 0.564 111 WB VP2-3 B2705 319 KRRVSRGSSQK 0.498 227 WB VP2-3 B2705 320 RRVSRGSSQKA 0.461 342 WB VP2-3 B2705 286 QRTAPQWMLPL 0.430 477 WB VP2-3 B2705 119 MALELFNPDEY 0.799 8 SB VP2-3 B3501 57 IAAIGLTPQTY 0.701 25 SB VP2-3 B3501 67 YAVIAGAPGAI 0.605 71 WB VP2-3 B3501 13 SVSEAAAATGF 0.558 119 WB VP2-3 B3501 201 WTIVNAPINFY 0.508 204 WB VP2-3 B3501 73 APGAIAGFAAL 0.500 224 WB VP2-3 B3501 301 YGTVTPALEAY 0.466 322 WB VP2-3 B3501 11 VASVSEAAAAT 0.445 404 WB VP2-3 B3501 146 YLDPRHWGPSL 0.500 223 WB VP2-3 B3901 211 YNYIQDYYSNL 0.445 405 WB VP2-3 B3901 31 GEAAAAIEVQI 0.587 87 WB VP2-3 B4001 15 SEAAAATGFSV 0.513 194 WB VP2-3 B4001 37 IEVQIASLATV 0.477 287 WB VP2-3 B4001 127 DEYYDILFPGV 0.451 380 WB VP2-3 B4001 178 QELQRRTERFF 0.497 231 WB VP2-3 B4002 26 AEIAAGEAAAA 0.428 489 WB VP2-3 B4002 26 AEIAAGEAAAA 0.484 264 WB VP2-3 B4403 26 AEIAAGEAAAA 0.620 61 WB VP2-3 B4501 294 LPLLLGLYGTV 0.749 15 SB VP2-3 B5101 134 FPGVNTFVNNI 0.632 53 WB VP2-3 B5101 134 FPGVNTFVNNI 0.791 9 SB VP2-3 B5301 294 LPLLLGLYGTV 0.479 281 WB VP2-3 B5301 119 MALELFNPDEY 0.477 287 WB VP2-3 B5301 294 LPLLLGLYGTV 0.839 5 SB VP2-3 B5401 134 FPGVNTFVNNI 0.750 14 SB VP2-3 B5401 63 TPQTYAVIAGA 0.491 245 WB VP2-3 B5401 80 FAALIQTVTGI 0.454 369 WB VP2-3 B5401 222 SPIRPSMVRQV 0.451 378 WB VP2-3 B5401 90 ISSLAQVGYRF 0.685 30 SB VP2-3 B5801 191 SLARFLEETTW 0.631 54 WB VP2-3 B5801 155 SLFATISQALW 0.572 102 WB VP2-3 B5801 57 IAAIGLTPQTY 0.539 145 WB VP2-3 B5801 282 GGANQRTAPQW 0.529 162 WB VP2-3 B5801 287 RTAPQWMLPLL 0.488 253 WB VP2-3 B5801 SEQ ID NOS: 52253-53779

Preferred BK virus fragments of VP1 capable of interacting with one or more MHC class 1 molecules are listed in Table K.

TABLE K Prediction of BK virus VP1 protein specific MHC class1, 8-, 9-, 10-, 11-mer peptide binders for 42 MHC class 1 alleles (see FIG. 11) using the //www.cbs.dtu.dk/ services/NetMHC/ database. The MHC class 1 molecules for which no binders were found are not listed. Pro- affinity Bind tein pos peptide logscore (nM) Level Name Allele 8-mers 196 YLDKNNAY 0.756 14 SB VP1 A0101 108 LMWEAVTV 0.819 7 SB VP1 A0201 243 VLLDEQGV 0.703 24 SB VP1 A0201 83 KMLPCYST 0.657 41 SB VP1 A0201 40 GVDAITEV 0.595 79 WB VP1 A0201 281 GLARYFKI 0.591 83 WB VP1 A0201 106 NLLMWEAV 0.580 94 WB VP1 A0201 84 MLPCYSTA 0.562 114 WB VP1 A0201 107 LLMWEAVT 0.498 229 WB VP1 A0201 281 GLARYFKI 0.717 21 SB VP1 A0202 108 LMWEAVTV 0.668 36 SB VP1 A0202 84 MLPCYSTA 0.666 37 SB VP1 A0202 243 VLLDEQGV 0.663 38 SB VP1 A0202 262 SAADICGL 0.662 38 SB VP1 A0202 40 GVDAITEV 0.633 52 WB VP1 A0202 34 VLEVKTGV 0.510 200 WB VP1 A0202 152 FAVGGDPL 0.508 205 WB VP1 A0202 121 GITSMLNL 0.475 291 WB VP1 A0202 125 MLNLHAGS 0.470 310 WB VP1 A0202 25 KLLIKGGV 0.457 354 WB VP1 A0202 107 LLMWEAVT 0.451 379 WB VP1 A0202 238 NTATTVLL 0.447 394 WB VP1 A0202 84 MLPCYSTA 0.841 5 SB VP1 A0203 108 LMWEAVTV 0.784 10 SB VP1 A0203 27 LIKGGVEV 0.779 10 SB VP1 A0203 281 GLARYFKI 0.762 13 SB VP1 A0203 243 VLLDEQGV 0.746 15 SB VP1 A0203 236 VTNTATTV 0.674 33 SB VP1 A0203 25 KLLIKGGV 0.657 41 SB VP1 A0203 106 NLLMWEAV 0.643 47 SB VP1 A0203 34 VLEVKTGV 0.635 51 WB VP1 A0203 233 VLHVTNTA 0.633 52 WB VP1 A0203 107 LLMWEAVT 0.563 113 WB VP1 A0203 262 SAADICGL 0.538 148 WB VP1 A0203 188 VMNTDHKA 0.531 159 WB VP1 A0203 83 KMLPCYST 0.509 203 WB VP1 A0203 125 MLNLHAGS 0.509 203 WB VP1 A0203 326 SQVEEVRV 0.501 221 WB VP1 A0203 229 NVPPVLHV 0.492 244 WB VP1 A0203 121 GITSMLNL 0.490 248 WB VP1 A0203 40 GVDAITEV 0.488 255 WB VP1 A0203 294 SVKNPYPI 0.470 308 WB VP1 A0203 112 AVTVKTEV 0.456 358 WB VP1 A0203 119 VIGITSML 0.439 433 WB VP1 A0203 108 LMWEAVTV 0.780 10 SB VP1 A0204 243 VLLDEQGV 0.740 16 SB VP1 A0204 25 KLLIKGGV 0.582 91 WB VP1 A0204 281 GLARYFKI 0.510 201 WB VP1 A0204 34 VLEVKTGV 0.498 228 WB VP1 A0204 236 VTNTATTV 0.489 253 WB VP1 A0204 326 SQVEEVRV 0.453 371 WB VP1 A0204 106 NLLMWEAV 0.441 423 WB VP1 A0204 27 LIKGGVEV 0.432 465 WB VP1 A0204 40 GVDAITEV 0.431 472 WB VP1 A0204 108 LMWEAVTV 0.852 4 SB VP1 A0206 326 SQVEEVRV 0.789 9 SB VP1 A0206 106 NLLMWEAV 0.731 18 SB VP1 A0206 152 FAVGGDPL 0.729 18 SB VP1 A0206 243 VLLDEQGV 0.720 20 SB VP1 A0206 40 GVDAITEV 0.691 28 SB VP1 A0206 21 VQVPKLLI 0.685 30 SB VP1 A0206 84 MLPCYSTA 0.624 58 WB VP1 A0206 83 KMLPCYST 0.623 59 WB VP1 A0206 354 GQLQTKMV 0.584 89 WB VP1 A0206 229 NVPPVLHV 0.574 99 WB VP1 A0206 25 KLLIKGGV 0.543 139 WB VP1 A0206 262 SAADICGL 0.513 193 WB VP1 A0206 236 VTNTATTV 0.506 208 WB VP1 A0206 281 GLARYFKI 0.505 211 WB VP1 A0206 144 VQGSNFHF 0.481 275 WB VP1 A0206 112 AVTVKTEV 0.454 368 WB VP1 A0206 276 TQQWRGLA 0.439 434 WB VP1 A0206 184 AQSQVMNT 0.432 465 WB VP1 A0206 147 SNFHFFAV 0.432 467 WB VP1 A0206 108 LMWEAVTV 0.966 1 SB VP1 A0211 243 VLLDEQGV 0.965 1 SB VP1 A0211 106 NLLMWEAV 0.910 2 SB VP1 A0211 40 GVDAITEV 0.856 4 SB VP1 A0211 27 LIKGGVEV 0.838 5 SB VP1 A0211 229 NVPPVLHV 0.830 6 SB VP1 A0211 25 KLLIKGGV 0.823 6 SB VP1 A0211 349 YIDRQGQL 0.819 7 SB VP1 A0211 281 GLARYFKI 0.788 9 SB VP1 A0211 84 MLPCYSTA 0.786 10 SB VP1 A0211 196 YLDKNNAY 0.751 14 SB VP1 A0211 83 KMLPCYST 0.746 15 SB VP1 A0211 34 VLEVKTGV 0.731 18 SB VP1 A0211 101 DLTCGNLL 0.639 49 SB VP1 A0211 262 SAADICGL 0.614 65 WB VP1 A0211 97 NLNEDLTC 0.603 73 WB VP1 A0211 188 VMNTDHKA 0.602 74 WB VP1 A0211 233 VLHVTNTA 0.594 80 WB VP1 A0211 112 AVTVKTEV 0.578 96 WB VP1 A0211 320 PMYGMESQ 0.573 102 WB VP1 A0211 326 SQVEEVRV 0.548 133 WB VP1 A0211 332 RVFDGTEQ 0.542 141 WB VP1 A0211 333 VFDGTEQL 0.505 211 WB VP1 A0211 254 CKADSLYV 0.500 224 WB VP1 A0211 236 VTNTATTV 0.498 229 WB VP1 A0211 124 SMLNLHAG 0.491 246 WB VP1 A0211 121 GITSMLNL 0.481 276 WB VP1 A0211 147 SNFHFFAV 0.471 305 WB VP1 A0211 107 LLMWEAVT 0.456 358 WB VP1 A0211 252 PLCKADSL 0.453 370 WB VP1 A0211 223 TYTGGENV 0.451 378 WB VP1 A0211 339 QLPGDPDM 0.440 428 WB VP1 A0211 119 VIGITSML 0.437 439 WB VP1 A0211 243 VLLDEQGV 0.938 1 SB VP1 A0212 108 LMWEAVTV 0.932 2 SB VP1 A0212 106 NLLMWEAV 0.866 4 SB VP1 A0212 27 LIKGGVEV 0.758 13 SB VP1 A0212 281 GLARYFKI 0.738 17 SB VP1 A0212 34 VLEVKTGV 0.730 18 SB VP1 A0212 196 YLDKNNAY 0.708 23 SB VP1 A0212 25 KLLIKGGV 0.691 28 SB VP1 A0212 349 YIDRQGQL 0.659 40 SB VP1 A0212 84 MLPCYSTA 0.645 46 SB VP1 A0212 40 GVDAITEV 0.626 57 WB VP1 A0212 229 NVPPVLHV 0.625 57 WB VP1 A0212 320 PMYGMESQ 0.570 104 WB VP1 A0212 188 VMNTDHKA 0.557 120 WB VP1 A0212 233 VLHVTNTA 0.537 149 WB VP1 A0212 83 KMLPCYST 0.496 234 WB VP1 A0212 339 QLPGDPDM 0.474 295 WB VP1 A0212 107 LLMWEAVT 0.462 337 WB VP1 A0212 124 SMLNLHAG 0.437 443 WB VP1 A0212 50 FLNPEMGD 0.437 444 WB VP1 A0212 236 VTNTATTV 0.435 450 WB VP1 A0212 97 NLNEDLTC 0.431 469 WB VP1 A0212 326 SQVEEVRV 0.429 483 WB VP1 A0212 108 LMWEAVTV 0.930 2 SB VP1 A0216 243 VLLDEQGV 0.867 4 SB VP1 A0216 106 NLLMWEAV 0.829 6 SB VP1 A0216 27 LIKGGVEV 0.816 7 SB VP1 A0216 229 NVPPVLHV 0.794 9 SB VP1 A0216 40 GVDAITEV 0.784 10 SB VP1 A0216 281 GLARYFKI 0.745 15 SB VP1 A0216 34 VLEVKTGV 0.709 23 SB VP1 A0216 84 MLPCYSTA 0.699 26 SB VP1 A0216 349 YIDRQGQL 0.698 26 SB VP1 A0216 25 KLLIKGGV 0.668 36 SB VP1 A0216 112 AVTVKTEV 0.647 45 SB VP1 A0216 252 PLCKADSL 0.627 56 WB VP1 A0216 101 DLTCGNLL 0.529 163 WB VP1 A0216 233 VLHVTNTA 0.520 179 WB VP1 A0216 119 VIGITSML 0.493 241 WB VP1 A0216 83 KMLPCYST 0.490 250 WB VP1 A0216 320 PMYGMESQ 0.474 296 WB VP1 A0216 236 VTNTATTV 0.470 309 WB VP1 A0216 196 YLDKNNAY 0.461 339 WB VP1 A0216 321 MYGMESQV 0.456 360 WB VP1 A0216 152 FAVGGDPL 0.438 439 WB VP1 A0216 223 TYTGGENV 0.434 457 WB VP1 A0216 108 LMWEAVTV 0.930 2 SB VP1 A0219 243 VLLDEQGV 0.896 3 SB VP1 A0219 106 NLLMWEAV 0.798 8 SB VP1 A0219 40 GVDAITEV 0.662 38 SB VP1 A0219 229 NVPPVLHV 0.606 70 WB VP1 A0219 27 LIKGGVEV 0.540 144 WB VP1 A0219 349 YIDRQGQL 0.526 168 WB VP1 A0219 34 VLEVKTGV 0.485 262 WB VP1 A0219 254 CKADSLYV 0.484 265 WB VP1 A0219 196 YLDKNNAY 0.451 381 WB VP1 A0219 236 VTNTATTV 0.446 399 WB VP1 A0219 333 VFDGTEQL 0.439 432 WB VP1 A0219 281 GLARYFKI 0.434 456 WB VP1 A0219 101 DLTCGNLL 0.430 474 WB VP1 A0219 289 RLRKRSVK 0.776 11 SB VP1 A0301 308 LINRRTQK 0.697 26 SB VP1 A0301 164 VLMNYRTK 0.693 27 SB VP1 A0301 127 NLHAGSQK 0.656 41 SB VP1 A0301 165 LMNYRTKY 0.467 318 WB VP1 A0301 280 RGLARYFK 0.446 399 WB VP1 A0301 352 RQGQLQTK 0.432 468 WB VP1 A0301 187 QVMNTDHK 0.705 24 SB VP1 A1101 164 VLMNYRTK 0.620 60 WB VP1 A1101 308 LINRRTQK 0.613 65 WB VP1 A1101 280 RGLARYFK 0.596 79 WB VP1 A1101 22 QVPKLLIK 0.510 200 WB VP1 A1101 31 GVEVLEVK 0.506 210 WB VP1 A1101 11 GAAPKKPK 0.444 408 WB VP1 A1101 352 RQGQLQTK 0.436 447 WB VP1 A1101 298 PYPISFLL 0.570 104 WB VP1 A2301 259 LYVSAADI 0.509 203 WB VP1 A2301 144 VQGSNFHF 0.499 225 WB VP1 A2301 109 MWEAVTVK 0.470 310 WB VP1 A2301 284 RYFKIRLR 0.448 393 WB VP1 A2301 298 PYPISFLL 0.771 11 SB VP1 A2402 202 AYPVECWI 0.672 34 SB VP1 A2402 259 LYVSAADI 0.538 148 WB VP1 A2402 302 SFLLSDLI 0.533 156 WB VP1 A2402 144 VQGSNFHF 0.441 422 WB VP1 A2402 202 AYPVECWI 0.721 20 SB VP1 A2403 298 PYPISFLL 0.614 65 WB VP1 A2403 259 LYVSAADI 0.464 329 WB VP1 A2403 118 EVIGITSM 0.834 6 SB VP1 A2601 118 EVIGITSM 0.909 2 SB VP1 A2602 315 KVDGQPMY 0.730 18 SB VP1 A2602 196 YLDKNNAY 0.675 33 SB VP1 A2602 182 PTAQSQVM 0.599 76 WB VP1 A2602 217 NTRYFGTY 0.573 101 WB VP1 A2602 349 YIDRQGQL 0.555 123 WB VP1 A2602 327 QVEEVRVF 0.491 245 WB VP1 A2602 190 NTDHKAYL 0.463 332 WB VP1 A2602 238 NTATTVLL 0.462 338 WB VP1 A2602 196 YLDKNNAY 0.550 130 WB VP1 A2902 165 LMNYRTKY 0.498 228 WB VP1 A2902 289 RLRKRSVK 0.873 3 SB VP1 A3001 280 RGLARYFK 0.802 8 SB VP1 A3001 187 QVMNTDHK 0.563 113 WB VP1 A3001 308 LINRRTQK 0.535 153 WB VP1 A3001 164 VLMNYRTK 0.534 153 WB VP1 A3001 285 YFKIRLRK 0.497 231 WB VP1 A3001 84 RYFKIRLR 0.452 377 WB VP1 A3001 127 NLHAGSQK 0.426 497 WB VP1 A3001 315 KVDGQPMY 0.436 447 WB VP1 A3002 165 LMNYRTKY 0.431 473 WB VP1 A3002 284 RYFKIRLR 0.898 3 SB VP1 A3101 280 RGLARYFK 0.716 21 SB VP1 A3101 289 RLRKRSVK 0.670 35 SB VP1 A3101 282 LARYFKIR 0.663 38 SB VP1 A3101 277 QQWRGLAR 0.643 47 SB VP1 A3101 285 YFKIRLRK 0.581 93 WB VP1 A3101 304 LLSDLINR 0.569 106 WB VP1 A3101 308 LINRRTQK 0.542 141 WB VP1 A3101 273 SSGTQQWR 0.503 215 WB VP1 A3101 164 VLMNYRTK 0.434 458 WB VP1 A3101 345 DMIRYIDR 0.767 12 SB VP1 A3301 284 RYFKIRLR 0.631 54 WB VP1 A3301 282 LARYFKIR 0.515 190 WB VP1 A3301 285 YFKIRLRK 0.504 213 WB VP1 A3301 277 QQWRGLAR 0.444 410 WB VP1 A3301 187 QVMNTDHK 0.708 23 SB VP1 A6801 345 DMIRYIDR 0.627 56 WB VP1 A6801 325 ESQVEEVR 0.606 70 WB VP1 A6801 85 LPCYSTAR 0.568 107 WB VP1 A6801 127 NLHAGSQK 0.503 217 WB VP1 A6801 304 LLSDLINR 0.497 230 WB VP1 A6801 308 LINRRTQK 0.497 231 WB VP1 A6801 284 RYFKIRLR 0.488 254 WB VP1 A6801 162 QGVLMNYR 0.487 257 WB VP1 A6801 305 LSDLINRR 0.439 431 WB VP1 A6801 282 LARYFKIR 0.438 439 WB VP1 A6801 238 NTATTVLL 0.723 19 SB VP1 A6802 262 SAADICGL 0.718 21 SB VP1 A6802 118 EVIGITSM 0.718 21 SB VP1 A6802 147 SNFHFFAV 0.659 39 SB VP1 A6802 229 NVPPVLHV 0.647 45 SB VP1 A6802 297 NPYPISFL 0.515 191 WB VP1 A6802 152 FAVGGDPL 0.506 210 WB VP1 A6802 88 YSTARIPL 0.473 300 WB VP1 A6802 294 SVKNPYPI 0.458 351 WB VP1 A6802 254 CKADSLYV 0.441 421 WB VP1 A6802 108 LMWEAVTV 0.730 18 SB VP1 A6901 238 NTATTVLL 0.636 51 WB VP1 A6901 157 DPLEMQGV 0.635 51 WB VP1 A6901 297 NPYPISFL 0.557 120 WB VP1 A6901 118 EVIGITSM 0.548 132 WB VP1 A6901 229 NVPPVLHV 0.545 137 WB VP1 A6901 106 NLLMWEAV 0.539 147 WB VP1 A6901 262 SAADICGL 0.441 421 WB VP1 A6901 19 EPVQVPKL 0.431 471 WB VP1 A6901 142 KPVQGSNF 0.685 30 SB VP1 B0702 297 NPYPISFL 0.489 251 WB VP1 B0702 16 KPKEPVQV 0.433 462 WB VP1 B0702 95 LPNLNEDL 0.428 488 WB VP1 B0702 68 HLSAENAF 0.555 123 WB VP1 B1501 165 LMNYRTKY 0.542 142 WB VP1 B1501 161 MQGVLMNY 0.509 202 WB VP1 B1501 144 VQGSNFHF 0.453 369 WB VP1 B1501 196 YLDKNNAY 0.448 393 WB VP1 B1501 246 DEQGVGPL 0.554 124 WB VP1 B1801 324 MESQVEEV 0.449 389 WB VP1 B1801 159 LEMQGVLM 0.439 432 WB VP1 B1801 283 ARYFKIRL 0.453 371 WB VP1 B2705 292 KRSVKNPY 0.436 446 WB VP1 B2705 279 WRGLARYF 0.426 496 WB VP1 B2705 152 FAVGGDPL 0.737 17 SB VP1 B3501 142 KPVQGSNF 0.631 54 WB VP1 B3501 19 EPVQVPKL 0.547 134 WB VP1 B3501 196 YLDKNNAY 0.544 138 WB VP1 B3501 118 EVIGITSM 0.533 157 WB VP1 B3501 95 LPNLNEDL 0.482 270 WB VP1 B3501 299 YPISFLLS 0.480 278 WB VP1 B3501 68 HLSAENAF 0.472 304 WB VP1 B3501 297 NPYPISFL 0.470 309 WB VP1 B3501 227 GENVPPVL 0.576 98 WB VP1 B4001 159 LEMQGVLM 0.513 194 WB VP1 B4001 324 MESQVEEV 0.433 462 WB VP1 B4001 246 DEQGVGPL 0.430 476 WB VP1 B4001 227 GENVPPVL 0.457 357 WB VP1 B4002 71 AENAFESD 0.469 312 WB VP1 B4501 340 LPGDPDMI 0.621 60 WB VP1 B5101 230 VPPVLHVT 0.446 401 WB VP1 B5101 203 YPVECWIP 0.426 498 WB VP1 B5101 297 NPYPISFL 0.568 107 WB VP1 B5301 142 KPVQGSNF 0.533 156 WB VP1 B5301 19 EPVQVPKL 0.525 171 WB VP1 B5301 340 LPGDPDMI 0.522 176 WB VP1 B5301 95 LPNLNEDL 0.434 456 WB VP1 B5301 299 YPISFLLS 0.612 66 WB VP1 B5401 203 YPVECWIP 0.524 172 WB VP1 B5401 230 VPPVLHVT 0.521 178 WB VP1 B5401 85 LPCYSTAR 0.450 382 WB VP1 B5401 340 LPGDPDMI 0.436 448 WB VP1 B5401 272 NSSGTQQW 0.527 166 WB VP1 B5701 201 NAYPVECW 0.479 280 WB VP1 B5701 201 NAYPVECW 0.691 28 SB VP1 B5801 272 NSSGTQQW 0.675 33 SB VP1 B5801 9-mers 107 LLMWEAVTV 0.761 13 SB VP1 A0201 83 KMLPCYSTA 0.724 19 SB VP1 A0201 26 LLIKGGVEV 0.573 101 WB VP1 A0201 323 GMESQVEEV 0.550 129 WB VP1 A0201 332 RVFDGTEQL 0.550 130 WB VP1 A0201 107 LLMWEAVTV 0.769 12 SB VP1 A0202 332 RVFDGTEQL 0.681 31 SB VP1 A0202 323 GMESQVEEV 0.678 32 SB VP1 A0202 26 LLIKGGVEV 0.632 53 WB VP1 A0202 83 KMLPCYSTA 0.540 145 WB VP1 A0202 308 LINRRTQKV 0.539 146 WB VP1 A0202 61 NLRGYSQHL 0.534 154 WB VP1 A0202 127 NLHAGSQKV 0.529 163 WB VP1 A0202 43 AITEVECFL 0.504 213 WB VP1 A0202 118 EVIGITSML 0.480 277 WB VP1 A0202 304 LLSDLINRR 0.474 295 WB VP1 A0202 268 GLFTNSSGT 0.463 333 WB VP1 A0202 339 QLPGDPDMI 0.455 363 WB VP1 A0202 146 GSNFHFFAV 0.439 430 WB VP1 A0202 236 VTNTATTVL 0.439 434 WB VP1 A0202 107 LLMWEAVTV 0.839 5 SB VP1 A0203 308 LINRRTQKV 0.820 6 SB VP1 A0203 26 LLIKGGVEV 0.818 7 SB VP1 A0203 127 NLHAGSQKV 0.786 10 SB VP1 A0203 83 KMLPCYSTA 0.761 13 SB VP1 A0203 27 LIKGGVEVL 0.623 59 WB VP1 A0203 61 NLRGYSQHL 0.616 64 WB VP1 A0203 332 RVFDGTEQL 0.609 68 WB VP1 A0203 323 GMESQVEEV 0.604 72 WB VP1 A0203 222 GTYTGGENV 0.586 88 WB VP1 A0203 258 SLYVSAADI 0.570 104 WB VP1 A0203 268 GLFTNSSGT 0.535 153 WB VP1 A0203 235 HVTNTATTV 0.512 195 WB VP1 A0203 320 PMYGMESQV 0.509 203 WB VP1 A0203 125 MLNLHAGSQ 0.480 277 WB VP1 A0203 114 TVKTEVIGI 0.476 288 WB VP1 A0203 287 KIRLRKRSV 0.452 374 WB VP1 A0203 236 VTNTATTVL 0.450 384 WB VP1 A0203 107 LLMWEAVTV 0.751 14 SB VP1 A0204 26 LLIKGGVEV 0.688 29 SB VP1 A0204 323 GMESQVEEV 0.648 45 SB VP1 A0204 127 NLHAGSQKV 0.613 65 WB VP1 A0204 308 LINRRTQKV 0.547 133 WB VP1 A0204 83 KMLPCYSTA 0.504 214 WB VP1 A0204 33 EVLEVKTGV 0.476 289 WB VP1 A0204 43 AITEVECFL 0.428 488 WB VP1 A0204 107 LLMWEAVTV 0.865 4 SB VP1 A0206 26 LLIKGGVEV 0.808 7 SB VP1 A0206 332 RVFDGTEQL 0.797 8 SB VP1 A0206 83 KMLPCYSTA 0.723 20 SB VP1 A0206 235 HVTNTATTV 0.591 83 WB VP1 A0206 144 VQGSNFHFF 0.586 88 WB VP1 A0206 146 GSNFHFFAV 0.555 123 WB VP1 A0206 43 AITEVECFL 0.542 142 WB VP1 A0206 326 SQVEEVRVF 0.472 303 WB VP1 A0206 39 TGVDAITEV 0.460 344 WB VP1 A0206 127 NLHAGSQKV 0.451 378 WB VP1 A0206 107 LLMWEAVTV 0.952 1 SB VP1 A0211 26 LLIKGGVEV 0.946 1 SB VP1 A0211 127 NLHAGSQKV 0.943 1 SB VP1 A0211 320 PMYGMESQV 0.941 1 SB VP1 A0211 332 RVFDGTEQL 0.923 2 SB VP1 A0211 83 KMLPCYSTA 0.869 4 SB VP1 A0211 43 AITEVECFL 0.830 6 SB VP1 A0211 33 EVLEVKTGV 0.818 7 SB VP1 A0211 61 NLRGYSQHL 0.804 8 SB VP1 A0211 323 GMESQVEEV 0.800 8 SB VP1 A0211 308 LINRRTQKV 0.688 29 SB VP1 A0211 235 HVTNTATTV 0.687 29 SB VP1 A0211 242 TVLLDEQGV 0.669 35 SB VP1 A0211 196 YLDKNNAYP 0.642 48 SB VP1 A0211 339 QLPGDPDMI 0.623 59 WB VP1 A0211 101 DLTCGNLLM 0.603 73 WB VP1 A0211 54 EMGDPDDNL 0.589 85 WB VP1 A0211 27 LIKGGVEVL 0.568 107 WB VP1 A0211 258 SLYVSAADI 0.564 111 WB VP1 A0211 176 TITPKNPTA 0.543 140 WB VP1 A0211 349 YIDRQGQLQ 0.525 169 WB VP1 A0211 222 GTYTGGENV 0.521 178 WB VP1 A0211 124 SMLNLHAGS 0.494 238 WB VP1 A0211 108 LMWEAVTVK 0.489 251 WB VP1 A0211 39 TGVDAITEV 0.488 253 WB VP1 A0211 94 PLPNLNEDL 0.487 256 WB VP1 A0211 255 KADSLYVSA 0.475 292 WB VP1 A0211 118 EVIGITSML 0.472 304 WB VP1 A0211 201 NAYPVECWI 0.470 310 WB VP1 A0211 106 NLLMWEAVT 0.467 320 WB VP1 A0211 268 GLFTNSSGT 0.463 332 WB VP1 A0211 244 LLDEQGVGP 0.443 415 WB VP1 A0211 26 LLIKGGVEV 0.905 2 SB VP1 A0212 107 LLMWEAVTV 0.903 2 SB VP1 A0212 127 NLHAGSQKV 0.895 3 SB VP1 A0212 320 PMYGMESQV 0.883 3 SB VP1 A0212 61 NLRGYSQHL 0.837 5 SB VP1 A0212 33 EVLEVKTGV 0.810 7 SB VP1 A0212 332 RVFDGTEQL 0.768 12 SB VP1 A0212 308 LINRRTQKV 0.710 23 SB VP1 A0212 43 AITEVECFL 0.696 26 SB VP1 A0212 323 GMESQVEEV 0.680 31 SB VP1 A0212 242 TVLLDEQGV 0.643 47 SB VP1 A0212 196 YLDKNNAYP 0.604 72 WB VP1 A0212 54 EMGDPDDNL 0.597 78 WB VP1 A0212 83 KMLPCYSTA 0.575 99 WB VP1 A0212 339 QLPGDPDMI 0.548 132 WB VP1 A0212 108 LMWEAVTVK 0.537 149 WB VP1 A0212 268 GLFTNSSGT 0.534 155 WB VP1 A0212 222 GTYTGGENV 0.527 166 WB VP1 A0212 27 LIKGGVEVL 0.505 212 WB VP1 A0212 124 SMLNLHAGS 0.492 243 WB VP1 A0212 244 LLDEQGVGP 0.484 266 WB VP1 A0212 164 VLMNYRTKY 0.481 274 WB VP1 A0212 94 PLPNLNEDL 0.480 276 WB VP1 A0212 235 HVTNTATTV 0.457 356 WB VP1 A0212 304 LLSDLINRR 0.443 414 WB VP1 A0212 258 SLYVSAADI 0.436 449 WB VP1 A0212 349 YIDRQGQLQ 0.435 452 WB VP1 A0212 201 NAYPVECWI 0.435 453 WB VP1 A0212 26 LLIKGGVEV 0.935 2 SB VP1 A0216 320 PMYGMESQV 0.926 2 SB VP1 A0216 127 NLHAGSQKV 0.887 3 SB VP1 A0216 107 LLMWEAVTV 0.872 3 SB VP1 A0216 332 RVFDGTEQL 0.838 5 SB VP1 A0216 61 NLRGYSQHL 0.835 5 SB VP1 A0216 43 AITEVECFL 0.834 6 SB VP1 A0216 323 GMESQVEEV 0.826 6 SB VP1 A0216 235 HVTNTATTV 0.762 13 SB VP1 A0216 33 EVLEVKTGV 0.742 16 SB VP1 A0216 308 LINRRTQKV 0.701 25 SB VP1 A0216 83 KMLPCYSTA 0.653 42 SB VP1 A0216 54 EMGDPDDNL 0.649 44 SB VP1 A0216 201 NAYPVECWI 0.593 81 WB VP1 A0216 111 EAVTVKTEV 0.540 145 WB VP1 A0216 39 TGVDAITEV 0.524 171 WB VP1 A0216 118 EVIGITSML 0.513 194 WB VP1 A0216 196 YLDKNNAYP 0.512 196 WB VP1 A0216 339 QLPGDPDMI 0.491 245 WB VP1 A0216 222 GTYTGGENV 0.485 262 WB VP1 A0216 27 LIKGGVEVL 0.467 318 WB VP1 A0216 176 TITPKNPTA 0.462 336 WB VP1 A0216 94 PLPNLNEDL 0.426 496 WB VP1 A0216 127 NLHAGSQKV 0.862 4 SB VP1 A0219 107 LLMWEAVTV 0.811 7 SB VP1 A0219 320 PMYGMESQV 0.786 10 SB VP1 A0219 26 LLIKGGVEV 0.776 11 SB VP1 A0219 332 RVFDGTEQL 0.762 13 SB VP1 A0219 323 GMESQVEEV 0.643 47 SB VP1 A0219 61 NLRGYSQHL 0.621 60 WB VP1 A0219 54 EMGDPDDNL 0.581 93 WB VP1 A0219 235 HVTNTATTV 0.537 150 WB VP1 A0219 33 EVLEVKTGV 0.529 162 WB VP1 A0219 308 LINRRTQKV 0.528 165 WB VP1 A0219 39 TGVDAITEV 0.492 242 WB VP1 A0219 108 LMWEAVTVK 0.442 417 WB VP1 A0219 27 LIKGGVEVL 0.438 437 WB VP1 A0219 284 RYFKIRLRK 0.643 47 SB VP1 A0301 108 LMWEAVTVK 0.570 104 WB VP1 A0301 134 KVHENGGGK 0.525 170 WB VP1 A0301 164 VLMNYRTKY 0.453 370 WB VP1 A0301 163 GVLMNYRTK 0.440 426 WB VP1 A0301 163 GVLMNYRTK 0.621 60 WB VP1 A1101 186 SQVMNTDHK 0.599 76 WB VP1 A1101 284 RYFKIRLRK 0.586 88 WB VP1 A1101 276 TQQWRGLAR 0.561 115 WB VP1 A1101 134 KVHENGGGK 0.556 121 WB VP1 A1101 284 RYFKIRLRK 0.724 19 SB VP1 A2301 87 CYSTARIPL 0.572 102 WB VP1 A2301 143 PVQGSNFHF 0.555 123 WB VP1 A2301 348 RYIDRQGQL 0.538 147 WB VP1 A2301 144 VQGSNFHFF 0.480 277 WB VP1 A2301 144 VQGSNFHFF 0.521 178 WB VP1 A2402 348 RYIDRQGQL 0.506 210 WB VP1 A2402 348 RYIDRQGQL 0.602 73 WB VP1 A2403 195 AYLDKNNAY 0.502 218 WB VP1 A2403 278 QWRGLARYF 0.434 457 WB VP1 A2403 118 EVIGITSML 0.663 38 SB VP1 A2601 160 EMQGVLMNY 0.553 126 WB VP1 A2601 118 EVIGITSML 0.898 3 SB VP1 A2602 160 EMQGVLMNY 0.659 39 SB VP1 A2602 36 EVKTGVDAI 0.584 90 WB VP1 A2602 164 VLMNYRTKY 0.620 61 WB VP1 A2902 188 VMNTDHKAY 0.535 153 WB VP1 A2902 195 AYLDKNNAY 0.524 172 WB VP1 A2902 284 RYFKIRLRK 0.812 7 SB VP1 A3001 134 KVHENGGGK 0.791 9 SB VP1 A3001 163 GVLMNYRTK 0.563 113 WB VP1 A3001 291 RKRSVKNPY 0.543 141 WB VP1 A3001 169 RTKYPQGTI 0.492 243 WB VP1 A3001 191 TDHKAYLDK 0.436 444 WB VP1 A3001 287 KIRLRKRSV 0.436 446 WB VP1 A3001 289 RLRKRSVKN 0.436 447 WB VP1 A3001 186 SQVMNTDHK 0.434 455 WB VP1 A3001 161 MQGVLMNYR 0.811 7 SB VP1 A3101 285 YFKIRLRKR 0.800 8 SB VP1 A3101 284 RYFKIRLRK 0.762 13 SB VP1 A3101 276 TQQWRGLAR 0.627 56 WB VP1 A3101 84 MLPCYSTAR 0.578 95 WB VP1 A3101 304 LLSDLINRR 0.573 101 WB VP1 A3101 281 GLARYFKIR 0.520 180 WB VP1 A3101 108 LMWEAVTVK 0.502 219 WB VP1 A3101 303 FLLSDLINR 0.441 422 WB VP1 A3101 285 YFKIRLRKR 0.782 10 SB VP1 A3301 307 DLINRRTQK 0.659 39 SB VP1 A3301 272 NSSGTQQWR 0.732 18 SB VP1 A6801 84 MLPCYSTAR 0.720 20 SB VP1 A6801 307 DLINRRTQK 0.593 81 WB VP1 A6801 324 MESQVEEVR 0.548 132 WB VP1 A6801 304 LLSDLINRR 0.543 140 WB VP1 A6801 118 EVIGITSML 0.509 202 WB VP1 A6801 161 MQGVLMNYR 0.437 442 WB VP1 A6801 284 RYFKIRLRK 0.437 444 WB VP1 A6801 118 EVIGITSML 0.903 2 SB VP1 A6802 111 EAVTVKTEV 0.739 16 SB VP1 A6802 33 EVLEVKTGV 0.728 18 SB VP1 A6802 39 TGVDAITEV 0.683 30 SB VP1 A6802 297 NPYPISFLL 0.632 53 WB VP1 A6802 332 RVFDGTEQL 0.578 95 WB VP1 A6802 145 QGSNFHFFA 0.563 113 WB VP1 A6802 201 NAYPVECWI 0.556 121 WB VP1 A6802 187 QVMNTDHKA 0.527 167 WB VP1 A6802 146 GSNFHFFAV 0.497 231 WB VP1 A6802 293 RSVKNPYPI 0.457 357 WB VP1 A6802 261 VSAADICGL 0.455 364 WB VP1 A6802 235 HVTNTATTV 0.444 410 WB VP1 A6802 229 NVPPVLHVT 0.441 422 WB VP1 A6802 297 NPYPISFLL 0.673 34 SB VP1 A6901 118 EVIGITSML 0.636 51 WB VP1 A6901 235 HVTNTATTV 0.546 136 WB VP1 A6901 107 LLMWEAVTV 0.499 225 WB VP1 A6901 201 NAYPVECWI 0.485 262 WB VP1 A6901 111 EAVTVKTEV 0.483 268 WB VP1 A6901 225 TGGENVPPV 0.469 311 WB VP1 A6901 222 GTYTGGENV 0.437 440 WB VP1 A6901 127 NLHAGSQKV 0.433 463 WB VP1 A6901 332 RVFDGTEQL 0.430 474 WB VP1 A6901 85 LPCYSTARI 0.692 28 SB VP1 B0702 13 APKKPKEPV 0.688 29 SB VP1 B0702 1 APTKRKGEC 0.619 61 WB VP1 B0702 282 LARYFKIRL 0.535 153 WB VP1 B0702 287 KIRLRKRSV 0.520 179 WB VP1 B0702 181 NPTAQSQVM 0.498 227 WB VP1 B0702 79 SPDRKMLPC 0.482 272 WB VP1 B0702 19 EPVQVPKLL 0.474 295 WB VP1 B0702 251 GPLCKADSL 0.455 364 WB VP1 B0702 287 KIRLRKRSV 0.431 472 WB VP1 B0801 326 SQVEEVRVF 0.598 77 WB VP1 B1501 188 VMNTDHKAY 0.589 85 WB VP1 B1501 313 TQKVDGQPM 0.566 108 WB VP1 B1501 277 QQWRGLARY 0.543 140 WB VP1 B1501 160 EMQGVLMNY 0.456 360 WB VP1 B1501 295 VKNPYPISF 0.595 79 WB VP1 B1801 117 TEVIGITSM 0.472 303 WB VP1 B1801 288 IRLRKRSVK 0.523 174 WB VP1 B2705 279 WRGLARYFK 0.486 259 WB VP1 B2705 181 NPTAQSQVM 0.758 13 SB VP1 B3501 57 DPDDNLRGY 0.613 65 WB VP1 B3501 157 DPLEMQGVL 0.577 97 WB VP1 B3501 142 KPVQGSNFH 0.574 99 WB VP1 B3501 297 NPYPISFLL 0.568 107 WB VP1 B3501 151 FFAVGGDPL 0.565 110 WB VP1 B3501 67 QHLSAENAF 0.495 235 WB VP1 B3501 203 YPVECWIPD 0.491 247 WB VP1 B3501 19 EPVQVPKLL 0.475 292 WB VP1 B3501 42 DAITEVECF 0.468 317 WB VP1 B3501 95 LPNLNEDLT 0.441 424 WB VP1 B3501 136 HENGGGKPV 0.448 391 WB VP1 B4001 47 VECFLNPEM 0.431 469 WB VP1 B4001 71 AENAFESDS 0.600 75 WB VP1 B4501 85 LPCYSTARI 0.659 39 SB VP1 B5101 19 EPVQVPKLL 0.475 292 WB VP1 B5101 297 NPYPISFLL 0.459 350 WB VP1 B5101 85 LPCYSTARI 0.655 41 SB VP1 B5301 297 NPYPISFLL 0.623 59 WB VP1 B5301 19 EPVQVPKLL 0.535 152 WB VP1 B5301 95 LPNLNEDLT 0.636 51 WB VP1 B5401 85 LPCYSTARI 0.591 83 WB VP1 B5401 203 YPVECWIPD 0.481 273 WB VP1 B5401 299 YPISFLLSD 0.435 452 WB VP1 B5401 102 LTCGNLLMW 0.453 371 WB VP1 B5701 102 LTCGNLLMW 0.624 58 WB VP1 B5801 10-mers 196 YLDKNNAYPV 0.866 4 SB VP1 A0201 108 LMWEAVTVKT 0.691 28 SB VP1 A0201 84 MLPCYSTARI 0.675 33 SB VP1 A0201 106 NLLMWEAVTV 0.634 52 WB VP1 A0201 224 YTGGENVPPV 0.608 69 WB VP1 A0201 260 YVSAADICGL 0.589 85 WB VP1 A0201 244 LLDEQGVGPL 0.537 150 WB VP1 A0201 25 KLLIKGGVEV 0.517 185 WB VP1 A0201 188 VMNTDHKAYL 0.504 214 WB VP1 A0201 281 GLARYFKIRL 0.482 271 WB VP1 A0201 322 YGMESQVEEV 0.465 325 WB VP1 A0201 26 LLIKGGVEVL 0.465 328 WB VP1 A0201 196 YLDKNNAYPV 0.722 20 SB VP1 A0202 260 YVSAADICGL 0.676 33 SB VP1 A0202 244 LLDEQGVGPL 0.652 43 SB VP1 A0202 26 LLIKGGVEVL 0.621 60 WB VP1 A0202 188 VMNTDHKAYL 0.613 66 WB VP1 A0202 84 MLPCYSTARI 0.604 72 WB VP1 A0202 106 NLLMWEAVTV 0.571 104 WB VP1 A0202 224 YTGGENVPPV 0.554 124 WB VP1 A0202 281 GLARYFKIRL 0.520 179 WB VP1 A0202 303 FLLSDLINRR 0.495 236 WB VP1 A0202 304 LLSDLINRRT 0.487 257 WB VP1 A0202 322 YGMESQVEEV 0.470 308 WB VP1 A0202 25 KLLIKGGVEV 0.462 338 WB VP1 A0202 38 KTGVDAITEV 0.453 372 WB VP1 A0202 255 KADSLYVSAA 0.442 419 WB VP1 A0202 84 MLPCYSTARI 0.854 4 SB VP1 A0203 196 YLDKNNAYPV 0.801 8 SB VP1 A0203 244 LLDEQGVGPL 0.704 24 SB VP1 A0203 188 VMNTDHKAYL 0.702 25 SB VP1 A0203 26 LLIKGGVEVL 0.663 38 SB VP1 A0203 106 NLLMWEAVTV 0.660 39 SB VP1 A0203 224 YTGGENVPPV 0.611 67 WB VP1 A0203 260 YVSAADICGL 0.606 70 WB VP1 A0203 25 KLLIKGGVEV 0.596 79 WB VP1 A0203 281 GLARYFKIRL 0.590 84 WB VP1 A0203 304 LLSDLINRRT 0.530 162 WB VP1 A0203 108 LMWEAVTVKT 0.467 319 WB VP1 A0203 233 VLHVTNTATT 0.462 338 WB VP1 A0203 352 RQGQLQTKMV 0.448 391 WB VP1 A0203 236 VTNTATTVLL 0.446 399 WB VP1 A0203 38 KTGVDAITEV 0.441 424 WB VP1 A0203 307 DLINRRTQKV 0.438 437 WB VP1 A0203 196 YLDKNNAYPV 0.658 40 SB VP1 A0204 25 KLLIKGGVEV 0.650 44 SB VP1 A0204 244 LLDEQGVGPL 0.598 77 WB VP1 A0204 224 YTGGENVPPV 0.596 78 WB VP1 A0204 108 LMWEAVTVKT 0.548 133 WB VP1 A0204 106 NLLMWEAVTV 0.541 142 WB VP1 A0204 38 KTGVDAITEV 0.517 185 WB VP1 A0204 322 YGMESQVEEV 0.499 226 WB VP1 A0204 188 VMNTDHKAYL 0.473 299 WB VP1 A0204 26 LLIKGGVEVL 0.468 315 WB VP1 A0204 89 STARIPLPNL 0.433 459 WB VP1 A0204 196 YLDKNNAYPV 0.873 3 SB VP1 A0206 144 VQGSNFHFFA 0.733 17 SB VP1 A0206 106 NLLMWEAVTV 0.694 27 SB VP1 A0206 260 YVSAADICGL 0.677 32 SB VP1 A0206 84 MLPCYSTARI 0.671 35 SB VP1 A0206 244 LLDEQGVGPL 0.637 50 WB VP1 A0206 224 YTGGENVPPV 0.606 71 WB VP1 A0206 38 KTGVDAITEV 0.590 84 WB VP1 A0206 25 KLLIKGGVEV 0.588 86 WB VP1 A0206 186 SQVMNTDHKA 0.588 86 WB VP1 A0206 352 RQGQLQTKMV 0.559 118 WB VP1 A0206 152 FAVGGDPLEM 0.550 129 WB VP1 A0206 26 LLIKGGVEVL 0.549 131 WB VP1 A0206 322 YGMESQVEEV 0.514 191 WB VP1 A0206 277 QQWRGLARYF 0.509 202 WB VP1 A0206 108 LMWEAVTVKT 0.503 216 WB VP1 A0206 161 MQGVLMNYRT 0.428 486 WB VP1 A0206 196 YLDKNNAYPV 0.976 1 SB VP1 A0211 106 NLLMWEAVTV 0.926 2 SB VP1 A0211 244 LLDEQGVGPL 0.906 2 SB VP1 A0211 25 KLLIKGGVEV 0.849 5 SB VP1 A0211 26 LLIKGGVEVL 0.843 5 SB VP1 A0211 224 YTGGENVPPV 0.820 7 SB VP1 A0211 281 GLARYFKIRL 0.817 7 SB VP1 A0211 252 PLCKADSLYV 0.801 8 SB VP1 A0211 188 VMNTDHKAYL 0.798 8 SB VP1 A0211 84 MLPCYSTARI 0.773 11 SB VP1 A0211 307 DLINRRTQKV 0.751 14 SB VP1 A0211 108 LMWEAVTVKT 0.740 16 SB VP1 A0211 260 YVSAADICGL 0.693 27 SB VP1 A0211 349 YIDRQGQLQT 0.652 43 SB VP1 A0211 304 LLSDLINRRT 0.628 55 WB VP1 A0211 322 YGMESQVEEV 0.608 69 WB VP1 A0211 155 GGDPLEMQGV 0.597 78 WB VP1 A0211 315 KVDGQPMYGM 0.593 82 WB VP1 A0211 124 SMLNLHAGSQ 0.578 96 WB VP1 A0211 38 KTGVDAITEV 0.533 156 WB VP1 A0211 268 GLFTNSSGTQ 0.499 226 WB VP1 A0211 243 VLLDEQGVGP 0.427 494 WB VP1 A0211 196 YLDKNNAYPV 0.940 1 SB VP1 A0212 106 NLLMWEAVTV 0.863 4 SB VP1 A0212 26 LLIKGGVEVL 0.799 8 SB VP1 A0212 244 LLDEQGVGPL 0.763 12 SB VP1 A0212 281 GLARYFKIRL 0.762 13 SB VP1 A0212 224 YTGGENVPPV 0.734 17 SB VP1 A0212 188 VMNTDHKAYL 0.728 19 SB VP1 A0212 108 LMWEAVTVKT 0.718 21 SB VP1 A0212 25 KLLIKGGVEV 0.705 24 SB VP1 A0212 84 MLPCYSTARI 0.659 40 SB VP1 A0212 260 YVSAADICGL 0.646 46 SB VP1 A0212 307 DLINRRTQKV 0.625 57 WB VP1 A0212 252 PLCKADSLYV 0.620 60 WB VP1 A0212 304 LLSDLINRRT 0.541 143 WB VP1 A0212 349 YIDRQGQLQT 0.533 157 WB VP1 A0212 155 GGDPLEMQGV 0.513 195 WB VP1 A0212 243 VLLDEQGVGP 0.504 213 WB VP1 A0212 303 FLLSDLINRR 0.481 274 WB VP1 A0212 322 YGMESQVEEV 0.474 297 WB VP1 A0212 124 SMLNLHAGSQ 0.430 477 WB VP1 A0212 196 YLDKNNAYPV 0.945 1 SB VP1 A0216 106 NLLMWEAVTV 0.882 3 SB VP1 A0216 252 PLCKADSLYV 0.866 4 SB VP1 A0216 281 GLARYFKIRL 0.844 5 SB VP1 A0216 307 DLINRRTQKV 0.820 7 SB VP1 A0216 26 LLIKGGVEVL 0.800 8 SB VP1 A0216 25 KLLIKGGVEV 0.779 10 SB VP1 A0216 244 LLDEQGVGPL 0.740 16 SB VP1 A0216 224 YTGGENVPPV 0.726 19 SB VP1 A0216 84 MLPCYSTARI 0.723 19 SB VP1 A0216 188 VMNTDHKAYL 0.662 38 SB VP1 A0216 108 LMWEAVTVKT 0.606 70 WB VP1 A0216 260 YVSAADICGL 0.545 136 WB VP1 A0216 38 KTGVDAITEV 0.510 199 WB VP1 A0216 304 LLSDLINRRT 0.477 285 WB VP1 A0216 349 YIDRQGQLQT 0.470 309 WB VP1 A0216 28 IKGGVEVLEV 0.430 478 WB VP1 A0216 196 YLDKNNAYPV 0.940 1 SB VP1 A0219 106 NLLMWEAVTV 0.763 12 SB VP1 A0219 224 YTGGENVPPV 0.678 32 SB VP1 A0219 26 LLIKGGVEVL 0.671 35 SB VP1 A0219 260 YVSAADICGL 0.656 41 SB VP1 A0219 244 LLDEQGVGPL 0.644 46 SB VP1 A0219 108 LMWEAVTVKT 0.615 64 WB VP1 A0219 188 VMNTDHKAYL 0.555 122 WB VP1 A0219 84 MLPCYSTARI 0.508 204 WB VP1 A0219 322 YGMESQVEEV 0.492 243 WB VP1 A0219 252 PLCKADSLYV 0.482 270 WB VP1 A0219 307 DLINRRTQKV 0.457 354 WB VP1 A0219 25 KLLIKGGVEV 0.429 484 WB VP1 A0219 107 LLMWEAVTVK 0.689 28 SB VP1 A0301 283 ARYFKIRLRK 0.645 46 SB VP1 A0301 287 KIRLRKRSVK 0.641 48 SB VP1 A0301 83 KMLPCYSTAR 0.532 157 WB VP1 A0301 171 KYPQGTITPK 0.503 216 WB VP1 A0301 278 QWRGLARYFK 0.449 387 WB VP1 A0301 190 NTDHKAYLDK 0.449 388 WB VP1 A0301 125 MLNLHAGSQK 0.679 32 SB VP1 A1101 275 GTQQWRGLAR 0.611 67 WB VP1 A1101 107 LLMWEAVTVK 0.606 70 WB VP1 A1101 185 QSQVMNTDHK 0.571 103 WB VP1 A1101 20 PVQVPKLLIK 0.498 228 WB VP1 A1101 190 NTDHKAYLDK 0.491 247 WB VP1 A1101 83 KMLPCYSTAR 0.430 478 WB VP1 A1101 143 PVQGSNFHFF 0.511 199 WB VP1 A2301 171 KYPQGTITPK 0.457 356 WB VP1 A2301 284 RYFKIRLRKR 0.441 423 WB VP1 A2301 187 QVMNTDHKAY 0.752 14 SB VP1 A2602 46 EVECFLNPEM 0.733 17 SB VP1 A2602 315 KVDGQPMYGM 0.715 21 SB VP1 A2602 294 SVKNPYPISF 0.643 47 SB VP1 A2602 89 STARIPLPNL 0.602 74 WB VP1 A2602 143 PVQGSNFHFF 0.581 92 WB VP1 A2602 260 YVSAADICGL 0.510 201 WB VP1 A2602 116 KTEVIGITSM 0.460 343 WB VP1 A2602 187 QVMNTDHKAY 0.558 119 WB VP1 A2902 163 GVLMNYRTKY 0.462 337 WB VP1 A2902 287 KIRLRKRSVK 0.842 5 SB VP1 A3001 278 QWRGLARYFK 0.767 12 SB VP1 A3001 6 KGECPGAAPK 0.695 27 SB VP1 A3001 16 KPKEPVQVPK 0.691 28 SB VP1 A3001 171 KYPQGTITPK 0.665 37 SB VP1 A3001 125 MLNLHAGSQK 0.599 76 WB VP1 A3001 185 QSQVMNTDHK 0.499 225 WB VP1 A3001 83 KMLPCYSTAR 0.463 333 WB VP1 A3001 282 LARYFKIRLR 0.426 496 WB VP1 A3001 284 RYFKIRLRKR 0.859 4 SB VP1 A3101 83 KMLPCYSTAR 0.777 11 SB VP1 A3101 282 LARYFKIRLR 0.689 28 SB VP1 A3101 287 KIRLRKRSVK 0.682 31 SB VP1 A3101 160 EMQGVLMNYR 0.668 36 SB VP1 A3101 278 QWRGLARYFK 0.657 40 SB VP1 A3101 275 GTQQWRGLAR 0.580 93 WB VP1 A3101 283 ARYFKIRLRK 0.575 99 WB VP1 A3101 302 SFLLSDLINR 0.565 110 WB VP1 A3101 160 EMQGVLMNYR 0.552 127 WB VP1 A3301 302 SFLLSDLINR 0.464 328 WB VP1 A3301 282 LARYFKIRLR 0.443 412 WB VP1 A3301 284 RYFKIRLRKR 0.438 439 WB VP1 A3301 73 NAFESDSPDR 0.798 8 SB VP1 A6801 160 EMQGVLMNYR 0.747 15 SB VP1 A6801 125 MLNLHAGSQK 0.647 45 SB VP1 A6801 282 LARYFKIRLR 0.540 145 WB VP1 A6801 271 TNSSGTQQWR 0.508 205 WB VP1 A6801 107 LLMWEAVTVK 0.504 213 WB VP1 A6801 118 EVIGITSMLN 0.492 243 WB VP1 A6801 54 EMGDPDDNLR 0.481 275 WB VP1 A6801 185 QSQVMNTDHK 0.480 278 WB VP1 A6801 303 FLLSDLINRR 0.453 372 WB VP1 A6801 275 GTQQWRGLAR 0.443 413 WB VP1 A6801 145 QGSNFHFFAV 0.746 15 SB VP1 A6802 241 TTVLLDEQGV 0.705 24 SB VP1 A6802 260 YVSAADICGL 0.681 31 SB VP1 A6802 84 MLPCYSTARI 0.661 39 SB VP1 A6802 89 STARIPLPNL 0.658 40 SB VP1 A6802 111 EAVTVKTEVI 0.641 48 SB VP1 A6802 322 YGMESQVEEV 0.619 61 WB VP1 A6802 224 YTGGENVPPV 0.529 163 WB VP1 A6802 104 CGNLLMWEAV 0.498 228 WB VP1 A6802 200 NNAYPVECWI 0.458 354 WB VP1 A6802 42 DAITEVECFL 0.447 397 WB VP1 A6802 319 QPMYGMESQV 0.444 411 WB VP1 A6802 224 YTGGENVPPV 0.750 14 SB VP1 A6901 196 YLDKNNAYPV 0.662 38 SB VP1 A6901 89 STARIPLPNL 0.596 79 WB VP1 A6901 106 NLLMWEAVTV 0.558 119 WB VP1 A6901 322 YGMESQVEEV 0.518 184 WB VP1 A6901 46 EVECFLNPEM 0.482 271 WB VP1 A6901 19 EPVQVPKLLI 0.478 283 WB VP1 A6901 319 QPMYGMESQV 0.476 289 WB VP1 A6901 157 DPLEMQGVLM 0.439 432 WB VP1 A6901 142 KPVQGSNFHF 0.666 37 SB VP1 B0702 299 YPISFLLSDL 0.604 72 WB VP1 B0702 235 HVTNTATTVL 0.525 170 WB VP1 B0702 319 QPMYGMESQV 0.457 357 WB VP1 B0702 93 IPLPNLNEDL 0.429 484 WB VP1 B0702 66 SQHLSAENAF 0.595 79 WB VP1 B1501 313 TQKVDGQPMY 0.589 85 WB VP1 B1501 187 QVMNTDHKAY 0.570 104 WB VP1 B1501 277 QQWRGLARYF 0.566 109 WB VP1 B1501 276 TQQWRGLARY 0.565 110 WB VP1 B1501 294 SVKNPYPISF 0.507 207 WB VP1 B1501 194 KAYLDKNNAY 0.474 297 WB VP1 B1501 261 VSAADICGLF 0.433 461 WB VP1 B1501 26 LLIKGGVEVL 0.430 478 WB VP1 B1501 159 LEMQGVLMNY 0.712 22 SB VP1 B1801 117 TEVIGITSML 0.548 133 WB VP1 B1801 215 NENTRYFGTY 0.514 192 WB VP1 B1801 110 WEAVTVKTEV 0.509 202 WB VP1 B1801 32 VEVLEVKTGV 0.462 335 WB VP1 B1801 283 ARYFKIRLRK 0.558 119 WB VP1 B2705 152 FAVGGDPLEM 0.756 13 SB VP1 B3501 157 DPLEMQGVLM 0.715 21 SB VP1 B3501 211 DPSRNENTRY 0.683 30 SB VP1 B3501 340 LPGDPDMIRY 0.676 33 SB VP1 B3501 142 KPVQGSNFHF 0.645 46 SB VP1 B3501 187 QVMNTDHKAY 0.604 72 WB VP1 B3501 194 KAYLDKNNAY 0.600 75 WB VP1 B3501 299 YPISFLLSDL 0.560 117 WB VP1 B3501 46 EVECFLNPEM 0.533 156 WB VP1 B3501 79 SPDRKMLPCY 0.513 194 WB VP1 B3501 95 LPNLNEDLTC 0.454 367 WB VP1 B3501 251 GPLCKADSLY 0.435 453 WB VP1 B3501 117 TEVIGITSML 0.570 104 WB VP1 B4001 324 MESQVEEVRV 0.475 293 WB VP1 B4001 53 PEMGDPDDNL 0.473 298 WB VP1 B4001 99 NEDLTCGNLL 0.471 304 WB VP1 B4001 110 WEAVTVKTEV 0.428 488 WB VP1 B4001 215 NENTRYFGTY 0.430 476 WB VP1 B4402 71 AENAFESDSP 0.495 235 WB VP1 B4501 19 EPVQVPKLLI 0.654 42 SB VP1 B5101 299 YPISFLLSDL 0.557 120 WB VP1 B5101 19 EPVQVPKLLI 0.658 40 SB VP1 B5301 299 YPISFLLSDL 0.604 72 WB VP1 B5301 142 KPVQGSNFHF 0.531 159 WB VP1 B5301 340 LPGDPDMIRY 0.523 174 WB VP1 B5301 79 SPDRKMLPCY 0.468 315 WB VP1 B5301 211 DPSRNENTRY 0.468 316 WB VP1 B5301 23 VPKLLIKGGV 0.607 70 WB VP1 B5401 231 PPVLHVTNTA 0.590 84 WB VP1 B5401 85 LPCYSTARIP 0.533 157 WB VP1 B5401 19 EPVQVPKLLI 0.463 332 WB VP1 B5401 203 YPVECWIPDP 0.456 358 WB VP1 B5401 270 FTNSSGTQQW 0.478 285 WB VP1 B5701 270 FTNSSGTQQW 0.738 16 SB VP1 B5801 199 KNNAYPVECW 0.634 52 WB VP1 B5801 261 VSAADICGLF 0.458 351 WB VP1 B5801 11-mers 83 KMLPCYSTARI 0.778 11 SB VP1 A0201 107 LLMWEAVTVKT 0.594 80 WB VP1 A0201 243 VLLDEQGVGPL 0.577 97 WB VP1 A0201 303 FLLSDLINRRT 0.551 129 WB VP1 A0201 233 VLHVTNTATTV 0.497 230 WB VP1 A0201 144 VQGSNFHFFAV 0.461 342 WB VP1 A0201 125 MLNLHAGSQKV 0.459 348 WB VP1 A0201 187 QVMNTDHKAYL 0.444 407 WB VP1 A0201 323 GMESQVEEVRV 0.434 458 WB VP1 A0201 125 MLNLHAGSQKV 0.757 13 SB VP1 A0202 97 NLNEDLTCGNL 0.678 32 SB VP1 A0202 243 VLLDEQGVGPL 0.618 62 WB VP1 A0202 83 KMLPCYSTARI 0.597 78 WB VP1 A0202 107 LLMWEAVTVKT 0.592 82 WB VP1 A0202 323 GMESQVEEVRV 0.558 119 WB VP1 A0202 144 VQGSNFHFFAV 0.548 133 WB VP1 A0202 233 VLHVTNTATTV 0.506 209 WB VP1 A0202 187 QVMNTDHKAYL 0.482 270 WB VP1 A0202 303 FLLSDLINRRT 0.438 436 WB VP1 A0202 125 MLNLHAGSQKV 0.897 3 SB VP1 A0203 27 LIKGGVEVLEV 0.784 10 SB VP1 A0203 83 KMLPCYSTARI 0.744 15 SB VP1 A0203 233 VLHVTNTATTV 0.743 16 SB VP1 A0203 97 NLNEDLTCGNL 0.709 23 SB VP1 A0203 243 VLLDEQGVGPL 0.708 23 SB VP1 A0203 61 NLRGYSQHLSA 0.693 27 SB VP1 A0203 107 LLMWEAVTVKT 0.605 71 WB VP1 A0203 134 KVHENGGGKPV 0.574 99 WB VP1 A0203 144 VQGSNFHFFAV 0.520 180 WB VP1 A0203 294 SVKNPYPISFL 0.475 292 WB VP1 A0203 346 MIRYIDRQGQL 0.471 306 WB VP1 A0203 323 GMESQVEEVRV 0.459 348 WB VP1 A0203 303 FLLSDLINRRT 0.454 367 WB VP1 A0203 125 MLNLHAGSQKV 0.687 29 SB VP1 A0204 233 VLHVTNTATTV 0.655 41 SB VP1 A0204 243 VLLDEQGVGPL 0.629 55 WB VP1 A0204 134 KVHENGGGKPV 0.544 138 WB VP1 A0204 323 GMESQVEEVRV 0.544 138 WB VP1 A0204 83 KMLPCYSTARI 0.497 230 WB VP1 A0204 144 VQGSNFHFFAV 0.476 290 WB VP1 A0204 107 LLMWEAVTVKT 0.464 328 WB VP1 A0204 195 AYLDKNNAYPV 0.460 345 WB VP1 A0204 25 KLLIKGGVEVL 0.443 415 WB VP1 A0204 224 YTGGENVPPVL 0.428 487 WB VP1 A0204 144 VQGSNFHFFAV 0.865 4 SB VP1 A0206 83 KMLPCYSTARI 0.720 20 SB VP1 A0206 125 MLNLHAGSQKV 0.576 97 WB VP1 A0206 243 VLLDEQGVGPL 0.571 103 WB VP1 A0206 318 GQPMYGMESQV 0.519 181 WB VP1 A0206 107 LLMWEAVTVKT 0.498 229 WB VP1 A0206 187 QVMNTDHKAYL 0.485 261 WB VP1 A0206 233 VLHVTNTATTV 0.435 450 WB VP1 A0206 303 FLLSDLINRRT 0.433 462 WB VP1 A0206 243 VLLDEQGVGPL 0.906 2 SB VP1 A0211 233 VLHVTNTATTV 0.899 2 SB VP1 A0211 125 MLNLHAGSQKV 0.897 3 SB VP1 A0211 83 KMLPCYSTARI 0.831 6 SB VP1 A0211 27 LIKGGVEVLEV 0.813 7 SB VP1 A0211 323 GMESQVEEVRV 0.770 12 SB VP1 A0211 244 LLDEQGVGPLC 0.735 17 SB VP1 A0211 61 NLRGYSQHLSA 0.703 24 SB VP1 A0211 304 LLSDLINRRTQ 0.696 26 SB VP1 A0211 25 KLLIKGGVEVL 0.681 31 SB VP1 A0211 134 KVHENGGGKPV 0.674 34 SB VP1 A0211 97 NLNEDLTCGNL 0.669 35 SB VP1 A0211 195 AYLDKNNAYPV 0.636 51 WB VP1 A0211 303 FLLSDLINRRT 0.612 66 WB VP1 A0211 164 VLMNYRTKYPQ 0.607 70 WB VP1 A0211 223 TYTGGENVPPV 0.585 89 WB VP1 A0211 196 YLDKNNAYPVE 0.560 116 WB VP1 A0211 107 LLMWEAVTVKT 0.551 128 WB VP1 A0211 235 HVTNTATTVLL 0.525 171 WB VP1 A0211 22 QVPKLLIKGGV 0.523 174 WB VP1 A0211 268 GLFTNSSGTQQ 0.506 209 WB VP1 A0211 339 QLPGDPDMIRY 0.501 222 WB VP1 A0211 144 VQGSNFHFFAV 0.500 224 WB VP1 A0211 187 QVMNTDHKAYL 0.499 225 WB VP1 A0211 11 GAAPKKPKEPV 0.474 297 WB VP1 A0211 224 YTGGENVPPVL 0.472 302 WB VP1 A0211 160 EMQGVLMNYRT 0.468 317 WB VP1 A0211 349 YIDRQGQLQTK 0.450 385 WB VP1 A0211 240 ATTVLLDEQGV 0.437 443 WB VP1 A0211 233 VLHVTNTATTV 0.838 5 SB VP1 A0212 243 VLLDEQGVGPL 0.823 6 SB VP1 A0212 125 MLNLHAGSQKV 0.813 7 SB VP1 A0212 323 GMESQVEEVRV 0.713 22 SB VP1 A0212 27 LIKGGVEVLEV 0.697 26 SB VP1 A0212 61 NLRGYSQHLSA 0.690 28 SB VP1 A0212 144 VQGSNFHFFAV 0.652 42 SB VP1 A0212 244 LLDEQGVGPLC 0.645 46 SB VP1 A0212 304 LLSDLINRRTQ 0.599 76 WB VP1 A0212 83 KMLPCYSTARI 0.596 79 WB VP1 A0212 164 VLMNYRTKYPQ 0.576 98 WB VP1 A0212 196 YLDKNNAYPVE 0.569 106 WB VP1 A0212 303 FLLSDLINRRT 0.561 115 WB VP1 A0212 224 YTGGENVPPVL 0.543 140 WB VP1 A0212 25 KLLIKGGVEVL 0.530 161 WB VP1 A0212 107 LLMWEAVTVKT 0.511 199 WB VP1 A0212 97 NLNEDLTCGNL 0.491 247 WB VP1 A0212 195 AYLDKNNAYPV 0.490 249 WB VP1 A0212 349 YIDRQGQLQTK 0.465 325 WB VP1 A0212 154 VGGDPLEMQGV 0.464 329 WB VP1 A0212 160 EMQGVLMNYRT 0.460 345 WB VP1 A0212 108 LMWEAVTVKTE 0.438 434 WB VP1 A0212 233 VLHVTNTATTV 0.865 4 SB VP1 A0216 125 MLNLHAGSQKV 0.827 6 SB VP1 A0216 323 GMESQVEEVRV 0.804 8 SB VP1 A0216 27 LIKGGVEVLEV 0.752 14 SB VP1 A0216 243 VLLDEQGVGPL 0.724 19 SB VP1 A0216 83 KMLPCYSTARI 0.660 39 SB VP1 A0216 61 NLRGYSQHLSA 0.647 45 SB VP1 A0216 187 QVMNTDHKAYL 0.643 47 SB VP1 A0216 164 VLMNYRTKYPQ 0.619 61 WB VP1 A0216 195 AYLDKNNAYPV 0.616 64 WB VP1 A0216 11 GAAPKKPKEPV 0.542 142 WB VP1 A0216 294 SVKNPYPISFL 0.530 162 WB VP1 A0216 318 GQPMYGMESQV 0.525 170 WB VP1 A0216 25 KLLIKGGVEVL 0.517 186 WB VP1 A0216 223 TYTGGENVPPV 0.512 196 WB VP1 A0216 268 GLFTNSSGTQQ 0.495 236 WB VP1 A0216 97 NLNEDLTCGNL 0.481 274 WB VP1 A0216 22 QVPKLLIKGGV 0.478 284 WB VP1 A0216 304 LLSDLINRRTQ 0.474 295 WB VP1 A0216 160 EMQGVLMNYRT 0.464 329 WB VP1 A0216 31 GVEVLEVKTGV 0.459 348 WB VP1 A0216 144 VQGSNFHFFAV 0.456 361 WB VP1 A0216 235 HVTNTATTVLL 0.454 368 WB VP1 A0216 303 FLLSDLINRRT 0.453 372 WB VP1 A0216 249 GVGPLCKADSL 0.450 383 WB VP1 A0216 220 YFGTYTGGENV 0.447 394 WB VP1 A0216 37 VKTGVDAITEV 0.439 433 WB VP1 A0216 134 KVHENGGGKPV 0.434 454 WB VP1 A0216 233 VLHVTNTATTV 0.703 24 SB VP1 A0219 125 MLNLHAGSQKV 0.697 26 SB VP1 A0219 243 VLLDEQGVGPL 0.673 34 SB VP1 A0219 27 LIKGGVEVLEV 0.581 93 WB VP1 A0219 144 VQGSNFHFFAV 0.546 135 WB VP1 A0219 323 GMESQVEEVRV 0.511 198 WB VP1 A0219 83 KMLPCYSTARI 0.501 221 WB VP1 A0219 223 TYTGGENVPPV 0.457 357 WB VP1 A0219 154 VGGDPLEMQGV 0.443 413 WB VP1 A0219 224 YTGGENVPPVL 0.428 485 WB VP1 A0219 124 SMLNLHAGSQK 0.698 26 SB VP1 A0301 289 RLRKRSVKNPY 0.560 117 WB VP1 A0301 281 GLARYFKIRLR 0.520 180 WB VP1 A0301 106 NLLMWEAVTVK 0.478 285 WB VP1 A0301 270 FTNSSGTQQWR 0.447 395 WB VP1 A0301 124 SMLNLHAGSQK 0.754 14 SB VP1 A1101 184 AQSQVMNTDHK 0.640 49 SB VP1 A1101 301 ISFLLSDLINR 0.631 54 WB VP1 A1101 277 QQWRGLARYFK 0.573 101 WB VP1 A1101 73 NAFESDSPDRK 0.538 148 WB VP1 A1101 275 GTQQWRGLARY 0.477 288 WB VP1 A1101 106 NLLMWEAVTVK 0.462 336 WB VP1 A1101 161 MQGVLMNYRTK 0.448 390 WB VP1 A1101 312 RTQKVDGQPMY 0.441 421 WB VP1 A1101 282 LARYFKIRLRK 0.432 467 WB VP1 A1101 305 LSDLINRRTQK 0.431 473 WB VP1 A1101 259 LYVSAADICGL 0.573 102 WB VP1 A2301 298 PYPISFLLSDL 0.474 295 WB VP1 A2301 298 PYPISFLLSDL 0.564 111 WB VP1 A2402 167 NYRTKYPQGTI 0.552 128 WB VP1 A2402 278 QWRGLARYFKI 0.438 439 WB VP1 A2402 65 YSQHLSAENAF 0.655 41 SB VP1 A2403 298 PYPISFLLSDL 0.628 56 WB VP1 A2403 259 LYVSAADICGL 0.536 151 WB VP1 A2403 269 LFTNSSGTQQW 0.434 458 WB VP1 A2403 118 EVIGITSMLNL 0.705 24 SB VP1 A2601 78 DSPDRKMLPCY 0.602 74 WB VP1 A2601 118 EVIGITSMLNL 0.894 3 SB VP1 A2602 294 SVKNPYPISFL 0.778 11 SB VP1 A2602 78 DSPDRKMLPCY 0.715 21 SB VP1 A2602 260 YVSAADICGLF 0.691 28 SB VP1 A2602 339 QLPGDPDMIRY 0.669 35 SB VP1 A2602 187 QVMNTDHKAYL 0.618 62 WB VP1 A2602 275 GTQQWRGLARY 0.593 81 WB VP1 A2602 312 RTQKVDGQPMY 0.482 273 WB VP1 A2602 289 RLRKRSVKNPY 0.805 8 SB VP1 A3001 282 LARYFKIRLRK 0.787 10 SB VP1 A3001 6 KGECPGAAPKK 0.656 41 SB VP1 A3001 134 KVHENGGGKPV 0.525 169 WB VP1 A3001 132 SQKVHENGGGK 0.508 205 WB VP1 A3001 312 RTQKVDGQPMY 0.498 227 WB VP1 A3001 277 QQWRGLARYFK 0.477 286 WB VP1 A3001 161 MQGVLMNYRTK 0.455 362 WB VP1 A3001 291 RKRSVKNPYPI 0.432 468 WB VP1 A3001 312 RTQKVDGQPMY 0.474 295 WB VP1 A3002 277 QQWRGLARYFK 0.695 27 SB VP1 A3101 301 ISFLLSDLINR 0.646 46 SB VP1 A3101 302 SFLLSDLINRR 0.634 52 WB VP1 A3101 270 FTNSSGTQQWR 0.615 64 WB VP1 A3101 124 SMLNLHAGSQK 0.602 74 WB VP1 A3101 281 GLARYFKIRLR 0.598 77 WB VP1 A3101 282 LARYFKIRLRK 0.457 355 WB VP1 A3101 161 MQGVLMNYRTK 0.453 371 WB VP1 A3101 82 RKMLPCYSTAR 0.428 486 WB VP1 A3101 301 ISFLLSDLINR 0.516 187 WB VP1 A3301 302 SFLLSDLINRR 0.486 259 WB VP1 A3301 270 FTNSSGTQQWR 0.792 9 SB VP1 A6801 301 ISFLLSDLINR 0.717 21 SB VP1 A6801 73 NAFESDSPDRK 0.709 23 SB VP1 A6801 72 ENAFESDSPDR 0.595 80 WB VP1 A6801 322 YGMESQVEEVR 0.478 284 WB VP1 A6801 282 LARYFKIRLRK 0.478 284 WB VP1 A6801 118 EVIGITSMLNL 0.811 7 SB VP1 A6802 187 QVMNTDHKAYL 0.666 36 SB VP1 A6802 22 QVPKLLIKGGV 0.649 44 SB VP1 A6802 235 HVTNTATTVLL 0.487 257 WB VP1 A6802 330 EVRVFDGTEQL 0.471 306 WB VP1 A6802 103 TCGNLLMWEAV 0.457 354 WB VP1 A6802 118 EVIGITSMLNL 0.681 31 SB VP1 A6901 33 EVLEVKTGVDA 0.574 99 WB VP1 A6901 187 QVMNTDHKAYL 0.533 155 WB VP1 A6901 99 YPISFLLSDLI 0.456 361 WB VP1 A6901 224 YTGGENVPPVL 0.454 366 WB VP1 A6901 235 HVTNTATTVLL 0.449 389 WB VP1 A6901 85 LPCYSTARIPL 0.805 8 SB VP1 B0702 142 KPVQGSNFHFF 0.686 29 SB VP1 B0702 13 APKKPKEPVQV 0.564 112 WB VP1 B0702 1 APTKRKGECPG 0.493 242 WB VP1 B0702 16 KPKEPVQVPKL 0.491 245 WB VP1 B0702 178 TPKNPTAQSQV 0.486 259 WB VP1 B0702 299 YPISFLLSDLI 0.435 452 WB VP1 B0702 285 YFKIRLRKRSV 0.492 244 WB VP1 B0801 276 TQQWRGLARYF 0.585 89 WB VP1 B1501 289 RLRKRSVKNPY 0.578 96 WB VP1 B1501 186 SQVMNTDHKAY 0.565 110 WB VP1 B1501 65 YSQHLSAENAF 0.559 118 WB VP1 B1501 60 YVSAADICGLF 0.550 130 WB VP1 B1501 312 RTQKVDGQPMY 0.427 492 WB VP1 B1501 324 MESQVEEVRVF 0.678 32 SB VP1 B1801 45 TEVECFLNPEM 0.554 124 WB VP1 B1801 75 FESDSPDRKML 0.525 171 WB VP1 B1801 110 WEAVTVKTEVI 0.483 267 WB VP1 B1801 311 RRTQKVDGQPM 0.521 177 WB VP1 B2705 277 QQWRGLARYFK 0.429 480 WB VP1 B2705 142 KPVQGSNFHFF 0.739 16 SB VP1 B3501 203 YPVECWIPDPS 0.712 22 SB VP1 B3501 85 LPCYSTARIPL 0.676 33 SB VP1 B3501 211 DPSRNENTRYF 0.625 57 WB VP1 B3501 65 YSQHLSAENAF 0.609 68 WB VP1 B3501 151 FFAVGGDPLEM 0.579 95 WB VP1 B3501 260 YVSAADICGLF 0.578 96 WB VP1 B3501 299 YPISFLLSDLI 0.498 227 WB VP1 B3501 52 NPEMGDPDDNL 0.470 310 WB VP1 B3501 193 HKAYLDKNNAY 0.461 342 WB VP1 B3501 149 FHFFAVGGDPL 0.586 88 WB VP1 B3901 234 LHVTNTATTVL 0.579 94 WB VP1 B3901 224 YTGGENVPPVL 0.498 227 WB VP1 B3901 75 FESDSPDRKML 0.556 121 WB VP1 B4001 45 TEVECFLNPEM 0.446 402 WB VP1 B4001 45 TEVECFLNPEM 0.451 379 WB VP1 B4002 45 TEVECFLNPEM 0.477 287 WB VP1 B4403 71 AENAFESDSPD 0.487 257 WB VP1 B4501 299 YPISFLLSDLI 0.706 24 SB VP1 B5101 340 LPGDPDMIRYI 0.600 75 WB VP1 B5101 30 VPPVLHVTNTA 0.508 206 WB VP1 B5101 85 LPCYSTARIPL 0.492 243 WB VP1 B5101 299 YPISFLLSDLI 0.735 17 SB VP1 B5301 340 LPGDPDMIRYI 0.564 112 WB VP1 B5301 142 KPVQGSNFHFF 0.534 154 WB VP1 B5301 85 LPCYSTARIPL 0.434 455 WB VP1 B5301 299 YPISFLLSDLI 0.778 11 SB VP1 B5401 230 VPPVLHVTNTA 0.720 20 SB VP1 B5401 203 YPVECWIPDPS 0.657 40 SB VP1 B5401 93 IPLPNLNEDLT 0.542 142 WB VP1 B5401 85 LPCYSTARIPL 0.510 200 WB VP1 B5401 340 LPGDPDMIRYI 0.458 350 WB VP1 B5401 293 RSVKNPYPISF 0.691 28 SB VP1 B5801 SEQ ID NOS.: 53780-54917

Preferred BK virus fragments of small T antigen capable of interacting with one or more MHC class 1 molecules are listed in Table L.

TABLE L Prediction of BK virus small t protein specific MHC class1, 8-, 9-, 10-, 11-mer peptide binders for 42 MHC class 1 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/ NetMHC/ database. The MHC class 1 molecules for which no binders were found are not listed. pos peptide logscore affinity (nM) Bind Level Protein Name Allele 8-mers 124 FLRKEPLV 0.663 38 SB Small t A0201 11 ELMDLLGL 0.599 76 WB Small t A0201 153 TLQWWVQI 0.543 141 WB Small t A0201 74 GTWNSSEV 0.542 141 WB Small t A0201 154 LQWWVQII 0.520 179 WB Small t A0201 110 CMLCQLRL 0.509 202 WB Small t A0201 21 AAWGNLPL 0.473 297 WB Small t A0201 60 KMEQDVKV 0.452 375 WB Small t A0201 11 ELMDLLGL 0.762 13 SB Small t A0202 124 FLRKEPLV 0.715 21 SB Small t A0202 9 SMELMDLL 0.628 56 WB Small t A0202 50 KMKRMNTL 0.586 88 WB Small t A0202 60 KMEQDVKV 0.505 211 WB Small t A0202 27 PLMRKAYL 0.488 254 WB Small t A0202 110 CMLCQLRL 0.475 292 WB Small t A0202 124 FLRKEPLV 0.863 4 SB Small t A0203 50 KMKRMNTL 0.758 13 SB Small t A0203 11 ELMDLLGL 0.712 22 SB Small t A0203 153 TLQWWVQI 0.690 28 SB Small t A0203 110 CMLCQLRL 0.515 189 WB Small t A0203 105 SVHCPCML 0.430 474 WB Small t A0203 60 KMEQDVKV 0.429 484 WB Small t A0203 60 KMEQDVKV 0.615 64 WB Small t A0204 124 FLRKEPLV 0.573 100 WB Small t A0204 153 TLQWWVQI 0.524 172 WB Small t A0204 11 ELMDLLGL 0.521 178 WB Small t A0204 50 KMKRMNTL 0.443 412 WB Small t A0204 154 LQWWVQII 0.679 32 SB Small t A0206 74 GTWNSSEV 0.645 46 SB Small t A0206 11 ELMDLLGL 0.594 80 WB Small t A0206 124 FLRKEPLV 0.581 92 WB Small t A0206 21 AAWGNLPL 0.571 104 WB Small t A0206 110 CMLCQLRL 0.496 233 WB Small t A0206 142 TQWFGLDL 0.494 239 WB Small t A0206 153 TLQWWVQI 0.468 315 WB Small t A0206 60 KMEQDVKV 0.427 490 WB Small t A0206 11 ELMDLLGL 0.904 2 SB Small t A0211 124 FLRKEPLV 0.865 4 SB Small t A0211 153 TLQWWVQI 0.861 4 SB Small t A0211 60 KMEQDVKV 0.845 5 SB Small t A0211 14 DLLGLERA 0.725 19 SB Small t A0211 74 GTWNSSEV 0.720 20 SB Small t A0211 110 CMLCQLRL 0.666 37 SB Small t A0211 27 PLMRKAYL 0.666 37 SB Small t A0211 21 AAWGNLPL 0.638 50 WB Small t A0211 9 SMELMDLL 0.635 51 WB Small t A0211 56 TLYKKMEQ 0.625 57 WB Small t A0211 50 KMKRMNTL 0.582 92 WB Small t A0211 146 GLDLTEET 0.563 113 WB Small t A0211 3 VLNREESM 0.494 239 WB Small t A0211 105 SVHCPCML 0.430 474 WB Small t A0211 148 DLTEETLQ 0.428 487 WB Small t A0211 124 FLRKEPLV 0.884 3 SB Small t A0212 11 ELMDLLGL 0.842 5 SB Small t A0212 153 TLQWWVQI 0.692 28 SB Small t A0212 60 KMEQDVKV 0.666 37 SB Small t A0212 3 VLNREESM 0.639 49 SB Small t A0212 27 PLMRKAYL 0.597 78 WB Small t A0212 110 CMLCQLRL 0.580 94 WB Small t A0212 50 KMKRMNTL 0.579 94 WB Small t A0212 14 DLLGLERA 0.523 174 WB Small t A0212 74 GTWNSSEV 0.521 178 WB Small t A0212 56 TLYKKMEQ 0.520 180 WB Small t A0212 21 AAWGNLPL 0.511 197 WB Small t A0212 9 SMELMDLL 0.426 495 WB Small t A0212 124 FLRKEPLV 0.876 3 SB Small t A0216 27 PLMRKAYL 0.829 6 SB Small t A0216 11 ELMDLLGL 0.740 16 SB Small t A0216 74 GTWNSSEV 0.734 17 SB Small t A0216 60 KMEQDVKV 0.732 18 SB Small t A0216 153 TLQWWVQI 0.684 30 SB Small t A0216 56 TLYKKMEQ 0.662 38 SB Small t A0216 50 KMKRMNTL 0.651 43 SB Small t A0216 21 AAWGNLPL 0.600 75 WB Small t A0216 110 CMLCQLRL 0.577 97 WB Small t A0216 14 DLLGLERA 0.566 109 WB Small t A0216 9 SMELMDLL 0.532 158 WB Small t A0216 146 GLDLTEET 0.453 370 WB Small t A0216 3 VLNREESM 0.429 482 WB Small t A0216 11 ELMDLLGL 0.807 8 SB Small t A0219 124 FLRKEPLV 0.736 17 SB Small t A0219 21 AAWGNLPL 0.637 51 WB Small t A0219 153 TLQWWVQI 0.608 69 WB Small t A0219 27 PLMRKAYL 0.589 85 WB Small t A0219 110 CMLCQLRL 0.548 133 WB Small t A0219 74 GTWNSSEV 0.540 145 WB Small t A0219 116 RLRHLNRK 0.728 19 SB Small t A0301 53 RMNTLYKK 0.719 20 SB Small t A0301 119 HLNRKFLR 0.676 33 SB Small t A0301 28 LMRKAYLK 0.671 35 SB Small t A0301 31 KAYLKKCK 0.506 210 WB Small t A0301 53 RMNTLYKK 0.727 19 SB Small t A1101 31 KAYLKKCK 0.639 49 SB Small t A1101 52 KRMNTLYK 0.454 367 WB Small t A1101 119 HLNRKFLR 0.443 415 WB Small t A1101 160 IIGETPFR 0.438 436 WB Small t A1101 28 LMRKAYLK 0.435 452 WB Small t A1101 131 VWIDCYCI 0.479 280 WB Small t A2301 92 LYCKEWPI 0.458 351 WB Small t A2301 131 VWIDCYCI 0.675 33 SB Small t A2402 92 LYCKEWPI 0.622 60 WB Small t A2402 11 ELMDLLGL 0.486 259 WB Small t A2601 159 QIIGETPF 0.823 6 SB Small t A2602 80 EVCADFPL 0.594 80 WB Small t A2602 66 KVAHQPDF 0.563 112 WB Small t A2602 11 ELMDLLGL 0.500 224 WB Small t A2602 86 PLCPDTLY 0.515 189 WB Small t A2902 116 RLRHLNRK 0.810 7 SB Small t A3001 28 LMRKAYLK 0.805 8 SB Small t A3001 53 RMNTLYKK 0.672 34 SB Small t A3001 31 KAYLKKCK 0.628 55 WB Small t A3001 52 KRMNTLYK 0.620 60 WB Small t A3001 29 MRKAYLKK 0.612 66 WB Small t A3001 120 LNRKFLRK 0.571 104 WB Small t A3001 119 HLNRKFLR 0.850 5 SB Small t A3101 53 RMNTLYKK 0.816 7 SB Small t A3101 111 MLCQLRLR 0.684 30 SB Small t A3101 28 LMRKAYLK 0.646 46 SB Small t A3101 116 RLRHLNRK 0.541 142 WB Small t A3101 160 IIGETPFR 0.540 145 WB Small t A3101 31 KAYLKKCK 0.504 214 WB Small t A3101 119 HLNRKFLR 0.745 15 SB Small t A3301 111 MLCQLRLR 0.521 177 WB Small t A3301 160 IIGETPFR 0.469 313 WB Small t A3301 163 ETPFRDLK 0.799 8 SB Small t A6801 111 MLCQLRLR 0.725 19 SB Small t A6801 119 HLNRKFLR 0.654 42 SB Small t A6801 160 IIGETPFR 0.568 107 WB Small t A6801 80 EVCADFPL 0.773 11 SB Small t A6802 11 ELMDLLGL 0.583 90 WB Small t A6802 8 ESMELMDL 0.563 113 WB Small t A6802 105 SVHCPCML 0.510 200 WB Small t A6802 19 ERAAWGNL 0.434 456 WB Small t A6802 11 ELMDLLGL 0.667 36 SB Small t A6901 80 EVCADFPL 0.549 131 WB Small t A6901 74 GTWNSSEV 0.545 137 WB Small t A6901 85 FPLCPDTL 0.537 150 WB Small t A6901 21 AAWGNLPL 0.513 193 WB Small t A6901 8 ESMELMDL 0.453 372 WB Small t A6901 103 KPSVHCPC 0.540 145 WB Small t B0702 21 AAWGNLPL 0.482 270 WB Small t B0702 26 LPLMRKAY 0.431 472 WB Small t B0702 50 KMKRMNTL 0.479 282 WB Small t B0801 33 YLKKCKEF 0.446 401 WB Small t B0801 159 QIIGETPF 0.529 163 WB Small t B1501 33 YLKKCKEF 0.496 232 WB Small t B1501 50 KMKRMNTL 0.474 294 WB Small t B1501 52 KRMNTLYK 0.623 58 WB Small t B2705 29 MRKAYLKK 0.430 477 WB Small t B2705 26 LPLMRKAY 0.749 15 SB Small t B3501 85 FPLCPDTL 0.706 24 SB Small t B3501 21 AAWGNLPL 0.509 203 WB Small t B3501 159 QIIGETPF 0.457 355 WB Small t B3501 5 NREESMEL 0.555 123 WB Small t B3901 162 GETPFRDL 0.607 69 WB Small t B4001 6 REESMELM 0.511 197 WB Small t B4001 6 REESMELM 0.433 463 WB Small t B4002 151 EETLQWWV 0.428 488 WB Small t B4002 150 TEETLQWW 0.443 414 WB Small t B4402 151 EETLQWWV 0.426 497 WB Small t B4403 151 EETLQWWV 0.447 397 WB Small t B4501 — 85 FPLCPDTL 0.509 202 WB Small t B5101 108 CPCMLCQL 0.480 276 WB Small t B5101 26 LPLMRKAY 0.636 51 WB Small t B5301 85 FPLCPDTL 0.559 117 WB Small t B5301 26 LPLMRKAY 0.482 271 WB Small t B5401 149 LTEETLQW 0.602 74 WB Small t B5701 149 LTEETLQW 0.555 123 WB Small t B5801 66 KVAHQPDF 0.491 246 WB Small t B5801 16 LGLERAAW 0.439 430 WB Small t B5801 9-mers 91 TLYCKEWPI 0.629 55 WB Small t A0201 153 TLQWWVQII 0.605 71 WB Small t A0201 130 LVWIDCYCI 0.509 201 WB Small t A0201 91 TLYCKEWPI 0.697 26 SB Small t A0202 146 GLDLTEETL 0.429 483 WB Small t A0202 153 TLQWWVQII 0.838 5 SB Small t A0203 91 TLYCKEWPI 0.728 18 SB Small t A0203 20 RAAWGNLPL 0.491 246 WB Small t A0203 53 RMNTLYKKM 0.490 249 WB Small t A0203 153 TLQWWVQII 0.535 152 WB Small t A0204 91 TLYCKEWPI 0.525 170 WB Small t A0204 59 KKMEQDVKV 0.514 191 WB Small t A0204 158 VQIIGETPF 0.700 25 SB Small t A0206 142 TQWFGLDLT 0.667 36 SB Small t A0206 91 TLYCKEWPI 0.660 39 SB Small t A0206 20 RAAWGNLPL 0.634 52 WB Small t A0206 79 SEVCADFPL 0.515 189 WB Small t A0206 10 MELMDLLGL 0.496 233 WB Small t A0206 21 AAWGNLPLM 0.457 357 WB Small t A0206 146 GLDLTEETL 0.857 4 SB Small t A0211 91 TLYCKEWPI 0.856 4 SB Small t A0211 153 TLQWWVQII 0.797 8 SB Small t A0211 20 RAAWGNLPL 0.620 61 WB Small t A0211 14 DLLGLERAA 0.614 65 WB Small t A0211 86 PLCPDTLYC 0.564 111 WB Small t A0211 130 LVWIDCYCI 0.505 210 WB Small t A0211 73 FGTWNSSEV 0.481 274 WB Small t A0211 21 AAWGNLPLM 0.448 394 WB Small t A0211 152 ETLQWWVQI 0.445 404 WB Small t A0211 98 PICSKKPSV 0.436 448 WB Small t A0211 129 PLVWIDCYC 0.432 465 WB Small t A0211 146 GLDLTEETL 0.773 11 SB Small t A0212 91 TLYCKEWPI 0.751 14 SB Small t A0212 153 TLQWWVQII 0.666 37 SB Small t A0212 14 DLLGLERAA 0.548 133 WB Small t A0212 141 FTQWFGLDL 0.521 178 WB Small t A0212 98 PICSKKPSV 0.430 474 WB Small t A0212 146 GLDLTEETL 0.773 11 SB Small t A0216 91 TLYCKEWPI 0.720 20 SB Small t A0216 98 PICSKKPSV 0.617 62 WB Small t A0216 153 TLQWWVQII 0.518 184 WB Small t A0216 129 PLVWIDCYC 0.472 302 WB Small t A0216 146 GLDLTEETL 0.704 24 SB Small t A0219 153 TLQWWVQII 0.531 160 WB Small t A0219 21 AAWGNLPLM 0.506 209 WB Small t A0219 91 TLYCKEWPI 0.505 211 WB Small t A0219 119 HLNRKFLRK 0.834 6 SB Small t A0301 28 LMRKAYLKK 0.703 24 SB Small t A0301 50 KMKRMNTLY 0.654 42 SB Small t A0301 27 PLMRKAYLK 0.578 96 WB Small t A0301 114 QLRLRHLNR 0.447 397 WB Small t A0301 119 HLNRKFLRK 0.694 27 SB Small t A1101 27 PLMRKAYLK 0.576 98 WB Small t A1101 159 QIIGETPFR 0.516 187 WB Small t A1101 32 AYLKKCKEF 0.708 23 SB Small t A2301 32 AYLKKCKEF 0.523 174 WB Small t A2402 32 AYLKKCKEF 0.859 4 SB Small t A2403 68 AHQPDFGTW 0.542 142 WB Small t A2403 8 ESMELMDLL 0.463 335 WB Small t A2601 163 ETPFRDLKL 0.795 9 SB Small t A2602 152 ETLQWWVQI 0.499 225 WB Small t A2602 8 ESMELMDLL 0.476 290 WB Small t A2602 50 KMKRMNTLY 0.576 98 WB Small t A2902 85 FPLCPDTLY 0.475 291 WB Small t A2902 28 LMRKAYLKK 0.830 6 SB Small t A3001 51 MKRMNTLYK 0.827 6 SB Small t A3001 36 KCKEFHPDK 0.817 7 SB Small t A3001 114 QLRLRHLNR 0.516 187 WB Small t A3001 50 KMKRMNTLY 0.501 220 WB Small t A3001 119 HLNRKFLRK 0.445 405 WB Small t A3001 27 PLMRKAYLK 0.439 431 WB Small t A3001 52 KRMNTLYKK 0.435 453 WB Small t A3001 50 KMKRMNTLY 0.561 115 WB Small t A3002 118 RHLNRKFLR 0.820 7 SB Small t A3101 110 CMLCQLRLR 0.649 44 SB Small t A3101 114 QLRLRHLNR 0.628 56 WB Small t A3101 50 KMKRMNTLY 0.540 144 WB Small t A3101 119 HLNRKFLRK 0.514 191 WB Small t A3101 28 LMRKAYLKK 0.436 447 WB Small t A3101 114 QLRLRHLNR 0.699 25 SB Small t A3301 159 QIIGETPFR 0.822 6 SB Small t A6801 108 CPCMLCQLR 0.553 125 WB Small t A6801 8 ESMELMDLL 0.767 12 SB Small t A6802 139 DCFTQWFGL 0.659 40 SB Small t A6802 73 FGTWNSSEV 0.580 94 WB Small t A6802 152 ETLQWWVQI 0.522 175 WB Small t A6802 134 DCYCIDCFT 0.491 247 WB Small t A6802 163 ETPFRDLKL 0.490 247 WB Small t A6802 152 ETLQWWVQI 0.832 6 SB Small t A6901 8 ESMELMDLL 0.609 68 WB Small t A6901 91 TLYCKEWPI 0.506 210 WB Small t A6901 130 LVWIDCYCI 0.492 244 WB Small t A6901 21 AAWGNLPLM 0.483 267 WB Small t A6901 20 RAAWGNLPL 0.721 20 SB Small t B0702 26 LPLMRKAYL 0.719 20 SB Small t B0702 103 KPSVHCPCM 0.431 472 WB Small t B0702 158 VQIIGETPF 0.615 64 WB Small t B1501 50 KMKRMNTLY 0.561 115 WB Small t B1501 116 RLRHLNRKF 0.503 216 WB Small t B1501 20 RAAWGNLPL 0.444 411 WB Small t B1501 10 MELMDLLGL 0.722 20 SB Small t B1801 150 TEETLQWWV 0.497 230 WB Small t B1801 79 SEVCADFPL 0.470 308 WB Small t B1801 52 KRMNTLYKK 0.656 41 SB Small t B2705 85 FPLCPDTLY 0.805 8 SB Small t B3501 128 EPLVWIDCY 0.750 14 SB Small t B3501 20 RAAWGNLPL 0.618 62 WB Small t B3501 21 AAWGNLPLM 0.545 137 WB Small t B3501 103 KPSVHCPCM 0.451 377 WB Small t B3501 10 MELMDLLGL 0.751 14 SB Small t B4001 79 SEVCADFPL 0.738 16 SB Small t B4001 7 EESMELMDL 0.561 115 WB Small t B4001 18 LERAAWGNL 0.497 231 WB Small t B4001 79 SEVCADFPL 0.455 365 WB Small t B4002 79 SEVCADFPL 0.591 83 WB Small t B4403 151 EETLQWWVQ 0.463 334 WB Small t B4403 85 FPLCPDTLY 0.710 23 SB Small t B5301 128 EPLVWIDCY 0.651 43 SB Small t B5301 26 LPLMRKAYL 0.625 57 WB Small t B5301 97 WPICSKKPS 0.548 132 WB Small t B5401 149 LTEETLQWW 0.564 112 WB Small t B5701 124 FLRKEPLVW 0.534 154 WB Small t B5801 20 RAAWGNLPL 0.460 344 WB Small t B5801 10-mers 124 FLRKEPLVWI 0.574 100 WB Small t A0201 56 TLYKKMEQDV 0.485 263 WB Small t A0201 12 LMDLLGLERA 0.456 361 WB Small t A0201 3 VLNREESMEL 0.434 454 WB Small t A0201 111 MLCQLRLRHL 0.647 45 SB Small t A0202 124 FLRKEPLVWI 0.608 69 WB Small t A0202 12 LMDLLGLERA 0.607 70 WB Small t A0202 3 VLNREESMEL 0.562 114 WB Small t A0202 56 TLYKKMEQDV 0.516 187 WB Small t A0202 145 FGLDLTEETL 0.516 188 WB Small t A0202 9 SMELMDLLGL 0.507 206 WB Small t A0202 25 NLPLMRKAYL 0.483 269 WB Small t A0202 124 FLRKEPLVWI 0.870 4 SB Small t A0203 56 TLYKKMEQDV 0.707 23 SB Small t A0203 3 VLNREESMEL 0.666 37 SB Small t A0203 111 MLCQLRLRHL 0.549 131 WB Small t A0203 12 LMDLLGLERA 0.468 314 WB Small t A0203 9 SMELMDLLGL 0.462 338 WB Small t A0203 116 RLRHLNRKFL 0.429 484 WB Small t A0203 149 LTEETLQWWV 0.571 104 WB Small t A0204 3 VLNREESMEL 0.557 120 WB Small t A0204 124 FLRKEPLVWI 0.500 223 WB Small t A0204 149 LTEETLQWWV 0.581 93 WB Small t A0206 154 LQWWVQIIGE 0.521 177 WB Small t A0206 20 RAAWGNLPLM 0.518 184 WB Small t A0206 142 TQWFGLDLTE 0.463 334 WB Small t A0206 124 FLRKEPLVWI 0.430 474 WB Small t A0206 56 TLYKKMEQDV 0.875 3 SB Small t A0211 3 VLNREESMEL 0.824 6 SB Small t A0211 149 LTEETLQWWV 0.779 10 SB Small t A0211 12 LMDLLGLERA 0.757 13 SB Small t A0211 124 FLRKEPLVWI 0.715 21 SB Small t A0211 9 SMELMDLLGL 0.706 24 SB Small t A0211 111 MLCQLRLRHL 0.689 28 SB Small t A0211 25 NLPLMRKAYL 0.682 31 SB Small t A0211 129 PLVWIDCYCI 0.681 31 SB Small t A0211 116 RLRHLNRKFL 0.554 124 WB Small t A0211 146 GLDLTEETLQ 0.516 188 WB Small t A0211 17 GLERAAWGNL 0.502 219 WB Small t A0211 145 FGLDLTEETL 0.451 381 WB Small t A0211 56 TLYKKMEQDV 0.893 3 SB Small t A0212 3 VLNREESMEL 0.788 9 SB Small t A0212 124 FLRKEPLVWI 0.756 13 SB Small t A0212 149 LTEETLQWWV 0.727 19 SB Small t A0212 12 LMDLLGLERA 0.604 72 WB Small t A0212 111 MLCQLRLRHL 0.584 90 WB Small t A0212 9 SMELMDLLGL 0.579 95 WB Small t A0212 145 FGLDLTEETL 0.484 264 WB Small t A0212 25 NLPLMRKAYL 0.477 287 WB Small t A0212 116 RLRHLNRKFL 0.449 386 WB Small t A0212 17 GLERAAWGNL 0.430 474 WB Small t A0212 56 TLYKKMEQDV 0.842 5 SB Small t A0216 3 VLNREESMEL 0.768 12 SB Small t A0216 25 NLPLMRKAYL 0.703 24 SB Small t A0216 124 FLRKEPLVWI 0.687 29 SB Small t A0216 149 LTEETLQWWV 0.632 53 WB Small t A0216 111 MLCQLRLRHL 0.627 56 WB Small t A0216 116 RLRHLNRKFL 0.566 110 WB Small t A0216 17 GLERAAWGNL 0.545 137 WB Small t A0216 129 PLVWIDCYCI 0.522 175 WB Small t A0216 12 LMDLLGLERA 0.484 265 WB Small t A0216 9 SMELMDLLGL 0.468 316 WB Small t A0216 149 LTEETLQWWV 0.627 56 WB Small t A0219 3 VLNREESMEL 0.573 101 WB Small t A0219 56 TLYKKMEQDV 0.570 104 WB Small t A0219 124 FLRKEPLVWI 0.551 128 WB Small t A0219 12 LMDLLGLERA 0.486 260 WB Small t A0219 50 KMKRMNTLYK 0.754 14 SB Small t A0301 118 RHLNRKFLRK 0.678 32 SB Small t A0301 27 PLMRKAYLKK 0.663 38 SB Small t A0301 114 QLRLRHLNRK 0.562 114 WB Small t A0301 22 AWGNLPLMRK 0.533 156 WB Small t A0301 26 LPLMRKAYLK 0.500 222 WB Small t A0301 50 KMKRMNTLYK 0.700 25 SB Small t A1101 27 PLMRKAYLKK 0.478 284 WB Small t A1101 21 AAWGNLPLMR 0.475 293 WB Small t A1101 22 AWGNLPLMRK 0.449 387 WB Small t A1101 86 PLCPDTLYCK 0.444 410 WB Small t A1101 135 CYCIDCFTQW 0.623 58 WB Small t A2301 57 LYKKMEQDVK 0.531 160 WB Small t A2301 136 YCIDCFTQWF 0.433 463 WB Small t A2301 135 CYCIDCFTQW 0.616 63 WB Small t A2403 123 KFLRKEPLVW 0.549 132 WB Small t A2403 64 DVKVAHQPDF 0.665 37 SB Small t A2602 152 ETLQWWVQII 0.483 269 WB Small t A2602 84 DFPLCPDTLY 0.458 353 WB Small t A2902 50 KMKRMNTLYK 0.848 5 SB Small t A3001 114 QLRLRHLNRK 0.729 18 SB Small t A3001 51 MKRMNTLYKK 0.685 30 SB Small t A3001 27 PLMRKAYLKK 0.500 224 WB Small t A3001 116 RLRHLNRKFL 0.497 231 WB Small t A3001 29 MRKAYLKKCK 0.488 255 WB Small t A3001 117 LRHLNRKFLR 0.676 33 SB Small t A3101 113 CQLRLRHLNR 0.674 34 SB Small t A3101 50 KMKRMNTLYK 0.640 49 SB Small t A3101 51 MKRMNTLYKK 0.468 316 WB Small t A3101 118 RHLNRKFLRK 0.446 400 WB Small t A3101 11 ELMDLLGLER 0.512 196 WB Small t A3301 117 LRHLNRKFLR 0.430 476 WB Small t A3301 11 ELMDLLGLER 0.720 20 SB Small t A6801 90 DTLYCKEWPI 0.574 99 WB Small t A6802 152 ETLQWWVQII 0.456 358 WB Small t A6802 19 ERAAWGNLPL 0.452 375 WB Small t A6802 152 ETLQWWVQII 0.795 9 SB Small t A6901 90 DTLYCKEWPI 0.586 88 WB Small t A6901 149 LTEETLQWWV 0.575 98 WB Small t A6901 97 WPICSKKPSV 0.518 184 WB Small t A6901 103 KPSVHCPCML 0.703 24 SB Small t B0702 97 WPICSKKPSV 0.563 113 WB Small t B0702 116 RLRHLNRKFL 0.471 304 WB Small t B0702 157 WVQIIGETPF 0.540 145 WB Small t B1501 52 KRMNTLYKKM 0.591 83 WB Small t B2705 157 WVQIIGETPF 0.638 50 WB Small t B3501 20 RAAWGNLPLM 0.595 80 WB Small t B3501 136 YCIDCFTQWF 0.429 483 WB Small t B3501 19 ERAAWGNLPL 0.539 147 WB Small t B3901 6 REESMELMDL 0.707 23 SB Small t B4001 162 GETPFRDLKL 0.618 62 WB Small t B4001 7 EESMELMDLL 0.488 253 WB Small t B4001 7 EESMELMDLL 0.482 271 WB Small t B4002 127 KEPLVWIDCY 0.429 481 WB Small t B4402 151 EETLQWWVQI 0.495 235 WB Small t B4403 127 KEPLVWIDCY 0.434 456 WB Small t B4403 97 WPICSKKPSV 0.434 454 WB Small t B5101 97 WPICSKKPSV 0.735 17 SB Small t B5401 26 LPLMRKAYLK 0.511 197 WB Small t B5401 67 VAHQPDFGTW 0.448 393 WB Small t B5701 123 KFLRKEPLVW 0.620 60 WB Small t B5801 67 VAHQPDFGTW 0.537 149 WB Small t B5801 20 RAAWGNLPLM 0.485 263 WB Small t B5801 31 KAYLKKCKEF 0.431 473 WB Small t B5801 11-mers 11 ELMDLLGLERA 0.458 351 WB Small t A0201 2 KVLNREESMEL 0.432 467 WB Small t A0201 11 ELMDLLGLERA 0.582 92 WB Small t A0202 137 CIDCFTQWFGL 0.516 187 WB Small t A0202 3 VLNREESMELM 0.491 245 WB Small t A0202 148 DLTEETLQWWV 0.445 404 WB Small t A0202 11 ELMDLLGLERA 0.652 42 SB Small t A0203 110 CMLCQLRLRHL 0.520 180 WB Small t A0203 3 VLNREESMELM 0.473 298 WB Small t A0203 105 SVHCPCMLCQL 0.449 389 WB Small t A0203 2 KVLNREESMEL 0.525 170 WB Small t A0204 148 DLTEETLQWWV 0.453 372 WB Small t A0204 105 SVHCPCMLCQL 0.450 384 WB Small t A0204 2 KVLNREESMEL 0.620 61 WB Small t A0206 154 LQWWVQIIGET 0.600 75 WB Small t A0206 137 CIDCFTQWFGL 0.565 110 WB Small t A0206 142 TQWFGLDLTEE 0.519 182 WB Small t A0206 132 WIDCYCIDCFT 0.435 452 WB Small t A0206 148 DLTEETLQWWV 0.957 1 SB Small t A0211 11 ELMDLLGLERA 0.815 7 SB Small t A0211 137 CIDCFTQWFGL 0.698 26 SB Small t A0211 12 LMDLLGLERAA 0.669 35 SB Small t A0211 2 KVLNREESMEL 0.597 77 WB Small t A0211 105 SVHCPCMLCQL 0.539 146 WB Small t A0211 3 VLNREESMELM 0.535 153 WB Small t A0211 148 DLTEETLQWWV 0.806 8 SB Small t A0212 11 ELMDLLGLERA 0.654 42 SB Small t A0212 12 LMDLLGLERAA 0.577 96 WB Small t A0212 137 CIDCFTQWFGL 0.551 128 WB Small t A0212 3 VLNREESMELM 0.514 192 WB Small t A0212 2 KVLNREESMEL 0.481 273 WB Small t A0212 148 DLTEETLQWWV 0.886 3 SB Small t A0216 11 ELMDLLGLERA 0.650 43 SB Small t A0216 2 KVLNREESMEL 0.514 191 WB Small t A0216 105 SVHCPCMLCQL 0.496 233 WB Small t A0216 137 CIDCFTQWFGL 0.440 427 WB Small t A0216 148 DLTEETLQWWV 0.849 5 SB Small t A0219 11 ELMDLLGLERA 0.602 73 WB Small t A0219 137 CIDCFTQWFGL 0.566 109 WB Small t A0219 50 KMKRMNTLYKK 0.667 36 SB Small t A0301 116 RLRHLNRKFLR 0.645 46 SB Small t A0301 56 TLYKKMEQDVK 0.645 46 SB Small t A0301 21 AAWGNLPLMRK 0.508 205 WB Small t A0301 28 LMRKAYLKKCK 0.454 369 WB Small t A0301 160 IIGETPFRDLK 0.432 464 WB Small t A0301 21 AAWGNLPLMRK 0.742 16 SB Small t A1101 56 TLYKKMEQDVK 0.640 49 SB Small t A1101 50 KMKRMNTLYKK 0.634 52 WB Small t A1101 160 IIGETPFRDLK 0.632 53 WB Small t A1101 113 CQLRLRHLNRK 0.537 149 WB Small t A1101 20 RAAWGNLPLMR 0.531 160 WB Small t A1101 135 CYCIDCFTQWF 0.785 10 SB Small t A2301 131 VWIDCYCIDCF 0.697 26 SB Small t A2301 92 LYCKEWPICSK 0.544 139 WB Small t A2301 156 WWVQIIGETPF 0.530 161 WB Small t A2301 75 TWNSSEVCADF 0.493 240 WB Small t A2301 131 VWIDCYCIDCF 0.708 23 SB Small t A2402 135 CYCIDCFTQWF 0.672 34 SB Small t A2402 156 WWVQIIGETPF 0.515 190 WB Small t A2402 123 KFLRKEPLVWI 0.489 251 WB Small t A2402 75 TWNSSEVCADF 0.462 339 WB Small t A2402 135 CYCIDCFTQWF 0.775 11 SB Small t A2403 123 KFLRKEPLVWI 0.525 170 WB Small t A2403 75 TWNSSEVCADF 0.428 485 WB Small t A2403 8 ESMELMDLLGL 0.474 297 WB Small t A2601 159 QIIGETPFRDL 0.618 62 WB Small t A2602 8 ESMELMDLLGL 0.433 462 WB Small t A2602 50 KMKRMNTLYKK 0.760 13 SB Small t A3001 28 LMRKAYLKKCK 0.745 15 SB Small t A3001 116 RLRHLNRKFLR 0.667 36 SB Small t A3001 117 LRHLNRKFLRK 0.531 160 WB Small t A3001 34 LKKCKEFHPDK 0.429 482 WB Small t A3001 116 RLRHLNRKFLR 0.853 4 SB Small t A3101 50 KMKRMNTLYKK 0.838 5 SB Small t A3101 20 RAAWGNLPLMR 0.617 63 WB Small t A3101 157 WVQIIGETPFR 0.496 232 WB Small t A3101 112 LCQLRLRHLNR 0.451 380 WB Small t A3101 31 KAYLKKCKEFH 0.448 392 WB Small t A3101 113 CQLRLRHLNRK 0.434 458 WB Small t A3101 28 LMRKAYLKKCK 0.433 461 WB Small t A3101 116 RLRHLNRKFLR 0.594 80 WB Small t A3301 157 WVQIIGETPFR 0.716 21 SB Small t A6801 20 RAAWGNLPLMR 0.562 114 WB Small t A6801 56 TLYKKMEQDVK 0.549 131 WB Small t A6801 25 NLPLMRKAYLK 0.482 272 WB Small t A6801 108 CPCMLCQLRLR 0.467 319 WB Small t A6801 8 ESMELMDLLGL 0.653 42 SB Small t A6802 77 NSSEVCADFPL 0.649 44 SB Small t A6802 11 ELMDLLGLERA 0.570 105 WB Small t A6802 105 SVHCPCMLCQL 0.506 209 WB Small t A6802 137 CIDCFTQWFGL 0.468 315 WB Small t A6802 128 EPLVWIDCYCI 0.606 71 WB Small t A6901 8 ESMELMDLLGL 0.560 116 WB Small t A6901 11 ELMDLLGLERA 0.539 145 WB Small t A6901 148 DLTEETLQWWV 0.482 273 WB Small t A6901 55 NTLYKKMEQDV 0.432 464 WB Small t A6901 114 QLRLRHLNRKF 0.463 333 WB Small t B0801 114 QLRLRHLNRKF 0.473 298 WB Small t B1501 18 LERAAWGNLPL 0.572 102 WB Small t B1801 41 HPDKGGDEDKM 0.545 136 WB Small t B3501 97 WPICSKKPSVH 0.529 164 WB Small t B3501 156 WWVQIIGETPF 0.482 270 WB Small t B3501 6 REESMELMDLL 0.673 34 SB Small t B4001 18 LERAAWGNLPL 0.630 54 WB Small t B4001 47 DEDKMKRMNTL 0.434 458 WB Small t B4001 6 REESMELMDLL 0.511 198 WB Small t B4002 151 EETLQWWVQII 0.500 224 WB Small t B4002 128 EPLVWIDCYCI 0.605 72 WB Small t B5101 128 EPLVWIDCYCI 0.529 163 WB Small t B5301 85 FPLCPDTLYCK 0.471 304 WB Small t B5401 66 KVAHQPDFGTW 0.658 40 SB Small t B5801 122 RKFLRKEPLVW 0.499 225 WB Small t B5801 SEQ ID NOS.: 54918-55453

Preferred BK virus fragments of large T antigen capable of interacting with one or more MHC class 1 molecules are listed in Table M.

TABLE M Prediction of BK virus Large T protein specific MHC class1, 8-, 9-, 10-, 11-mer peptide binders for 42 MHC class 1 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/ NetMHC/ database. The MHC class 1 molecules for which no binders were found are not listed. pos peptide logscore affinity (nM) Bind Level Protein Name Allele 8-mers 77 NSSEVPTY 0.514 193 WB Large T A0101 611 YTFSRMKY 0.480 276 WB Large T A0101 175 KLMEKYSV 0.847 5 SB Large T A0201 388 YMAGVAWL 0.833 6 SB Large T A0201 287 FLLLGMYL 0.807 8 SB Large T A0201 501 YLDGSVKV 0.800 8 SB Large T A0201 272 KLITEYAV 0.733 18 SB Large T A0201 469 YMVVFEDV 0.711 22 SB Large T A0201 579 LLIWFRPV 0.705 24 SB Large T A0201 372 KMDLIFGA 0.695 27 SB Large T A0201 155 RTLACFAV 0.663 38 SB Large T A0201 293 YLEFQYNV 0.656 41 SB Large T A0201 527 VTMNEYPV 0.629 55 WB Large T A0201 563 FLLEKRIL 0.620 61 WB Large T A0201 322 FANAIIFA 0.612 66 WB Large T A0201 231 YLLYSALT 0.611 67 WB Large T A0201 557 SLQNSEFL 0.608 69 WB Large T A0201 11 ELMDLLGL 0.599 76 WB Large T A0201 215 KLCTFSFL 0.590 84 WB Large T A0201 457 RLTFELGV 0.587 86 WB Large T A0201 398 LLPKMDSV 0.582 91 WB Large T A0201 465 AIDQYMVV 0.565 111 WB Large T A0201 369 ILDKMDLI 0.551 128 WB Large T A0201 74 GTWNSSEV 0.542 141 WB Large T A0201 603 RLDSEISM 0.535 153 WB Large T A0201 569 ILQSGMTL 0.529 164 WB Large T A0201 573 GMTLLLLL 0.519 181 WB Large T A0201 146 FLSQAVFS 0.495 234 WB Large T A0201 21 AAWGNLPL 0.473 297 WB Large T A0201 448 ALNVNLPM 0.468 316 WB Large T A0201 609 SMYTFSRM 0.459 347 WB Large T A0201 574 MTLLLLLI 0.458 350 WB Large T A0201 60 KMEQDVKV 0.452 375 WB Large T A0201 388 YMAGVAWL 0.861 4 SB Large T A0202 175 KLMEKYSV 0.858 4 SB Large T A0202 293 YLEFQYNV 0.811 7 SB Large T A0202 287 FLLLGMYL 0.800 8 SB Large T A0202 272 KLITEYAV 0.772 11 SB Large T A0202 11 ELMDLLGL 0.762 13 SB Large T A0202 146 FLSQAVFS 0.740 16 SB Large T A0202 322 FANAIIFA 0.740 16 SB Large T A0202 215 KLCTFSFL 0.732 18 SB Large T A0202 398 LLPKMDSV 0.721 20 SB Large T A0202 501 YLDGSVKV 0.716 21 SB Large T A0202 557 SLQNSEFL 0.712 22 SB Large T A0202 570 LQSGMTLL 0.696 26 SB Large T A0202 372 KMDLIFGA 0.672 34 SB Large T A0202 457 RLTFELGV 0.666 37 SB Large T A0202 573 GMTLLLLL 0.655 41 SB Large T A0202 579 LLIWFRPV 0.643 47 SB Large T A0202 9 SMELMDLL 0.628 56 WB Large T A0202 469 YMVVFEDV 0.606 70 WB Large T A0202 558 LQNSEFLL 0.596 78 WB Large T A0202 563 FLLEKRIL 0.593 81 WB Large T A0202 50 KMKRMNTL 0.586 88 WB Large T A0202 369 ILDKMDLI 0.585 89 WB Large T A0202 391 GVAWLHCL 0.577 96 WB Large T A0202 491 GINNLDSL 0.576 98 WB Large T A0202 184 FISRHMCA 0.571 103 WB Large T A0202 514 HLNKRTQI 0.561 115 WB Large T A0202 377 FGAHGNAV 0.549 131 WB Large T A0202 569 ILQSGMTL 0.546 135 WB Large T A0202 527 VTMNEYPV 0.533 156 WB Large T A0202 226 GVNKEYLL 0.525 171 WB Large T A0202 448 ALNVNLPM 0.512 196 WB Large T A0202 355 HMTREEML 0.510 200 WB Large T A0202 60 KMEQDVKV 0.505 211 WB Large T A0202 27 PLMRKAYL 0.488 254 WB Large T A0202 603 RLDSEISM 0.481 276 WB Large T A0202 144 HQFLSQAV 0.472 301 WB Large T A0202 465 AIDQYMVV 0.458 353 WB Large T A0202 155 RTLACFAV 0.443 412 WB Large T A0202 609 SMYTFSRM 0.442 419 WB Large T A0202 464 VAIDQYMV 0.429 483 WB Large T A0202 388 YMAGVAWL 0.893 3 SB Large T A0203 579 LLIWFRPV 0.884 3 SB Large T A0203 175 KLMEKYSV 0.870 4 SB Large T A0203 501 YLDGSVKV 0.811 7 SB Large T A0203 457 RLTFELGV 0.781 10 SB Large T A0203 287 FLLLGMYL 0.780 10 SB Large T A0203 272 KLITEYAV 0.779 10 SB Large T A0203 398 LLPKMDSV 0.777 11 SB Large T A0203 293 YLEFQYNV 0.769 12 SB Large T A0203 50 KMKRMNTL 0.758 13 SB Large T A0203 469 YMVVFEDV 0.736 17 SB Large T A0203 11 ELMDLLGL 0.712 22 SB Large T A0203 569 ILQSGMTL 0.711 22 SB Large T A0203 322 FANAIIFA 0.697 26 SB Large T A0203 184 FISRHMCA 0.689 28 SB Large T A0203 514 HLNKRTQI 0.680 31 SB Large T A0203 609 SMYTFSRM 0.642 48 SB Large T A0203 563 FLLEKRIL 0.628 55 WB Large T A0203 372 KMDLIFGA 0.622 59 WB Large T A0203 570 LQSGMTLL 0.608 69 WB Large T A0203 215 KLCTFSFL 0.607 70 WB Large T A0203 391 GVAWLHCL 0.570 104 WB Large T A0203 448 ALNVNLPM 0.556 122 WB Large T A0203 188 HMCAGHNI 0.551 128 WB Large T A0203 527 VTMNEYPV 0.548 132 WB Large T A0203 573 GMTLLLLL 0.535 153 WB Large T A0203 520 QIFPPGLV 0.531 159 WB Large T A0203 146 FLSQAVFS 0.528 165 WB Large T A0203 144 HQFLSQAV 0.527 166 WB Large T A0203 491 GINNLDSL 0.526 168 WB Large T A0203 557 SLQNSEFL 0.517 186 WB Large T A0203 465 AIDQYMVV 0.513 193 WB Large T A0203 155 RTLACFAV 0.509 202 WB Large T A0203 464 VAIDQYMV 0.497 232 WB Large T A0203 551 KIYLRKSL 0.489 252 WB Large T A0203 369 ILDKMDLI 0.466 321 WB Large T A0203 654 SQVSDTSA 0.462 338 WB Large T A0203 231 YLLYSALT 0.453 372 WB Large T A0203 199 LTPHRHRV 0.447 394 WB Large T A0203 60 KMEQDVKV 0.429 484 WB Large T A0203 615 RMKYNICM 0.427 490 WB Large T A0203 175 KLMEKYSV 0.762 13 SB Large T A0204 388 YMAGVAWL 0.708 23 SB Large T A0204 272 KLITEYAV 0.652 43 SB Large T A0204 527 VTMNEYPV 0.635 52 WB Large T A0204 579 LLIWFRPV 0.627 56 WB Large T A0204 60 KMEQDVKV 0.615 64 WB Large T A0204 287 FLLLGMYL 0.601 75 WB Large T A0204 569 ILQSGMTL 0.572 102 WB Large T A0204 501 YLDGSVKV 0.571 104 WB Large T A0204 557 SLQNSEFL 0.565 110 WB Large T A0204 563 FLLEKRIL 0.554 124 WB Large T A0204 293 YLEFQYNV 0.537 149 WB Large T A0204 215 KLCTFSFL 0.534 154 WB Large T A0204 11 ELMDLLGL 0.521 178 WB Large T A0204 469 YMVVFEDV 0.512 195 WB Large T A0204 464 VAIDQYMV 0.512 196 WB Large T A0204 536 KTLQARFV 0.494 239 WB Large T A0204 155 RTLACFAV 0.475 293 WB Large T A0204 398 LLPKMDSV 0.460 345 WB Large T A0204 465 AIDQYMVV 0.459 349 WB Large T A0204 457 RLTFELGV 0.448 393 WB Large T A0204 50 KMKRMNTL 0.443 412 WB Large T A0204 175 KLMEKYSV 0.879 3 SB Large T A0206 155 RTLACFAV 0.822 6 SB Large T A0206 272 KLITEYAV 0.820 6 SB Large T A0206 579 LLIWFRPV 0.813 7 SB Large T A0206 287 FLLLGMYL 0.784 10 SB Large T A0206 654 SQVSDTSA 0.782 10 SB Large T A0206 501 YLDGSVKV 0.771 11 SB Large T A0206 388 YMAGVAWL 0.737 17 SB Large T A0206 469 YMVVFEDV 0.730 18 SB Large T A0206 267 KQVSWKLI 0.720 20 SB Large T A0206 144 HQFLSQAV 0.705 24 SB Large T A0206 372 KMDLIFGA 0.695 27 SB Large T A0206 570 LQSGMTLL 0.694 27 SB Large T A0206 296 FQYNVEEC 0.688 29 SB Large T A0206 457 RLTFELGV 0.678 32 SB Large T A0206 398 LLPKMDSV 0.673 34 SB Large T A0206 558 LQNSEFLL 0.665 37 SB Large T A0206 338 CQQAVDTV 0.654 42 SB Large T A0206 322 FANAIIFA 0.648 45 SB Large T A0206 465 AIDQYMVV 0.646 45 SB Large T A0206 74 GTWNSSEV 0.645 46 SB Large T A0206 527 VTMNEYPV 0.615 64 WB Large T A0206 293 YLEFQYNV 0.613 65 WB Large T A0206 11 ELMDLLGL 0.594 80 WB Large T A0206 536 KTLQARFV 0.593 81 WB Large T A0206 464 VAIDQYMV 0.572 102 WB Large T A0206 21 AAWGNLPL 0.571 104 WB Large T A0206 383 AVLEQYMA 0.539 146 WB Large T A0206 563 FLLEKRIL 0.534 155 WB Large T A0206 574 MTLLLLLI 0.517 185 WB Large T A0206 215 KLCTFSFL 0.512 195 WB Large T A0206 184 FISRHMCA 0.511 197 WB Large T A0206 519 TQIFPPGL 0.505 210 WB Large T A0206 377 FGAHGNAV 0.470 308 WB Large T A0206 335 KSICQQAV 0.469 311 WB Large T A0206 369 ILDKMDLI 0.464 328 WB Large T A0206 520 QIFPPGLV 0.458 352 WB Large T A0206 391 GVAWLHCL 0.457 355 WB Large T A0206 231 YLLYSALT 0.451 380 WB Large T A0206 569 ILQSGMTL 0.445 406 WB Large T A0206 339 QQAVDTVL 0.443 414 WB Large T A0206 146 FLSQAVFS 0.438 436 WB Large T A0206 169 AQILYKKL 0.435 453 WB Large T A0206 60 KMEQDVKV 0.427 490 WB Large T A0206 501 YLDGSVKV 0.977 1 SB Large T A0211 388 YMAGVAWL 0.963 1 SB Large T A0211 175 KLMEKYSV 0.945 1 SB Large T A0211 287 FLLLGMYL 0.937 1 SB Large T A0211 579 LLIWFRPV 0.922 2 SB Large T A0211 465 AIDQYMVV 0.919 2 SB Large T A0211 272 KLITEYAV 0.906 2 SB Large T A0211 11 ELMDLLGL 0.904 2 SB Large T A0211 398 LLPKMDSV 0.900 2 SB Large T A0211 457 RLTFELGV 0.899 2 SB Large T A0211 293 YLEFQYNV 0.897 3 SB Large T A0211 557 SLQNSEFL 0.882 3 SB Large T A0211 569 ILQSGMTL 0.870 4 SB Large T A0211 469 YMVVFEDV 0.866 4 SB Large T A0211 563 FLLEKRIL 0.862 4 SB Large T A0211 603 RLDSEISM 0.848 5 SB Large T A0211 60 KMEQDVKV 0.845 5 SB Large T A0211 369 ILDKMDLI 0.828 6 SB Large T A0211 573 GMTLLLLL 0.824 6 SB Large T A0211 215 KLCTFSFL 0.821 6 SB Large T A0211 520 QIFPPGLV 0.811 7 SB Large T A0211 609 SMYTFSRM 0.780 10 SB Large T A0211 372 KMDLIFGA 0.777 11 SB Large T A0211 464 VAIDQYMV 0.743 16 SB Large T A0211 14 DLLGLERA 0.725 19 SB Large T A0211 74 GTWNSSEV 0.720 20 SB Large T A0211 391 GVAWLHCL 0.719 20 SB Large T A0211 485 DLPSGHGI 0.719 21 SB Large T A0211 155 RTLACFAV 0.693 27 SB Large T A0211 442 DLCGGKAL 0.686 29 SB Large T A0211 231 YLLYSALT 0.682 31 SB Large T A0211 536 KTLQARFV 0.668 36 SB Large T A0211 355 HMTREEML 0.667 36 SB Large T A0211 27 PLMRKAYL 0.666 37 SB Large T A0211 406 IFDFLHCV 0.646 46 SB Large T A0211 514 HLNKRTQI 0.642 48 SB Large T A0211 21 AAWGNLPL 0.638 50 WB Large T A0211 9 SMELMDLL 0.635 51 WB Large T A0211 56 TLYKKMEQ 0.625 57 WB Large T A0211 188 HMCAGHNI 0.618 62 WB Large T A0211 576 LLLLLIWF 0.614 64 WB Large T A0211 146 FLSQAVFS 0.597 78 WB Large T A0211 383 AVLEQYMA 0.594 81 WB Large T A0211 405 VIFDFLHC 0.587 87 WB Large T A0211 344 TVLAKKRV 0.583 91 WB Large T A0211 50 KMKRMNTL 0.582 92 WB Large T A0211 288 LLLGMYLE 0.577 96 WB Large T A0211 448 ALNVNLPM 0.573 100 WB Large T A0211 368 HILDKMDL 0.570 104 WB Large T A0211 527 VTMNEYPV 0.561 115 WB Large T A0211 150 AVFSNRTL 0.555 122 WB Large T A0211 184 FISRHMCA 0.545 137 WB Large T A0211 199 LTPHRHRV 0.543 140 WB Large T A0211 551 KIYLRKSL 0.523 173 WB Large T A0211 3 VLNREESM 0.494 239 WB Large T A0211 491 GINNLDSL 0.485 262 WB Large T A0211 291 GMYLEFQY 0.468 315 WB Large T A0211 350 RVDTLHMT 0.466 322 WB Large T A0211 142 DLHQFLSQ 0.459 348 WB Large T A0211 401 KMDSVIFD 0.458 350 WB Large T A0211 673 HLCKGFQC 0.458 350 WB Large T A0211 289 LLGMYLEF 0.450 383 WB Large T A0211 577 LLLLIWFR 0.450 384 WB Large T A0211 439 GLLDLCGG 0.448 390 WB Large T A0211 501 YLDGSVKV 0.940 1 SB Large T A0212 388 YMAGVAWL 0.924 2 SB Large T A0212 175 KLMEKYSV 0.912 2 SB Large T A0212 287 FLLLGMYL 0.903 2 SB Large T A0212 398 LLPKMDSV 0.879 3 SB Large T A0212 469 YMVVFEDV 0.878 3 SB Large T A0212 293 YLEFQYNV 0.872 4 SB Large T A0212 579 LLIWFRPV 0.853 4 SB Large T A0212 563 FLLEKRIL 0.852 4 SB Large T A0212 272 KLITEYAV 0.852 4 SB Large T A0212 465 AIDQYMVV 0.843 5 SB Large T A0212 11 ELMDLLGL 0.842 5 SB Large T A0212 569 ILQSGMTL 0.821 6 SB Large T A0212 457 RLTFELGV 0.787 10 SB Large T A0212 557 SLQNSEFL 0.757 13 SB Large T A0212 609 SMYTFSRM 0.711 22 SB Large T A0212 464 VAIDQYMV 0.698 26 SB Large T A0212 60 KMEQDVKV 0.666 37 SB Large T A0212 355 HMTREEML 0.663 38 SB Large T A0212 603 RLDSEISM 0.662 38 SB Large T A0212 368 HILDKMDL 0.659 39 SB Large T A0212 3 VLNREESM 0.639 49 SB Large T A0212 184 FISRHMCA 0.635 52 WB Large T A0212 405 VIFDFLHC 0.629 55 WB Large T A0212 215 KLCTFSFL 0.615 64 WB Large T A0212 369 ILDKMDLI 0.609 68 WB Large T A0212 27 PLMRKAYL 0.597 78 WB Large T A0212 372 KMDLIFGA 0.588 86 WB Large T A0212 50 KMKRMNTL 0.579 94 WB Large T A0212 520 QIFPPGLV 0.577 96 WB Large T A0212 573 GMTLLLLL 0.577 96 WB Large T A0212 527 VTMNEYPV 0.571 104 WB Large T A0212 188 HMCAGHNI 0.546 135 WB Large T A0212 14 DLLGLERA 0.523 174 WB Large T A0212 442 DLCGGKAL 0.521 178 WB Large T A0212 74 GTWNSSEV 0.521 178 WB Large T A0212 56 TLYKKMEQ 0.520 180 WB Large T A0212 485 DLPSGHGI 0.518 183 WB Large T A0212 21 AAWGNLPL 0.511 197 WB Large T A0212 391 GVAWLHCL 0.511 199 WB Large T A0212 231 YLLYSALT 0.504 213 WB Large T A0212 288 LLLGMYLE 0.486 259 WB Large T A0212 514 HLNKRTQI 0.480 276 WB Large T A0212 199 LTPHRHRV 0.477 285 WB Large T A0212 155 RTLACFAV 0.476 290 WB Large T A0212 377 FGAHGNAV 0.461 340 WB Large T A0212 146 FLSQAVFS 0.442 418 WB Large T A0212 9 SMELMDLL 0.426 495 WB Large T A0212 501 YLDGSVKV 0.928 2 SB Large T A0216 388 YMAGVAWL 0.917 2 SB Large T A0216 175 KLMEKYSV 0.905 2 SB Large T A0216 398 LLPKMDSV 0.895 3 SB Large T A0216 287 FLLLGMYL 0.891 3 SB Large T A0216 293 YLEFQYNV 0.849 5 SB Large T A0216 557 SLQNSEFL 0.846 5 SB Large T A0216 569 ILQSGMTL 0.836 5 SB Large T A0216 272 KLITEYAV 0.832 6 SB Large T A0216 465 AIDQYMVV 0.829 6 SB Large T A0216 27 PLMRKAYL 0.829 6 SB Large T A0216 579 LLIWFRPV 0.804 8 SB Large T A0216 215 KLCTFSFL 0.784 10 SB Large T A0216 11 ELMDLLGL 0.740 16 SB Large T A0216 74 GTWNSSEV 0.734 17 SB Large T A0216 60 KMEQDVKV 0.732 18 SB Large T A0216 457 RLTFELGV 0.727 19 SB Large T A0216 469 YMVVFEDV 0.718 21 SB Large T A0216 563 FLLEKRIL 0.709 23 SB Large T A0216 520 QIFPPGLV 0.701 25 SB Large T A0216 514 HLNKRTQI 0.689 29 SB Large T A0216 369 ILDKMDLI 0.673 34 SB Large T A0216 56 TLYKKMEQ 0.662 38 SB Large T A0216 50 KMKRMNTL 0.651 43 SB Large T A0216 609 SMYTFSRM 0.647 45 SB Large T A0216 603 RLDSEISM 0.626 56 WB Large T A0216 355 HMTREEML 0.623 58 WB Large T A0216 21 AAWGNLPL 0.600 75 WB Large T A0216 442 DLCGGKAL 0.597 78 WB Large T A0216 573 GMTLLLLL 0.595 79 WB Large T A0216 464 VAIDQYMV 0.593 82 WB Large T A0216 344 TVLAKKRV 0.583 91 WB Large T A0216 199 LTPHRHRV 0.568 106 WB Large T A0216 14 DLLGLERA 0.566 109 WB Large T A0216 485 DLPSGHGI 0.550 130 WB Large T A0216 536 KTLQARFV 0.548 132 WB Large T A0216 9 SMELMDLL 0.532 158 WB Large T A0216 391 GVAWLHCL 0.522 176 WB Large T A0216 150 AVFSNRTL 0.516 187 WB Large T A0216 188 HMCAGHNI 0.512 195 WB Large T A0216 527 VTMNEYPV 0.506 210 WB Large T A0216 146 FLSQAVFS 0.504 213 WB Large T A0216 231 YLLYSALT 0.501 220 WB Large T A0216 491 GINNLDSL 0.476 290 WB Large T A0216 184 FISRHMCA 0.474 296 WB Large T A0216 551 KIYLRKSL 0.468 315 WB Large T A0216 155 RTLACFAV 0.465 327 WB Large T A0216 673 HLCKGFQC 0.463 334 WB Large T A0216 448 ALNVNLPM 0.442 418 WB Large T A0216 372 KMDLIFGA 0.442 419 WB Large T A0216 406 IFDFLHCV 0.433 460 WB Large T A0216 3 VLNREESM 0.429 482 WB Large T A0216 501 YLDGSVKV 0.939 1 SB Large T A0219 388 YMAGVAWL 0.930 2 SB Large T A0219 287 FLLLGMYL 0.835 5 SB Large T A0219 11 ELMDLLGL 0.807 8 SB Large T A0219 175 KLMEKYSV 0.800 8 SB Large T A0219 569 ILQSGMTL 0.780 10 SB Large T A0219 398 LLPKMDSV 0.713 22 SB Large T A0219 293 YLEFQYNV 0.711 22 SB Large T A0219 557 SLQNSEFL 0.660 39 SB Large T A0219 465 AIDQYMVV 0.659 39 SB Large T A0219 272 KLITEYAV 0.651 43 SB Large T A0219 21 AAWGNLPL 0.637 51 WB Large T A0219 457 RLTFELGV 0.599 76 WB Large T A0219 27 PLMRKAYL 0.589 85 WB Large T A0219 603 RLDSEISM 0.574 100 WB Large T A0219 369 ILDKMDLI 0.567 108 WB Large T A0219 469 YMVVFEDV 0.565 111 WB Large T A0219 579 LLIWFRPV 0.564 112 WB Large T A0219 563 FLLEKRIL 0.555 123 WB Large T A0219 485 DLPSGHGI 0.542 142 WB Large T A0219 74 GTWNSSEV 0.540 145 WB Large T A0219 464 VAIDQYMV 0.507 208 WB Large T A0219 355 HMTREEML 0.497 230 WB Large T A0219 372 KMDLIFGA 0.431 469 WB Large T A0219 406 IFDFLHCV 0.429 482 WB Large T A0219 573 GMTLLLLL 0.426 497 WB Large T A0219 53 RMNTLYKK 0.719 20 SB Large T A0301 232 LLYSALTR 0.673 34 SB Large T A0301 28 LMRKAYLK 0.671 35 SB Large T A0301 394 WLHCLLPK 0.536 150 WB Large T A0301 208 AINNFCQK 0.529 162 WB Large T A0301 161 AVYTTKEK 0.526 169 WB Large T A0301 577 LLLLIWFR 0.513 193 WB Large T A0301 365 RFNHILDK 0.512 196 WB Large T A0301 291 GMYLEFQY 0.507 207 WB Large T A0301 31 KAYLKKCK 0.506 210 WB Large T A0301 608 ISMYTFSR 0.489 252 WB Large T A0301 413 VVFNVPKR 0.483 270 WB Large T A0301 121 SQHSTPPK 0.481 274 WB Large T A0301 156 TLACFAVY 0.475 294 WB Large T A0301 222 LICKGVNK 0.438 435 WB Large T A0301 195 IIFFLTPH 0.434 456 WB Large T A0301 412 CVVFNVPK 0.428 486 WB Large T A0301 208 AINNFCQK 0.764 12 SB Large T A1101 161 AVYTTKEK 0.761 13 SB Large T A1101 121 SQHSTPPK 0.746 15 SB Large T A1101 325 AIIFAESK 0.737 17 SB Large T A1101 341 AVDTVLAK 0.732 18 SB Large T A1101 53 RMNTLYKK 0.727 19 SB Large T A1101 608 ISMYTFSR 0.721 20 SB Large T A1101 544 RQIDFRPK 0.709 23 SB Large T A1101 505 SVKVNLEK 0.695 27 SB Large T A1101 168 KAQILYKK 0.672 34 SB Large T A1101 412 CVVFNVPK 0.665 37 SB Large T A1101 669 SQELHLCK 0.657 40 SB Large T A1101 31 KAYLKKCK 0.639 49 SB Large T A1101 218 TFSFLICK 0.626 57 WB Large T A1101 413 VVFNVPKR 0.613 65 WB Large T A1101 537 TLQARFVR 0.609 68 WB Large T A1101 470 MVVFEDVK 0.604 72 WB Large T A1101 404 SVIFDFLH 0.596 79 WB Large T A1101 222 LICKGVNK 0.581 93 WB Large T A1101 560 NSEFLLEK 0.574 100 WB Large T A1101 611 YTFSRMKY 0.568 107 WB Large T A1101 148 SQAVFSNR 0.553 125 WB Large T A1101 450 NVNLPMER 0.526 168 WB Large T A1101 394 WLHCLLPK 0.499 226 WB Large T A1101 291 GMYLEFQY 0.497 231 WB Large T A1101 617 KYNICMGK 0.464 328 WB Large T A1101 247 ESIQGGLK 0.464 331 WB Large T A1101 577 LLLLIWFR 0.462 338 WB Large T A1101 52 KRMNTLYK 0.454 367 WB Large T A1101 678 FQCFKRPK 0.440 426 WB Large T A1101 28 LMRKAYLK 0.435 452 WB Large T A1101 365 RFNHILDK 0.427 494 WB Large T A1101 408 DFLHCVVF 0.671 35 SB Large T A2301 541 RFVRQIDF 0.664 37 SB Large T A2301 610 MYTFSRMK 0.660 39 SB Large T A2301 321 HFANAIIF 0.633 53 WB Large T A2301 172 LYKKLMEK 0.626 57 WB Large T A2301 104 LFCHEDMF 0.617 63 WB Large T A2301 500 DYLDGSVK 0.609 68 WB Large T A2301 582 WFRPVADF 0.608 69 WB Large T A2301 230 EYLLYSAL 0.601 75 WB Large T A2301 617 KYNICMGK 0.599 76 WB Large T A2301 205 RVSAINNF 0.504 214 WB Large T A2301 387 QYMAGVAW 0.502 219 WB Large T A2301 576 LLLLLIWF 0.493 241 WB Large T A2301 92 WWSSFNEK 0.492 243 WB Large T A2301 145 QFLSQAVF 0.489 252 WB Large T A2301 365 RFNHILDK 0.475 292 WB Large T A2301 556 KSLQNSEF 0.460 343 WB Large T A2301 159 CFAVYTTK 0.441 423 WB Large T A2301 230 EYLLYSAL 0.680 32 SB Large T A2402 145 QFLSQAVF 0.522 176 WB Large T A2402 408 DFLHCVVF 0.519 182 WB Large T A2402 531 EYPVPKTL 0.510 199 WB Large T A2402 321 HFANAIIF 0.507 206 WB Large T A2402 422 YWLFKGPI 0.506 210 WB Large T A2402 541 RFVRQIDF 0.460 344 WB Large T A2402 387 QYMAGVAW 0.445 405 WB Large T A2402 387 QYMAGVAW 0.768 12 SB Large T A2403 582 WFRPVADF 0.765 12 SB Large T A2403 145 QFLSQAVF 0.713 22 SB Large T A2403 541 RFVRQIDF 0.706 24 SB Large T A2403 321 HFANAIIF 0.691 28 SB Large T A2403 230 EYLLYSAL 0.591 83 WB Large T A2403 408 DFLHCVVF 0.567 108 WB Large T A2403 556 KSLQNSEF 0.546 135 WB Large T A2403 104 LFCHEDMF 0.497 230 WB Large T A2403 531 EYPVPKTL 0.496 233 WB Large T A2403 611 YTFSRMKY 0.680 31 SB Large T A2601 285 DVFLLLGM 0.588 86 WB Large T A2601 11 ELMDLLGL 0.486 259 WB Large T A2601 611 YTFSRMKY 0.903 2 SB Large T A2602 285 DVFLLLGM 0.810 7 SB Large T A2602 280 ETKCEDVF 0.737 17 SB Large T A2602 66 KVAHQPDF 0.563 112 WB Large T A2602 11 ELMDLLGL 0.500 224 WB Large T A2602 463 GVAIDQYM 0.486 261 WB Large T A2602 80 EVPTYGTE 0.485 262 WB Large T A2602 291 GMYLEFQY 0.680 31 SB Large T A2902 286 VFLLLGMY 0.624 58 WB Large T A2902 611 YTFSRMKY 0.617 63 WB Large T A2902 156 TLACFAVY 0.552 127 WB Large T A2902 270 SWKLITEY 0.500 223 WB Large T A2902 121 SQHSTPPK 0.836 5 SB Large T A3001 419 KRRYWLFK 0.811 7 SB Large T A3001 28 LMRKAYLK 0.805 8 SB Large T A3001 544 RQIDFRPK 0.771 11 SB Large T A3001 683 RPKTPPPK 0.740 16 SB Large T A3001 505 SVKVNLEK 0.732 18 SB Large T A3001 53 RMNTLYKK 0.672 34 SB Large T A3001 394 WLHCLLPK 0.669 36 SB Large T A3001 309 KDQPYHFK 0.647 45 SB Large T A3001 31 KAYLKKCK 0.628 55 WB Large T A3001 52 KRMNTLYK 0.620 60 WB Large T A3001 161 AVYTTKEK 0.613 65 WB Large T A3001 29 MRKAYLKK 0.612 66 WB Large T A3001 594 QSRIVEWK 0.594 80 WB Large T A3001 168 KAQILYKK 0.583 91 WB Large T A3001 549 RPKIYLRK 0.571 103 WB Large T A3001 172 LYKKLMEK 0.566 109 WB Large T A3001 130 KRKVEDPK 0.560 116 WB Large T A3001 617 KYNICMGK 0.549 131 WB Large T A3001 610 MYTFSRMK 0.541 142 WB Large T A3001 365 RFNHILDK 0.516 188 WB Large T A3001 196 IFFLTPHR 0.458 350 WB Large T A3001 208 AINNFCQK 0.450 382 WB Large T A3001 237 LTRDPYHI 0.443 416 WB Large T A3001 205 RVSAINNF 0.506 210 WB Large T A3002 611 YTFSRMKY 0.440 428 WB Large T A3002 577 LLLLIWFR 0.818 7 SB Large T A3101 53 RMNTLYKK 0.816 7 SB Large T A3101 608 ISMYTFSR 0.791 9 SB Large T A3101 537 TLQARFVR 0.773 11 SB Large T A3101 196 IFFLTPHR 0.772 11 SB Large T A3101 414 VFNVPKRR 0.682 31 SB Large T A3101 148 SQAVFSNR 0.678 32 SB Large T A3101 180 YSVTFISR 0.672 34 SB Large T A3101 676 KGFQCFKR 0.671 35 SB Large T A3101 413 VVFNVPKR 0.665 37 SB Large T A3101 617 KYNICMGK 0.648 45 SB Large T A3101 28 LMRKAYLK 0.646 46 SB Large T A3101 544 RQIDFRPK 0.646 46 SB Large T A3101 232 LLYSALTR 0.630 55 WB Large T A3101 168 KAQILYKK 0.618 62 WB Large T A3101 542 FVRQIDFR 0.590 84 WB Large T A3101 589 FSKDIQSR 0.590 84 WB Large T A3101 596 RIVEWKER 0.580 93 WB Large T A3101 198 FLTPHRHR 0.569 106 WB Large T A3101 172 LYKKLMEK 0.550 129 WB Large T A3101 365 RFNHILDK 0.540 145 WB Large T A3101 610 MYTFSRMK 0.532 157 WB Large T A3101 450 NVNLPMER 0.515 189 WB Large T A3101 31 KAYLKKCK 0.504 214 WB Large T A3101 208 AINNFCQK 0.461 339 WB Large T A3101 155 RTLACFAV 0.460 345 WB Large T A3101 121 SQHSTPPK 0.452 376 WB Large T A3101 577 LLLLIWFR 0.795 9 SB Large T A3301 196 IFFLTPHR 0.758 13 SB Large T A3301 608 ISMYTFSR 0.631 54 WB Large T A3301 450 NVNLPMER 0.631 54 WB Large T A3301 542 FVRQIDFR 0.628 55 WB Large T A3301 537 TLQARFVR 0.608 69 WB Large T A3301 343 DTVLAKKR 0.575 99 WB Large T A3301 180 YSVTFISR 0.574 100 WB Large T A3301 589 FSKDIQSR 0.535 152 WB Large T A3301 547 DFRPKIYL 0.526 169 WB Large T A3301 500 DYLDGSVK 0.521 178 WB Large T A3301 198 FLTPHRHR 0.504 215 WB Large T A3301 265 ETKQVSWK 0.447 397 WB Large T A3301 265 ETKQVSWK 0.836 5 SB Large T A6801 608 ISMYTFSR 0.827 6 SB Large T A6801 470 MVVFEDVK 0.812 7 SB Large T A6801 180 YSVTFISR 0.805 8 SB Large T A6801 343 DTVLAKKR 0.798 8 SB Large T A6801 412 CVVFNVPK 0.772 11 SB Large T A6801 450 NVNLPMER 0.771 11 SB Large T A6801 542 FVRQIDFR 0.764 12 SB Large T A6801 611 YTFSRMKY 0.753 14 SB Large T A6801 610 MYTFSRMK 0.746 15 SB Large T A6801 413 VVFNVPKR 0.728 19 SB Large T A6801 247 ESIQGGLK 0.662 38 SB Large T A6801 232 LLYSALTR 0.652 43 SB Large T A6801 589 FSKDIQSR 0.648 44 SB Large T A6801 537 TLQARFVR 0.632 53 WB Large T A6801 196 IFFLTPHR 0.626 57 WB Large T A6801 577 LLLLIWFR 0.606 71 WB Large T A6801 218 TFSFLICK 0.597 78 WB Large T A6801 560 NSEFLLEK 0.575 99 WB Large T A6801 325 AIIFAESK 0.570 105 WB Large T A6801 198 FLTPHRHR 0.567 108 WB Large T A6801 505 SVKVNLEK 0.553 126 WB Large T A6801 167 EKAQILYK 0.548 132 WB Large T A6801 148 SQAVFSNR 0.536 151 WB Large T A6801 159 CFAVYTTK 0.531 159 WB Large T A6801 161 AVYTTKEK 0.529 163 WB Large T A6801 208 AINNFCQK 0.516 188 WB Large T A6801 328 FAESKNQK 0.505 212 WB Large T A6801 596 RIVEWKER 0.471 306 WB Large T A6801 492 INNLDSLR 0.464 329 WB Large T A6801 156 TLACFAVY 0.458 351 WB Large T A6801 124 STPPKKKR 0.453 371 WB Large T A6801 275 TEYAVETK 0.432 465 WB Large T A6801 123 HSTPPKKK 0.429 482 WB Large T A6801 404 SVIFDFLH 0.427 492 WB Large T A6801 313 YHFKYHEK 0.426 496 WB Large T A6801 322 FANAIIFA 0.703 24 SB Large T A6802 520 QIFPPGLV 0.669 35 SB Large T A6802 155 RTLACFAV 0.653 42 SB Large T A6802 377 FGAHGNAV 0.634 52 WB Large T A6802 527 VTMNEYPV 0.617 63 WB Large T A6802 403 DSVIFDFL 0.603 73 WB Large T A6802 11 ELMDLLGL 0.583 90 WB Large T A6802 189 MCAGHNII 0.575 99 WB Large T A6802 8 ESMELMDL 0.563 113 WB Large T A6802 199 LTPHRHRV 0.555 123 WB Large T A6802 178 EKYSVTFI 0.531 160 WB Large T A6802 388 YMAGVAWL 0.523 174 WB Large T A6802 574 MTLLLLLI 0.480 278 WB Large T A6802 464 VAIDQYMV 0.479 281 WB Large T A6802 579 LLIWFRPV 0.477 286 WB Large T A6802 649 QSQCSSQV 0.455 365 WB Large T A6802 19 ERAAWGNL 0.434 456 WB Large T A6802 434 TTLAAGLL 0.431 470 WB Large T A6802 216 LCTFSFLI 0.428 489 WB Large T A6802 520 QIFPPGLV 0.711 22 SB Large T A6901 11 ELMDLLGL 0.667 36 SB Large T A6901 155 RTLACFAV 0.636 51 WB Large T A6901 574 MTLLLLLI 0.613 66 WB Large T A6901 527 VTMNEYPV 0.575 99 WB Large T A6901 434 TTLAAGLL 0.571 103 WB Large T A6901 501 YLDGSVKV 0.546 135 WB Large T A6901 74 GTWNSSEV 0.545 137 WB Large T A6901 464 VAIDQYMV 0.523 175 WB Large T A6901 322 FANAIIFA 0.514 192 WB Large T A6901 21 AAWGNLPL 0.513 193 WB Large T A6901 579 LLIWFRPV 0.508 205 WB Large T A6901 287 FLLLGMYL 0.504 214 WB Large T A6901 388 YMAGVAWL 0.494 238 WB Large T A6901 340 QAVDTVLA 0.464 328 WB Large T A6901 8 ESMELMDL 0.453 372 WB Large T A6901 458 LTFELGVA 0.433 462 WB Large T A6901 377 FGAHGNAV 0.431 472 WB Large T A6901 383 AVLEQYMA 0.426 499 WB Large T A6901 453 LPMERLTF 0.735 17 SB Large T B0702 417 VPKRRYWL 0.608 69 WB Large T B0702 399 LPKMDSVI 0.500 223 WB Large T B0702 21 AAWGNLPL 0.482 270 WB Large T B0702 139 FPSDLHQF 0.479 281 WB Large T B0702 26 LPLMRKAY 0.431 472 WB Large T B0702 417 VPKRRYWL 0.555 123 WB Large T B0801 50 KMKRMNTL 0.479 282 WB Large T B0801 33 YLKKCKEF 0.446 401 WB Large T B0801 205 RVSAINNF 0.544 139 WB Large T B1501 306 CQKKDQPY 0.511 199 WB Large T B1501 339 QQAVDTVL 0.504 214 WB Large T B1501 615 RMKYNICM 0.498 228 WB Large T B1501 33 YLKKCKEF 0.496 232 WB Large T B1501 388 YMAGVAWL 0.493 240 WB Large T B1501 611 YTFSRMKY 0.492 244 WB Large T B1501 291 GMYLEFQY 0.486 261 WB Large T B1501 144 HQFLSQAV 0.476 288 WB Large T B1501 50 KMKRMNTL 0.474 294 WB Large T B1501 156 TLACFAVY 0.469 311 WB Large T B1501 570 LQSGMTLL 0.441 424 WB Large T B1501 89 WESWWSSF 0.814 7 SB Large T B1801 455 MERLTFEL 0.686 29 SB Large T B1801 606 SEISMYTF 0.646 45 SB Large T B1801 177 MEKYSVTF 0.627 56 WB Large T B1801 363 TERFNHIL 0.449 388 WB Large T B1801 86 TEEWESWW 0.434 458 WB Large T B1801 52 KRMNTLYK 0.623 58 WB Large T B2705 567 KRILQSGM 0.555 122 WB Large T B2705 544 RQIDFRPK 0.533 155 WB Large T B2705 419 KRRYWLFK 0.506 209 WB Large T B2705 349 KRVDTLHM 0.461 341 WB Large T B2705 29 MRKAYLKK 0.430 477 WB Large T B2705 139 FPSDLHQF 0.796 9 SB Large T B3501 522 FPPGLVTM 0.773 11 SB Large T B3501 453 LPMERLTF 0.752 14 SB Large T B3501 26 LPLMRKAY 0.749 15 SB Large T B3501 235 SALTRDPY 0.599 76 WB Large T B3501 382 NAVLEQYM 0.558 119 WB Large T B3501 111 FASDEEAT 0.538 148 WB Large T B3501 156 TLACFAVY 0.533 156 WB Large T B3501 321 HFANAIIF 0.513 193 WB Large T B3501 21 AAWGNLPL 0.509 203 WB Large T B3501 77 NSSEVPTY 0.502 218 WB Large T B3501 98 EKWDEDLF 0.451 381 WB Large T B3501 145 QFLSQAVF 0.450 384 WB Large T B3501 89 WESWWSSF 0.445 407 WB Large T B3501 5 NREESMEL 0.555 123 WB Large T B3901 339 QQAVDTVL 0.464 330 WB Large T B3901 388 YMAGVAWL 0.429 483 WB Large T B3901 455 MERLTFEL 0.676 33 SB Large T B4001 363 TERFNHIL 0.626 57 WB Large T B4001 283 CEDVFLLL 0.595 80 WB Large T B4001 606 SEISMYTF 0.593 81 WB Large T B4001 6 REESMELM 0.511 197 WB Large T B4001 177 MEKYSVTF 0.487 257 WB Large T B4001 246 EESIQGGL 0.432 465 WB Large T B4001 606 SEISMYTF 0.568 107 WB Large T B4002 89 WESWWSSF 0.495 237 WB Large T B4002 166 KEKAQILY 0.489 250 WB Large T B4002 359 EEMLTERF 0.489 251 WB Large T B4002 246 EESIQGGL 0.464 328 WB Large T B4002 177 MEKYSVTF 0.454 367 WB Large T B4002 264 EETKQVSW 0.446 403 WB Large T B4002 6 REESMELM 0.433 463 WB Large T B4002 264 EETKQVSW 0.514 193 WB Large T B4402 606 SEISMYTF 0.472 303 WB Large T B4402 86 TEEWESWW 0.464 329 WB Large T B4402 166 KEKAQILY 0.461 342 WB Large T B4402 359 EEMLTERF 0.449 388 WB Large T B4402 606 SEISMYTF 0.549 131 WB Large T B4403 359 EEMLTERF 0.526 167 WB Large T B4403 359 EEMLTERF 0.512 196 WB Large T B4501 329 AESKNQKS 0.443 415 WB Large T B4501 246 EESIQGGL 0.433 460 WB Large T B4501 481 AESKDLPS 0.431 470 WB Large T B4501 522 FPPGLVTM 0.629 55 WB Large T B5101 453 LPMERLTF 0.621 60 WB Large T B5101 399 LPKMDSVI 0.598 77 WB Large T B5101 453 LPMERLTF 0.755 14 SB Large T B5301 139 FPSDLHQF 0.729 18 SB Large T B5301 26 LPLMRKAY 0.636 51 WB Large T B5301 399 LPKMDSVI 0.632 53 WB Large T B5301 522 FPPGLVTM 0.582 91 WB Large T B5301 522 FPPGLVTM 0.577 97 WB Large T B5401 322 FANAIIFA 0.511 198 WB Large T B5401 26 LPLMRKAY 0.482 271 WB Large T B5401 82 PTYGTEEW 0.517 186 WB Large T B5701 93 WSSFNEKW 0.678 32 SB Large T B5801 556 KSLQNSEF 0.602 74 WB Large T B5801 593 IQSRIVEW 0.573 101 WB Large T B5801 205 RVSAINNF 0.525 169 WB Large T B5801 82 PTYGTEEW 0.504 215 WB Large T B5801 66 KVAHQPDF 0.491 246 WB Large T B5801 16 LGLERAAW 0.439 430 WB Large T B5801 77 NSSEVPTY 0.431 469 WB Large T B5801 9-mers 603 RLDSEISMY 0.648 44 SB Large T A0101 226 GVNKEYLLY 0.477 286 WB Large T A0101 234 YSALTRDPY 0.471 304 WB Large T A0101 409 FLHCVVFNV 0.891 3 SB Large T A0201 405 VIFDFLHCV 0.842 5 SB Large T A0201 215 KLCTFSFLI 0.747 15 SB Large T A0201 198 FLTPHRHRV 0.693 27 SB Large T A0201 578 LLLIWFRPV 0.690 28 SB Large T A0201 384 VLEQYMAGV 0.680 31 SB Large T A0201 557 SLQNSEFLL 0.658 40 SB Large T A0201 397 CLLPKMDSV 0.639 49 SB Large T A0201 569 ILQSGMTLL 0.614 64 WB Large T A0201 175 KLMEKYSVT 0.580 94 WB Large T A0201 435 TLAAGLLDL 0.578 95 WB Large T A0201 361 MLTERFNHI 0.562 114 WB Large T A0201 579 LLIWFRPVA 0.505 212 WB Large T A0201 573 GMTLLLLLI 0.494 237 WB Large T A0201 368 HILDKMDLI 0.488 254 WB Large T A0201 621 CMGKCILDI 0.465 327 WB Large T A0201 394 WLHCLLPKM 0.443 412 WB Large T A0201 156 TLACFAVYT 0.437 440 WB Large T A0201 409 FLHCVVFNV 0.885 3 SB Large T A0202 198 FLTPHRHRV 0.824 6 SB Large T A0202 361 MLTERFNHI 0.774 11 SB Large T A0202 569 ILQSGMTLL 0.765 12 SB Large T A0202 405 VIFDFLHCV 0.742 16 SB Large T A0202 384 VLEQYMAGV 0.728 19 SB Large T A0202 494 NLDSLRDYL 0.687 29 SB Large T A0202 557 SLQNSEFLL 0.676 33 SB Large T A0202 570 LQSGMTLLL 0.676 33 SB Large T A0202 397 CLLPKMDSV 0.658 40 SB Large T A0202 402 MDSVIFDFL 0.642 48 SB Large T A0202 215 KLCTFSFLI 0.640 49 SB Large T A0202 497 SLRDYLDGS 0.630 54 WB Large T A0202 463 GVAIDQYMV 0.614 65 WB Large T A0202 435 TLAAGLLDL 0.605 71 WB Large T A0202 175 KLMEKYSVT 0.560 116 WB Large T A0202 573 GMTLLLLLI 0.558 119 WB Large T A0202 156 TLACFAVYT 0.554 124 WB Large T A0202 289 LLGMYLEFQ 0.542 142 WB Large T A0202 648 SQSQCSSQV 0.542 142 WB Large T A0202 391 GVAWLHCLL 0.529 163 WB Large T A0202 219 FSFLICKGV 0.528 165 WB Large T A0202 208 AINNFCQKL 0.524 173 WB Large T A0202 191 AGHNIIFFL 0.514 191 WB Large T A0202 111 FASDEEATA 0.506 208 WB Large T A0202 139 FPSDLHQFL 0.505 211 WB Large T A0202 236 ALTRDPYHI 0.501 220 WB Large T A0202 589 FSKDIQSRI 0.499 226 WB Large T A0202 526 LVTMNEYPV 0.493 240 WB Large T A0202 146 FLSQAVFSN 0.480 278 WB Large T A0202 578 LLLIWFRPV 0.466 321 WB Large T A0202 377 FGAHGNAVL 0.465 327 WB Large T A0202 458 LTFELGVAI 0.452 376 WB Large T A0202 572 SGMTLLLLL 0.450 385 WB Large T A0202 398 LLPKMDSVI 0.448 392 WB Large T A0202 368 HILDKMDLI 0.438 438 WB Large T A0202 409 FLHCVVFNV 0.911 2 SB Large T A0203 198 FLTPHRHRV 0.891 3 SB Large T A0203 361 MLTERFNHI 0.884 3 SB Large T A0203 384 VLEQYMAGV 0.838 5 SB Large T A0203 578 LLLIWFRPV 0.819 7 SB Large T A0203 397 CLLPKMDSV 0.815 7 SB Large T A0203 569 ILQSGMTLL 0.803 8 SB Large T A0203 405 VIFDFLHCV 0.796 9 SB Large T A0203 435 TLAAGLLDL 0.744 16 SB Large T A0203 175 KLMEKYSVT 0.694 27 SB Large T A0203 457 RLTFELGVA 0.683 30 SB Large T A0203 497 SLRDYLDGS 0.596 79 WB Large T A0203 579 LLIWFRPVA 0.575 99 WB Large T A0203 553 YLRKSLQNS 0.569 105 WB Large T A0203 215 KLCTFSFLI 0.566 108 WB Large T A0203 236 ALTRDPYHI 0.540 144 WB Large T A0203 375 LIFGAHGNA 0.540 145 WB Large T A0203 573 GMTLLLLLI 0.537 150 WB Large T A0203 570 LQSGMTLLL 0.528 165 WB Large T A0203 156 TLACFAVYT 0.527 166 WB Large T A0203 648 SQSQCSSQV 0.520 179 WB Large T A0203 391 GVAWLHCLL 0.517 185 WB Large T A0203 398 LLPKMDSVI 0.516 188 WB Large T A0203 394 WLHCLLPKM 0.513 194 WB Large T A0203 464 VAIDQYMVV 0.512 195 WB Large T A0203 188 HMCAGHNII 0.510 199 WB Large T A0203 519 TQIFPPGLV 0.506 210 WB Large T A0203 208 AINNFCQKL 0.501 220 WB Large T A0203 368 HILDKMDLI 0.496 232 WB Large T A0203 20 RAAWGNLPL 0.491 246 WB Large T A0203 53 RMNTLYKKM 0.490 249 WB Large T A0203 568 RILQSGMTL 0.485 263 WB Large T A0203 538 LQARFVRQI 0.458 352 WB Large T A0203 289 LLGMYLEFQ 0.456 360 WB Large T A0203 557 SLQNSEFLL 0.447 396 WB Large T A0203 596 RIVEWKERL 0.441 423 WB Large T A0203 463 GVAIDQYMV 0.432 464 WB Large T A0203 198 FLTPHRHRV 0.766 12 SB Large T A0204 409 FLHCVVFNV 0.744 15 SB Large T A0204 405 VIFDFLHCV 0.645 46 SB Large T A0204 578 LLLIWFRPV 0.640 48 SB Large T A0204 384 VLEQYMAGV 0.607 70 WB Large T A0204 464 VAIDQYMVV 0.564 111 WB Large T A0204 557 SLQNSEFLL 0.552 127 WB Large T A0204 59 KKMEQDVKV 0.514 191 WB Large T A0204 526 LVTMNEYPV 0.512 196 WB Large T A0204 435 TLAAGLLDL 0.489 251 WB Large T A0204 292 MYLEFQYNV 0.488 255 WB Large T A0204 569 ILQSGMTLL 0.485 264 WB Large T A0204 208 AINNFCQKL 0.474 296 WB Large T A0204 397 CLLPKMDSV 0.468 315 WB Large T A0204 175 KLMEKYSVT 0.464 329 WB Large T A0204 361 MLTERFNHI 0.447 395 WB Large T A0204 236 ALTRDPYHI 0.447 398 WB Large T A0204 215 KLCTFSFLI 0.445 404 WB Large T A0204 361 MLTERFNHI 0.848 5 SB Large T A0206 397 CLLPKMDSV 0.834 6 SB Large T A0206 409 FLHCVVFNV 0.819 7 SB Large T A0206 578 LLLIWFRPV 0.801 8 SB Large T A0206 198 FLTPHRHRV 0.793 9 SB Large T A0206 405 VIFDFLHCV 0.746 15 SB Large T A0206 544 RQIDFRPKI 0.739 16 SB Large T A0206 648 SQSQCSSQV 0.729 18 SB Large T A0206 384 VLEQYMAGV 0.692 27 SB Large T A0206 570 LQSGMTLLL 0.683 30 SB Large T A0206 596 RIVEWKERL 0.674 34 SB Large T A0206 568 RILQSGMTL 0.638 50 WB Large T A0206 20 RAAWGNLPL 0.634 52 WB Large T A0206 435 TLAAGLLDL 0.583 91 WB Large T A0206 215 KLCTFSFLI 0.560 116 WB Large T A0206 464 VAIDQYMVV 0.560 117 WB Large T A0206 368 HILDKMDLI 0.550 130 WB Large T A0206 339 QQAVDTVLA 0.549 131 WB Large T A0206 569 ILQSGMTLL 0.520 180 WB Large T A0206 111 FASDEEATA 0.520 180 WB Large T A0206 267 KQVSWKLIT 0.516 188 WB Large T A0206 579 LLIWFRPVA 0.507 206 WB Large T A0206 458 LTFELGVAI 0.503 216 WB Large T A0206 10 MELMDLLGL 0.496 233 WB Large T A0206 391 GVAWLHCLL 0.476 291 WB Large T A0206 287 FLLLGMYLE 0.473 298 WB Large T A0206 519 TQIFPPGLV 0.470 308 WB Large T A0206 288 LLLGMYLEF 0.469 312 WB Large T A0206 447 KALNVNLPM 0.457 357 WB Large T A0206 21 AAWGNLPLM 0.457 357 WB Large T A0206 394 WLHCLLPKM 0.451 379 WB Large T A0206 526 LVTMNEYPV 0.441 421 WB Large T A0206 175 KLMEKYSVT 0.439 432 WB Large T A0206 148 SQAVFSNRT 0.438 437 WB Large T A0206 198 FLTPHRHRV 0.978 1 SB Large T A0211 405 VIFDFLHCV 0.968 1 SB Large T A0211 409 FLHCVVFNV 0.933 2 SB Large T A0211 397 CLLPKMDSV 0.929 2 SB Large T A0211 384 VLEQYMAGV 0.926 2 SB Large T A0211 557 SLQNSEFLL 0.912 2 SB Large T A0211 494 NLDSLRDYL 0.903 2 SB Large T A0211 569 ILQSGMTLL 0.890 3 SB Large T A0211 435 TLAAGLLDL 0.890 3 SB Large T A0211 215 KLCTFSFLI 0.876 3 SB Large T A0211 578 LLLIWFRPV 0.862 4 SB Large T A0211 563 FLLEKRILQ 0.862 4 SB Large T A0211 579 LLIWFRPVA 0.849 5 SB Large T A0211 292 MYLEFQYNV 0.832 6 SB Large T A0211 388 YMAGVAWLH 0.799 8 SB Large T A0211 463 GVAIDQYMV 0.796 9 SB Large T A0211 428 PIDSGKTTL 0.778 11 SB Large T A0211 573 GMTLLLLLI 0.771 11 SB Large T A0211 500 DYLDGSVKV 0.751 14 SB Large T A0211 454 PMERLTFEL 0.736 17 SB Large T A0211 288 LLLGMYLEF 0.733 17 SB Large T A0211 526 LVTMNEYPV 0.733 18 SB Large T A0211 391 GVAWLHCLL 0.725 19 SB Large T A0211 464 VAIDQYMVV 0.721 20 SB Large T A0211 568 RILQSGMTL 0.720 20 SB Large T A0211 142 DLHQFLSQA 0.703 24 SB Large T A0211 361 MLTERFNHI 0.692 28 SB Large T A0211 236 ALTRDPYHI 0.685 30 SB Large T A0211 596 RIVEWKERL 0.685 30 SB Large T A0211 156 TLACFAVYT 0.663 38 SB Large T A0211 287 FLLLGMYLE 0.659 40 SB Large T A0211 208 AINNFCQKL 0.637 50 WB Large T A0211 575 TLLLLLIWF 0.632 53 WB Large T A0211 20 RAAWGNLPL 0.620 61 WB Large T A0211 14 DLLGLERAA 0.614 65 WB Large T A0211 289 LLGMYLEFQ 0.602 74 WB Large T A0211 603 RLDSEISMY 0.592 82 WB Large T A0211 368 HILDKMDLI 0.590 84 WB Large T A0211 576 LLLLLIWFR 0.575 99 WB Large T A0211 394 WLHCLLPKM 0.569 106 WB Large T A0211 353 TLHMTREEM 0.558 119 WB Large T A0211 273 LITEYAVET 0.545 137 WB Large T A0211 398 LLPKMDSVI 0.535 152 WB Large T A0211 401 KMDSVIFDF 0.531 160 WB Large T A0211 146 FLSQAVFSN 0.527 166 WB Large T A0211 188 HMCAGHNII 0.524 172 WB Large T A0211 406 IFDFLHCVV 0.519 181 WB Large T A0211 648 SQSQCSSQV 0.514 191 WB Large T A0211 458 LTFELGVAI 0.508 204 WB Large T A0211 497 SLRDYLDGS 0.503 216 WB Large T A0211 501 YLDGSVKVN 0.501 220 WB Large T A0211 171 ILYKKLMEK 0.485 264 WB Large T A0211 73 FGTWNSSEV 0.481 274 WB Large T A0211 609 SMYTFSRMK 0.474 295 WB Large T A0211 416 NVPKRRYWL 0.464 330 WB Large T A0211 109 DMFASDEEA 0.459 346 WB Large T A0211 139 FPSDLHQFL 0.459 349 WB Large T A0211 439 GLLDLCGGK 0.452 377 WB Large T A0211 465 AIDQYMVVF 0.449 389 WB Large T A0211 21 AAWGNLPLM 0.448 394 WB Large T A0211 521 IFPPGLVTM 0.438 438 WB Large T A0211 175 KLMEKYSVT 0.437 440 WB Large T A0211 457 RLTFELGVA 0.430 478 WB Large T A0211 150 AVFSNRTLA 0.428 486 WB Large T A0211 198 FLTPHRHRV 0.950 1 SB Large T A0212 405 VIFDFLHCV 0.944 1 SB Large T A0212 384 VLEQYMAGV 0.915 2 SB Large T A0212 397 CLLPKMDSV 0.909 2 SB Large T A0212 409 FLHCVVFNV 0.905 2 SB Large T A0212 435 TLAAGLLDL 0.836 5 SB Large T A0212 569 ILQSGMTLL 0.822 6 SB Large T A0212 292 MYLEFQYNV 0.776 11 SB Large T A0212 578 LLLIWFRPV 0.774 11 SB Large T A0212 557 SLQNSEFLL 0.763 12 SB Large T A0212 563 FLLEKRILQ 0.736 17 SB Large T A0212 464 VAIDQYMVV 0.723 20 SB Large T A0212 494 NLDSLRDYL 0.711 22 SB Large T A0212 361 MLTERFNHI 0.692 27 SB Large T A0212 579 LLIWFRPVA 0.684 30 SB Large T A0212 288 LLLGMYLEF 0.636 51 WB Large T A0212 497 SLRDYLDGS 0.636 51 WB Large T A0212 215 KLCTFSFLI 0.619 61 WB Large T A0212 596 RIVEWKERL 0.610 68 WB Large T A0212 388 YMAGVAWLH 0.607 69 WB Large T A0212 287 FLLLGMYLE 0.598 77 WB Large T A0212 428 PIDSGKTTL 0.561 115 WB Large T A0212 14 DLLGLERAA 0.548 133 WB Large T A0212 454 PMERLTFEL 0.545 137 WB Large T A0212 526 LVTMNEYPV 0.533 155 WB Large T A0212 458 LTFELGVAI 0.531 160 WB Large T A0212 236 ALTRDPYHI 0.525 171 WB Large T A0212 208 AINNFCQKL 0.521 177 WB Large T A0212 500 DYLDGSVKV 0.517 185 WB Large T A0212 111 FASDEEATA 0.507 206 WB Large T A0212 289 LLGMYLEFQ 0.505 212 WB Large T A0212 188 HMCAGHNII 0.504 214 WB Large T A0212 368 HILDKMDLI 0.496 232 WB Large T A0212 398 LLPKMDSVI 0.494 239 WB Large T A0212 463 GVAIDQYMV 0.481 275 WB Large T A0212 401 KMDSVIFDF 0.477 286 WB Large T A0212 171 ILYKKLMEK 0.476 289 WB Large T A0212 568 RILQSGMTL 0.453 370 WB Large T A0212 139 FPSDLHQFL 0.450 385 WB Large T A0212 394 WLHCLLPKM 0.439 434 WB Large T A0212 198 FLTPHRHRV 0.957 1 SB Large T A0216 405 VIFDFLHCV 0.924 2 SB Large T A0216 384 VLEQYMAGV 0.898 2 SB Large T A0216 397 CLLPKMDSV 0.898 3 SB Large T A0216 409 FLHCVVFNV 0.881 3 SB Large T A0216 569 ILQSGMTLL 0.861 4 SB Large T A0216 494 NLDSLRDYL 0.860 4 SB Large T A0216 557 SLQNSEFLL 0.844 5 SB Large T A0216 454 PMERLTFEL 0.756 13 SB Large T A0216 428 PIDSGKTTL 0.749 15 SB Large T A0216 578 LLLIWFRPV 0.694 27 SB Large T A0216 435 TLAAGLLDL 0.679 32 SB Large T A0216 526 LVTMNEYPV 0.669 36 SB Large T A0216 289 LLGMYLEFQ 0.657 40 SB Large T A0216 215 KLCTFSFLI 0.657 41 SB Large T A0216 142 DLHQFLSQA 0.655 41 SB Large T A0216 292 MYLEFQYNV 0.655 41 SB Large T A0216 563 FLLEKRILQ 0.646 45 SB Large T A0216 596 RIVEWKERL 0.646 46 SB Large T A0216 236 ALTRDPYHI 0.645 46 SB Large T A0216 416 NVPKRRYWL 0.628 55 WB Large T A0216 463 GVAIDQYMV 0.626 57 WB Large T A0216 361 MLTERFNHI 0.601 74 WB Large T A0216 156 TLACFAVYT 0.590 84 WB Large T A0216 208 AINNFCQKL 0.578 96 WB Large T A0216 568 RILQSGMTL 0.574 99 WB Large T A0216 500 DYLDGSVKV 0.539 146 WB Large T A0216 398 LLPKMDSVI 0.537 149 WB Large T A0216 579 LLIWFRPVA 0.529 163 WB Large T A0216 391 GVAWLHCLL 0.519 181 WB Large T A0216 353 TLHMTREEM 0.510 200 WB Large T A0216 619 NICMGKCIL 0.500 224 WB Large T A0216 648 SQSQCSSQV 0.495 236 WB Large T A0216 171 ILYKKLMEK 0.463 333 WB Large T A0216 464 VAIDQYMVV 0.456 359 WB Large T A0216 188 HMCAGHNII 0.440 428 WB Large T A0216 368 HILDKMDLI 0.426 497 WB Large T A0216 198 FLTPHRHRV 0.947 1 SB Large T A0219 405 VIFDFLHCV 0.932 2 SB Large T A0219 409 FLHCVVFNV 0.879 3 SB Large T A0219 397 CLLPKMDSV 0.868 4 SB Large T A0219 569 ILQSGMTLL 0.849 5 SB Large T A0219 435 TLAAGLLDL 0.795 9 SB Large T A0219 384 VLEQYMAGV 0.766 12 SB Large T A0219 494 NLDSLRDYL 0.716 21 SB Large T A0219 428 PIDSGKTTL 0.697 26 SB Large T A0219 557 SLQNSEFLL 0.621 60 WB Large T A0219 578 LLLIWFRPV 0.588 86 WB Large T A0219 292 MYLEFQYNV 0.530 162 WB Large T A0219 526 LVTMNEYPV 0.519 182 WB Large T A0219 361 MLTERFNHI 0.518 183 WB Large T A0219 500 DYLDGSVKV 0.508 205 WB Large T A0219 21 AAWGNLPLM 0.506 209 WB Large T A0219 454 PMERLTFEL 0.461 340 WB Large T A0219 236 ALTRDPYHI 0.459 349 WB Large T A0219 146 FLSQAVFSN 0.428 486 WB Large T A0219 171 ILYKKLMEK 0.858 4 SB Large T A0301 609 SMYTFSRMK 0.762 13 SB Large T A0301 28 LMRKAYLKK 0.703 24 SB Large T A0301 195 IIFFLTPHR 0.658 40 SB Large T A0301 50 KMKRMNTLY 0.654 42 SB Large T A0301 217 CTFSFLICK 0.640 49 SB Large T A0301 221 FLICKGVNK 0.633 52 WB Large T A0301 528 TMNEYPVPK 0.599 76 WB Large T A0301 155 RTLACFAVY 0.595 79 WB Large T A0301 27 PLMRKAYLK 0.578 96 WB Large T A0301 226 GVNKEYLLY 0.545 137 WB Large T A0301 121 SQHSTPPKK 0.490 248 WB Large T A0301 231 YLLYSALTR 0.475 294 WB Large T A0301 341 AVDTVLAKK 0.472 302 WB Large T A0301 576 LLLLLIWFR 0.467 318 WB Large T A0301 668 HSQELHLCK 0.464 331 WB Large T A0301 504 GSVKVNLEK 0.452 376 WB Large T A0301 509 NLEKKHLNK 0.452 377 WB Large T A0301 350 RVDTLHMTR 0.444 409 WB Large T A0301 603 RLDSEISMY 0.433 461 WB Large T A0301 217 CTFSFLICK 0.826 6 SB Large T A1101 528 TMNEYPVPK 0.817 7 SB Large T A1101 609 SMYTFSRMK 0.802 8 SB Large T A1101 207 SAINNFCQK 0.774 11 SB Large T A1101 171 ILYKKLMEK 0.747 15 SB Large T A1101 668 HSQELHLCK 0.730 18 SB Large T A1101 341 AVDTVLAKK 0.703 24 SB Large T A1101 195 IIFFLTPHR 0.686 30 SB Large T A1101 504 GSVKVNLEK 0.679 32 SB Large T A1101 121 SQHSTPPKK 0.674 33 SB Large T A1101 147 LSQAVFSNR 0.654 42 SB Large T A1101 536 KTLQARFVR 0.650 44 SB Large T A1101 155 RTLACFAVY 0.646 46 SB Large T A1101 340 QAVDTVLAK 0.602 74 WB Large T A1101 505 SVKVNLEKK 0.583 91 WB Large T A1101 27 PLMRKAYLK 0.576 98 WB Large T A1101 120 DSQHSTPPK 0.567 108 WB Large T A1101 393 AWLHCLLPK 0.566 109 WB Large T A1101 413 VVFNVPKRR 0.559 118 WB Large T A1101 439 GLLDLCGGK 0.551 129 WB Large T A1101 324 NAIIFAESK 0.539 146 WB Large T A1101 350 RVDTLHMTR 0.529 163 WB Large T A1101 226 GVNKEYLLY 0.518 184 WB Large T A1101 607 EISMYTFSR 0.496 233 WB Large T A1101 274 ITEYAVETK 0.491 247 WB Large T A1101 593 IQSRIVEWK 0.489 252 WB Large T A1101 491 GINNLDSLR 0.488 254 WB Large T A1101 296 FQYNVEECK 0.478 285 WB Large T A1101 576 LLLLLIWFR 0.466 321 WB Large T A1101 91 SWWSSFNEK 0.461 340 WB Large T A1101 158 ACFAVYTTK 0.456 360 WB Large T A1101 221 FLICKGVNK 0.446 399 WB Large T A1101 32 AYLKKCKEF 0.708 23 SB Large T A2301 581 IWFRPVADF 0.678 32 SB Large T A2301 312 PYHFKYHEK 0.647 45 SB Large T A2301 91 SWWSSFNEK 0.552 126 WB Large T A2301 387 QYMAGVAWL 0.546 135 WB Large T A2301 190 CAGHNIIFF 0.527 166 WB Large T A2301 401 KMDSVIFDF 0.522 176 WB Large T A2301 286 VFLLLGMYL 0.518 183 WB Large T A2301 292 MYLEFQYNV 0.512 196 WB Large T A2301 138 DFPSDLHQF 0.501 220 WB Large T A2301 314 HFKYHEKHF 0.501 222 WB Large T A2301 575 TLLLLLIWF 0.496 233 WB Large T A2301 213 CQKLCTFSF 0.485 263 WB Large T A2301 393 AWLHCLLPK 0.471 305 WB Large T A2301 288 LLLGMYLEF 0.464 331 WB Large T A2301 320 KHFANAIIF 0.463 334 WB Large T A2301 327 IFAESKNQK 0.458 352 WB Large T A2301 610 MYTFSRMKY 0.455 365 WB Large T A2301 211 NFCQKLCTF 0.454 368 WB Large T A2301 612 TFSRMKYNI 0.440 427 WB Large T A2301 88 EWESWWSSF 0.597 78 WB Large T A2402 387 QYMAGVAWL 0.587 87 WB Large T A2402 138 DFPSDLHQF 0.544 138 WB Large T A2402 241 PYHIIEESI 0.536 150 WB Large T A2402 32 AYLKKCKEF 0.523 174 WB Large T A2402 581 IWFRPVADF 0.503 216 WB Large T A2402 468 QYMVVFEDV 0.502 219 WB Large T A2402 612 TFSRMKYNI 0.451 381 WB Large T A2402 286 VFLLLGMYL 0.434 456 WB Large T A2402 417 VPKRRYWLF 0.432 466 WB Large T A2402 32 AYLKKCKEF 0.859 4 SB Large T A2403 387 QYMAGVAWL 0.773 11 SB Large T A2403 138 DFPSDLHQF 0.618 62 WB Large T A2403 320 KHFANAIIF 0.569 105 WB Large T A2403 521 IFPPGLVTM 0.551 129 WB Large T A2403 68 AHQPDFGTW 0.542 142 WB Large T A2403 286 VFLLLGMYL 0.532 158 WB Large T A2403 581 IWFRPVADF 0.506 209 WB Large T A2403 401 KMDSVIFDF 0.462 338 WB Large T A2403 190 CAGHNIIFF 0.458 351 WB Large T A2403 468 QYMVVFEDV 0.446 400 WB Large T A2403 211 NFCQKLCTF 0.433 461 WB Large T A2403 285 DVFLLLGMY 0.689 29 SB Large T A2601 265 ETKQVSWKL 0.506 209 WB Large T A2601 8 ESMELMDLL 0.463 335 WB Large T A2601 285 DVFLLLGMY 0.923 2 SB Large T A2602 465 AIDQYMVVF 0.801 8 SB Large T A2602 280 ETKCEDVFL 0.742 16 SB Large T A2602 545 QIDFRPKIY 0.724 19 SB Large T A2602 138 DFPSDLHQF 0.617 63 WB Large T A2602 226 GVNKEYLLY 0.612 66 WB Large T A2602 155 RTLACFAVY 0.609 68 WB Large T A2602 152 FSNRTLACF 0.590 84 WB Large T A2602 265 ETKQVSWKL 0.518 183 WB Large T A2602 8 ESMELMDLL 0.476 290 WB Large T A2602 103 DLFCHEDMF 0.457 358 WB Large T A2602 450 NVNLPMERL 0.447 396 WB Large T A2602 164 TTKEKAQIL 0.437 441 WB Large T A2602 290 LGMYLEFQY 0.593 81 WB Large T A2902 50 KMKRMNTLY 0.576 98 WB Large T A2902 269 VSWKLITEY 0.552 127 WB Large T A2902 285 DVFLLLGMY 0.538 148 WB Large T A2902 226 GVNKEYLLY 0.508 204 WB Large T A2902 610 MYTFSRMKY 0.474 295 WB Large T A2902 414 VFNVPKRRY 0.429 480 WB Large T A2902 28 LMRKAYLKK 0.830 6 SB Large T A3001 51 MKRMNTLYK 0.827 6 SB Large T A3001 36 KCKEFHPDK 0.817 7 SB Large T A3001 418 PKRRYWLFK 0.813 7 SB Large T A3001 121 SQHSTPPKK 0.755 14 SB Large T A3001 682 KRPKTPPPK 0.723 19 SB Large T A3001 528 TMNEYPVPK 0.716 21 SB Large T A3001 677 GFQCFKRPK 0.683 30 SB Large T A3001 120 DSQHSTPPK 0.675 33 SB Large T A3001 674 LCKGFQCFK 0.669 36 SB Large T A3001 129 KKRKVEDPK 0.666 37 SB Large T A3001 158 ACFAVYTTK 0.657 40 SB Large T A3001 536 KTLQARFVR 0.637 51 WB Large T A3001 505 SVKVNLEKK 0.634 52 WB Large T A3001 609 SMYTFSRMK 0.598 77 WB Large T A3001 166 KEKAQILYK 0.579 95 WB Large T A3001 312 PYHFKYHEK 0.574 100 WB Large T A3001 195 IIFFLTPHR 0.569 105 WB Large T A3001 393 AWLHCLLPK 0.519 181 WB Large T A3001 50 KMKRMNTLY 0.501 220 WB Large T A3001 340 QAVDTVLAK 0.481 273 WB Large T A3001 274 ITEYAVETK 0.481 274 WB Large T A3001 124 STPPKKKRK 0.478 282 WB Large T A3001 171 ILYKKLMEK 0.467 318 WB Large T A3001 411 HCVVFNVPK 0.465 325 WB Large T A3001 27 PLMRKAYLK 0.439 431 WB Large T A3001 544 RQIDFRPKI 0.437 440 WB Large T A3001 668 HSQELHLCK 0.436 445 WB Large T A3001 52 KRMNTLYKK 0.435 453 WB Large T A3001 50 KMKRMNTLY 0.561 115 WB Large T A3002 401 KMDSVIFDF 0.525 169 WB Large T A3002 172 LYKKLMEKY 0.524 172 WB Large T A3002 285 DVFLLLGMY 0.509 201 WB Large T A3002 610 MYTFSRMKY 0.502 218 WB Large T A3002 226 GVNKEYLLY 0.497 231 WB Large T A3002 603 RLDSEISMY 0.483 269 WB Large T A3002 536 KTLQARFVR 0.856 4 SB Large T A3101 576 LLLLLIWFR 0.848 5 SB Large T A3101 179 KYSVTFISR 0.844 5 SB Large T A3101 541 RFVRQIDFR 0.836 5 SB Large T A3101 147 LSQAVFSNR 0.821 6 SB Large T A3101 547 DFRPKIYLR 0.799 8 SB Large T A3101 195 IIFFLTPHR 0.720 20 SB Large T A3101 528 TMNEYPVPK 0.713 22 SB Large T A3101 350 RVDTLHMTR 0.712 22 SB Large T A3101 197 FFLTPHRHR 0.682 31 SB Large T A3101 491 GINNLDSLR 0.668 36 SB Large T A3101 413 VVFNVPKRR 0.651 43 SB Large T A3101 607 EISMYTFSR 0.604 72 WB Large T A3101 155 RTLACFAVY 0.573 101 WB Large T A3101 609 SMYTFSRMK 0.567 108 WB Large T A3101 217 CTFSFLICK 0.563 113 WB Large T A3101 50 KMKRMNTLY 0.540 144 WB Large T A3101 91 SWWSSFNEK 0.515 190 WB Large T A3101 123 HSTPPKKKR 0.487 257 WB Large T A3101 292 MYLEFQYNV 0.476 289 WB Large T A3101 677 GFQCFKRPK 0.472 301 WB Large T A3101 231 YLLYSALTR 0.438 439 WB Large T A3101 28 LMRKAYLKK 0.436 447 WB Large T A3101 547 DFRPKIYLR 0.938 1 SB Large T A3301 576 LLLLLIWFR 0.827 6 SB Large T A3301 607 EISMYTFSR 0.826 6 SB Large T A3301 195 IIFFLTPHR 0.692 27 SB Large T A3301 588 DFSKDIQSR 0.669 35 SB Large T A3301 197 FFLTPHRHR 0.615 64 WB Large T A3301 147 LSQAVFSNR 0.592 82 WB Large T A3301 231 YLLYSALTR 0.473 299 WB Large T A3301 607 EISMYTFSR 0.908 2 SB Large T A6801 412 CVVFNVPKR 0.851 5 SB Large T A6801 195 IIFFLTPHR 0.838 5 SB Large T A6801 217 CTFSFLICK 0.813 7 SB Large T A6801 324 NAIIFAESK 0.796 9 SB Large T A6801 207 SAINNFCQK 0.749 15 SB Large T A6801 160 FAVYTTKEK 0.721 20 SB Large T A6801 274 ITEYAVETK 0.648 44 SB Large T A6801 147 LSQAVFSNR 0.643 47 SB Large T A6801 536 KTLQARFVR 0.643 47 SB Large T A6801 231 YLLYSALTR 0.628 56 WB Large T A6801 616 MKYNICMGK 0.625 58 WB Large T A6801 491 GINNLDSLR 0.625 58 WB Large T A6801 413 VVFNVPKRR 0.622 60 WB Large T A6801 560 NSEFLLEKR 0.620 61 WB Large T A6801 609 SMYTFSRMK 0.595 80 WB Large T A6801 167 EKAQILYKK 0.595 80 WB Large T A6801 610 MYTFSRMKY 0.588 86 WB Large T A6801 576 LLLLLIWFR 0.573 101 WB Large T A6801 469 YMVVFEDVK 0.567 108 WB Large T A6801 296 FQYNVEECK 0.534 153 WB Large T A6801 123 HSTPPKKKR 0.530 162 WB Large T A6801 340 QAVDTVLAK 0.527 167 WB Large T A6801 668 HSQELHLCK 0.512 196 WB Large T A6801 505 SVKVNLEKK 0.501 220 WB Large T A6801 120 DSQHSTPPK 0.485 263 WB Large T A6801 528 TMNEYPVPK 0.481 275 WB Large T A6801 171 ILYKKLMEK 0.479 281 WB Large T A6801 504 GSVKVNLEK 0.451 380 WB Large T A6801 285 DVFLLLGMY 0.450 385 WB Large T A6801 449 LNVNLPMER 0.448 390 WB Large T A6801 350 RVDTLHMTR 0.441 422 WB Large T A6801 403 DSVIFDFLH 0.439 432 WB Large T A6801 388 YMAGVAWLH 0.437 440 WB Large T A6801 588 DFSKDIQSR 0.437 444 WB Large T A6801 547 DFRPKIYLR 0.427 492 WB Large T A6801 8 ESMELMDLL 0.767 12 SB Large T A6802 409 FLHCVVFNV 0.700 25 SB Large T A6802 402 MDSVIFDFL 0.694 27 SB Large T A6802 450 NVNLPMERL 0.691 28 SB Large T A6802 219 FSFLICKGV 0.689 28 SB Large T A6802 265 ETKQVSWKL 0.607 70 WB Large T A6802 280 ETKCEDVFL 0.589 85 WB Large T A6802 416 NVPKRRYWL 0.585 89 WB Large T A6802 526 LVTMNEYPV 0.585 89 WB Large T A6802 405 VIFDFLHCV 0.583 91 WB Large T A6802 73 FGTWNSSEV 0.580 94 WB Large T A6802 458 LTFELGVAI 0.577 96 WB Large T A6802 371 DKMDLIFGA 0.565 110 WB Large T A6802 589 FSKDIQSRI 0.558 119 WB Large T A6802 198 FLTPHRHRV 0.543 140 WB Large T A6802 519 TQIFPPGLV 0.515 189 WB Large T A6802 377 FGAHGNAVL 0.502 218 WB Large T A6802 156 TLACFAVYT 0.493 239 WB Large T A6802 464 VAIDQYMVV 0.486 261 WB Large T A6802 468 QYMVVFEDV 0.482 271 WB Large T A6802 608 ISMYTFSRM 0.465 326 WB Large T A6802 343 DTVLAKKRV 0.459 348 WB Large T A6802 361 MLTERFNHI 0.450 382 WB Large T A6802 191 AGHNIIFFL 0.447 396 WB Large T A6802 154 NRTLACFAV 0.432 468 WB Large T A6802 458 LTFELGVAI 0.702 25 SB Large T A6901 405 VIFDFLHCV 0.691 28 SB Large T A6901 409 FLHCVVFNV 0.683 30 SB Large T A6901 578 LLLIWFRPV 0.630 54 WB Large T A6901 8 ESMELMDLL 0.609 68 WB Large T A6901 368 HILDKMDLI 0.587 87 WB Large T A6901 139 FPSDLHQFL 0.553 125 WB Large T A6901 292 MYLEFQYNV 0.522 176 WB Large T A6901 21 AAWGNLPLM 0.483 267 WB Large T A6901 198 FLTPHRHRV 0.481 274 WB Large T A6901 265 ETKQVSWKL 0.457 355 WB Large T A6901 500 DYLDGSVKV 0.449 389 WB Large T A6901 464 VAIDQYMVV 0.431 472 WB Large T A6901 20 RAAWGNLPL 0.721 20 SB Large T B0702 26 LPLMRKAYL 0.719 20 SB Large T B0702 200 TPHRHRVSA 0.662 38 SB Large T B0702 532 YPVPKTLQA 0.651 43 SB Large T B0702 399 LPKMDSVIF 0.516 187 WB Large T B0702 568 RILQSGMTL 0.499 226 WB Large T B0702 81 VPTYGTEEW 0.497 232 WB Large T B0702 139 FPSDLHQFL 0.467 320 WB Large T B0702 417 VPKRRYWLF 0.461 339 WB Large T B0702 417 VPKRRYWLF 0.587 87 WB Large T B0801 144 HQFLSQAVF 0.618 62 WB Large T B1501 234 YSALTRDPY 0.569 105 WB Large T B1501 50 KMKRMNTLY 0.561 115 WB Large T B1501 213 CQKLCTFSF 0.528 165 WB Large T B1501 155 RTLACFAVY 0.522 176 WB Large T B1501 514 HLNKRTQIF 0.501 221 WB Large T B1501 288 LLLGMYLEF 0.495 236 WB Large T B1501 570 LQSGMTLLL 0.479 280 WB Large T B1501 152 FSNRTLACF 0.468 315 WB Large T B1501 176 LMEKYSVTF 0.466 324 WB Large T B1501 20 RAAWGNLPL 0.444 411 WB Large T B1501 388 YMAGVAWLH 0.439 434 WB Large T B1501 10 MELMDLLGL 0.722 20 SB Large T B1801 530 NEYPVPKTL 0.706 24 SB Large T B1801 670 QELHLCKGF 0.692 27 SB Large T B1801 229 KEYLLYSAL 0.571 104 WB Large T B1801 664 SENPHSQEL 0.520 179 WB Large T B1801 52 KRMNTLYKK 0.656 41 SB Large T B2705 548 FRPKIYLRK 0.526 169 WB Large T B2705 420 RRYWLFKGP 0.518 184 WB Large T B2705 364 ERFNHILDK 0.460 343 WB Large T B2705 614 SRMKYNICM 0.452 375 WB Large T B2705 540 ARFVRQIDF 0.436 448 WB Large T B2705 682 KRPKTPPPK 0.430 477 WB Large T B2705 399 LPKMDSVIF 0.752 14 SB Large T B3501 139 FPSDLHQFL 0.633 52 WB Large T B3501 20 RAAWGNLPL 0.618 62 WB Large T B3501 234 YSALTRDPY 0.565 111 WB Large T B3501 447 KALNVNLPM 0.561 115 WB Large T B3501 21 AAWGNLPLM 0.545 137 WB Large T B3501 189 MCAGHNIIF 0.537 149 WB Large T B3501 111 FASDEEATA 0.509 202 WB Large T B3501 534 VPKTLQARF 0.498 229 WB Large T B3501 81 VPTYGTEEW 0.486 260 WB Large T B3501 269 VSWKLITEY 0.463 334 WB Large T B3501 285 DVFLLLGMY 0.447 394 WB Large T B3501 532 YPVPKTLQA 0.445 403 WB Large T B3501 176 LMEKYSVTF 0.441 423 WB Large T B3501 155 RTLACFAVY 0.434 455 WB Large T B3501 666 NPHSQELHL 0.426 495 WB Large T B3501 377 FGAHGNAVL 0.547 133 WB Large T B3901 10 MELMDLLGL 0.751 14 SB Large T B4001 229 KEYLLYSAL 0.690 28 SB Large T B4001 664 SENPHSQEL 0.681 31 SB Large T B4001 530 NEYPVPKTL 0.592 82 WB Large T B4001 7 EESMELMDL 0.561 115 WB Large T B4001 245 IEESIQGGL 0.552 127 WB Large T B4001 561 SEFLLEKRI 0.498 227 WB Large T B4001 18 LERAAWGNL 0.497 231 WB Large T B4001 358 REEMLTERF 0.441 422 WB Large T B4001 664 SENPHSQEL 0.630 54 WB Large T B4002 229 KEYLLYSAL 0.583 91 WB Large T B4002 606 SEISMYTFS 0.489 252 WB Large T B4002 279 VETKCEDVF 0.469 314 WB Large T B4002 177 MEKYSVTFI 0.462 335 WB Large T B4002 606 SEISMYTFS 0.521 177 WB Large T B4403 561 SEFLLEKRI 0.458 353 WB Large T B4403 664 SENPHSQEL 0.446 403 WB Large T B4403 — 329 AESKNQKSI 0.497 229 WB Large T B4501 453 LPMERLTFE 0.451 378 WB Large T B5101 139 FPSDLHQFL 0.438 437 WB Large T B5101 81 VPTYGTEEW 0.673 34 SB Large T B5301 399 LPKMDSVIF 0.628 55 WB Large T B5301 26 LPLMRKAYL 0.625 57 WB Large T B5301 666 NPHSQELHL 0.553 126 WB Large T B5301 139 FPSDLHQFL 0.509 202 WB Large T B5301 574 MTLLLLLIW 0.454 366 WB Large T B5301 522 FPPGLVTMN 0.672 34 SB Large T B5401 200 TPHRHRVSA 0.530 162 WB Large T B5401 219 FSFLICKGV 0.453 373 WB Large T B5401 453 LPMERLTFE 0.432 466 WB Large T B5401 574 MTLLLLLIW 0.446 399 WB Large T B5701 401 KMDSVIFDF 0.615 64 WB Large T B5801 574 MTLLLLLIW 0.594 80 WB Large T B5801 152 FSNRTLACF 0.562 114 WB Large T B5801 84 YGTEEWESW 0.553 125 WB Large T B5801 20 RAAWGNLPL 0.460 344 WB Large T B5801 447 KALNVNLPM 0.442 419 WB Large T B5801 269 VSWKLITEY 0.429 482 WB Large T B5801 10-mers 164 TTKEKAQILY 0.528 165 WB Large T A0101 401 KMDSVIFDFL 0.830 6 SB Large T A0201 291 GMYLEFQYNV 0.761 13 SB Large T A0201 405 VIFDFLHCVV 0.679 32 SB Large T A0201 525 GLVTMNEYPV 0.676 33 SB Large T A0201 501 YLDGSVKVNL 0.671 35 SB Large T A0201 569 ILQSGMTLLL 0.658 40 SB Large T A0201 577 LLLLIWFRPV 0.657 40 SB Large T A0201 383 AVLEQYMAGV 0.637 50 WB Large T A0201 361 MLTERFNHIL 0.616 63 WB Large T A0201 176 LMEKYSVTFI 0.609 68 WB Large T A0201 404 SVIFDFLHCV 0.585 89 WB Large T A0201 603 RLDSEISMYT 0.583 90 WB Large T A0201 497 SLRDYLDGSV 0.570 104 WB Large T A0201 272 KLITEYAVET 0.543 140 WB Large T A0201 578 LLLIWFRPVA 0.503 216 WB Large T A0201 563 FLLEKRILQS 0.500 222 WB Large T A0201 56 TLYKKMEQDV 0.485 263 WB Large T A0201 528 TMNEYPVPKT 0.457 354 WB Large T A0201 12 LMDLLGLERA 0.456 361 WB Large T A0201 568 RILQSGMTLL 0.454 367 WB Large T A0201 288 LLLGMYLEFQ 0.448 391 WB Large T A0201 3 VLNREESMEL 0.434 454 WB Large T A0201 401 KMDSVIFDFL 0.773 11 SB Large T A0202 603 RLDSEISMYT 0.720 20 SB Large T A0202 569 ILQSGMTLLL 0.716 21 SB Large T A0202 291 GMYLEFQYNV 0.681 31 SB Large T A0202 525 GLVTMNEYPV 0.674 33 SB Large T A0202 497 SLRDYLDGSV 0.665 37 SB Large T A0202 405 VIFDFLHCVV 0.649 44 SB Large T A0202 501 YLDGSVKVNL 0.648 44 SB Large T A0202 288 LLLGMYLEFQ 0.645 46 SB Large T A0202 577 LLLLIWFRPV 0.628 55 WB Large T A0202 287 FLLLGMYLEF 0.618 62 WB Large T A0202 570 LQSGMTLLLL 0.609 69 WB Large T A0202 12 LMDLLGLERA 0.607 70 WB Large T A0202 388 YMAGVAWLHC 0.582 91 WB Large T A0202 156 TLACFAVYTT 0.566 109 WB Large T A0202 175 KLMEKYSVTF 0.566 109 WB Large T A0202 3 VLNREESMEL 0.562 114 WB Large T A0202 397 CLLPKMDSVI 0.561 115 WB Large T A0202 285 DVFLLLGMYL 0.560 117 WB Large T A0202 435 TLAAGLLDLC 0.550 130 WB Large T A0202 361 MLTERFNHIL 0.543 140 WB Large T A0202 383 AVLEQYMAGV 0.535 153 WB Large T A0202 353 TLHMTREEML 0.532 157 WB Large T A0202 461 ELGVAIDQYM 0.520 180 WB Large T A0202 56 TLYKKMEQDV 0.516 187 WB Large T A0202 103 DLFCHEDMFA 0.516 187 WB Large T A0202 463 GVAIDQYMVV 0.509 202 WB Large T A0202 9 SMELMDLLGL 0.507 206 WB Large T A0202 142 DLHQFLSQAV 0.497 230 WB Large T A0202 611 YTFSRMKYNI 0.493 240 WB Large T A0202 272 KLITEYAVET 0.492 243 WB Large T A0202 375 LIFGAHGNAV 0.491 247 WB Large T A0202 563 FLLEKRILQS 0.488 253 WB Large T A0202 440 LLDLCGGKAL 0.488 255 WB Large T A0202 25 NLPLMRKAYL 0.483 269 WB Large T A0202 568 RILQSGMTLL 0.478 285 WB Large T A0202 176 LMEKYSVTFI 0.471 305 WB Large T A0202 236 ALTRDPYHII 0.461 341 WB Large T A0202 493 NNLDSLRDYL 0.454 366 WB Large T A0202 572 SGMTLLLLLI 0.453 371 WB Large T A0202 148 SQAVFSNRTL 0.450 383 WB Large T A0202 439 GLLDLCGGKA 0.445 406 WB Large T A0202 609 SMYTFSRMKY 0.445 406 WB Large T A0202 345 VLAKKRVDTL 0.445 407 WB Large T A0202 360 EMLTERFNHI 0.440 427 WB Large T A0202 578 LLLIWFRPVA 0.438 435 WB Large T A0202 556 KSLQNSEFLL 0.437 441 WB Large T A0202 213 CQKLCTFSFL 0.433 461 WB Large T A0202 497 SLRDYLDGSV 0.883 3 SB Large T A0203 361 MLTERFNHIL 0.815 7 SB Large T A0203 291 GMYLEFQYNV 0.792 9 SB Large T A0203 525 GLVTMNEYPV 0.769 12 SB Large T A0203 383 AVLEQYMAGV 0.755 14 SB Large T A0203 569 ILQSGMTLLL 0.731 18 SB Large T A0203 375 LIFGAHGNAV 0.731 18 SB Large T A0203 577 LLLLIWFRPV 0.708 23 SB Large T A0203 56 TLYKKMEQDV 0.707 23 SB Large T A0203 405 VIFDFLHCVV 0.674 34 SB Large T A0203 3 VLNREESMEL 0.666 37 SB Large T A0203 457 RLTFELGVAI 0.665 37 SB Large T A0203 404 SVIFDFLHCV 0.654 42 SB Large T A0203 501 YLDGSVKVNL 0.627 56 WB Large T A0203 345 VLAKKRVDTL 0.625 57 WB Large T A0203 176 LMEKYSVTFI 0.611 67 WB Large T A0203 156 TLACFAVYTT 0.600 75 WB Large T A0203 236 ALTRDPYHII 0.576 98 WB Large T A0203 401 KMDSVIFDFL 0.549 132 WB Large T A0203 537 TLQARFVRQI 0.548 132 WB Large T A0203 439 GLLDLCGGKA 0.546 136 WB Large T A0203 570 LQSGMTLLLL 0.542 142 WB Large T A0203 568 RILQSGMTLL 0.541 143 WB Large T A0203 397 CLLPKMDSVI 0.534 154 WB Large T A0203 611 YTFSRMKYNI 0.521 177 WB Large T A0203 142 DLHQFLSQAV 0.503 217 WB Large T A0203 603 RLDSEISMYT 0.488 254 WB Large T A0203 578 LLLIWFRPVA 0.485 261 WB Large T A0203 272 KLITEYAVET 0.485 263 WB Large T A0203 213 CQKLCTFSFL 0.480 277 WB Large T A0203 463 GVAIDQYMVV 0.473 298 WB Large T A0203 12 LMDLLGLERA 0.468 314 WB Large T A0203 528 TMNEYPVPKT 0.465 326 WB Large T A0203 9 SMELMDLLGL 0.462 338 WB Large T A0203 333 NQKSICQQAV 0.456 361 WB Large T A0203 336 SICQQAVDTV 0.435 451 WB Large T A0203 383 AVLEQYMAGV 0.666 37 SB Large T A0204 525 GLVTMNEYPV 0.603 73 WB Large T A0204 577 LLLLIWFRPV 0.591 83 WB Large T A0204 361 MLTERFNHIL 0.573 101 WB Large T A0204 497 SLRDYLDGSV 0.565 110 WB Large T A0204 336 SICQQAVDTV 0.557 120 WB Large T A0204 3 VLNREESMEL 0.557 120 WB Large T A0204 291 GMYLEFQYNV 0.549 132 WB Large T A0204 405 VIFDFLHCVV 0.533 155 WB Large T A0204 375 LIFGAHGNAV 0.515 190 WB Large T A0204 537 TLQARFVRQI 0.496 234 WB Large T A0204 236 ALTRDPYHII 0.494 238 WB Large T A0204 401 KMDSVIFDFL 0.484 266 WB Large T A0204 528 TMNEYPVPKT 0.473 300 WB Large T A0204 345 VLAKKRVDTL 0.461 339 WB Large T A0204 175 KLMEKYSVTF 0.451 380 WB Large T A0204 569 ILQSGMTLLL 0.446 401 WB Large T A0204 176 LMEKYSVTFI 0.437 440 WB Large T A0204 463 GVAIDQYMVV 0.434 454 WB Large T A0204 518 RTQIFPPGLV 0.431 473 WB Large T A0204 383 AVLEQYMAGV 0.832 6 SB Large T A0206 404 SVIFDFLHCV 0.773 11 SB Large T A0206 401 KMDSVIFDFL 0.762 13 SB Large T A0206 577 LLLLIWFRPV 0.744 15 SB Large T A0206 570 LQSGMTLLLL 0.714 22 SB Large T A0206 525 GLVTMNEYPV 0.698 26 SB Large T A0206 291 GMYLEFQYNV 0.682 31 SB Large T A0206 405 VIFDFLHCVV 0.674 33 SB Large T A0206 568 RILQSGMTLL 0.670 35 SB Large T A0206 361 MLTERFNHIL 0.650 43 SB Large T A0206 375 LIFGAHGNAV 0.644 47 SB Large T A0206 287 FLLLGMYLEF 0.607 70 WB Large T A0206 497 SLRDYLDGSV 0.596 79 WB Large T A0206 267 KQVSWKLITE 0.564 112 WB Large T A0206 175 KLMEKYSVTF 0.553 125 WB Large T A0206 148 SQAVFSNRTL 0.535 153 WB Large T A0206 20 RAAWGNLPLM 0.518 184 WB Large T A0206 388 YMAGVAWLHC 0.510 201 WB Large T A0206 213 CQKLCTFSFL 0.505 212 WB Large T A0206 272 KLITEYAVET 0.494 237 WB Large T A0206 578 LLLIWFRPVA 0.494 238 WB Large T A0206 336 SICQQAVDTV 0.493 242 WB Large T A0206 501 YLDGSVKVNL 0.487 257 WB Large T A0206 569 ILQSGMTLLL 0.483 269 WB Large T A0206 520 QIFPPGLVTM 0.482 272 WB Large T A0206 338 CQQAVDTVLA 0.481 275 WB Large T A0206 277 YAVETKCEDV 0.480 278 WB Large T A0206 155 RTLACFAVYT 0.469 312 WB Large T A0206 563 FLLEKRILQS 0.454 368 WB Large T A0206 603 RLDSEISMYT 0.445 405 WB Large T A0206 397 CLLPKMDSVI 0.441 422 WB Large T A0206 457 RLTFELGVAI 0.437 440 WB Large T A0206 207 SAINNFCQKL 0.433 463 WB Large T A0206 463 GVAIDQYMVV 0.429 481 WB Large T A0206 501 YLDGSVKVNL 0.958 1 SB Large T A0211 405 VIFDFLHCVV 0.936 2 SB Large T A0211 525 GLVTMNEYPV 0.915 2 SB Large T A0211 291 GMYLEFQYNV 0.909 2 SB Large T A0211 569 ILQSGMTLLL 0.902 2 SB Large T A0211 142 DLHQFLSQAV 0.898 3 SB Large T A0211 497 SLRDYLDGSV 0.895 3 SB Large T A0211 401 KMDSVIFDFL 0.890 3 SB Large T A0211 577 LLLLIWFRPV 0.888 3 SB Large T A0211 56 TLYKKMEQDV 0.875 3 SB Large T A0211 361 MLTERFNHIL 0.874 3 SB Large T A0211 383 AVLEQYMAGV 0.866 4 SB Large T A0211 442 DLCGGKALNV 0.854 4 SB Large T A0211 375 LIFGAHGNAV 0.829 6 SB Large T A0211 3 VLNREESMEL 0.824 6 SB Large T A0211 288 LLLGMYLEFQ 0.816 7 SB Large T A0211 603 RLDSEISMYT 0.797 9 SB Large T A0211 404 SVIFDFLHCV 0.791 9 SB Large T A0211 236 ALTRDPYHII 0.782 10 SB Large T A0211 388 YMAGVAWLHC 0.782 10 SB Large T A0211 12 LMDLLGLERA 0.757 13 SB Large T A0211 287 FLLLGMYLEF 0.747 15 SB Large T A0211 463 GVAIDQYMVV 0.742 16 SB Large T A0211 336 SICQQAVDTV 0.736 17 SB Large T A0211 345 VLAKKRVDTL 0.725 19 SB Large T A0211 353 TLHMTREEML 0.722 20 SB Large T A0211 568 RILQSGMTLL 0.720 20 SB Large T A0211 440 LLDLCGGKAL 0.713 22 SB Large T A0211 578 LLLIWFRPVA 0.712 22 SB Large T A0211 563 FLLEKRILQS 0.708 23 SB Large T A0211 9 SMELMDLLGL 0.706 24 SB Large T A0211 439 GLLDLCGGKA 0.690 28 SB Large T A0211 520 QIFPPGLVTM 0.684 30 SB Large T A0211 25 NLPLMRKAYL 0.682 31 SB Large T A0211 457 RLTFELGVAI 0.675 33 SB Large T A0211 156 TLACFAVYTT 0.669 35 SB Large T A0211 435 TLAAGLLDLC 0.649 44 SB Large T A0211 397 CLLPKMDSVI 0.648 44 SB Large T A0211 197 FFLTPHRHRV 0.635 51 WB Large T A0211 537 TLQARFVRQI 0.630 55 WB Large T A0211 609 SMYTFSRMKY 0.624 58 WB Large T A0211 176 LMEKYSVTFI 0.612 66 WB Large T A0211 175 KLMEKYSVTF 0.575 98 WB Large T A0211 103 DLFCHEDMFA 0.573 101 WB Large T A0211 289 LLGMYLEFQY 0.539 146 WB Large T A0211 428 PIDSGKTTLA 0.534 155 WB Large T A0211 272 KLITEYAVET 0.531 160 WB Large T A0211 545 QIDFRPKIYL 0.527 166 WB Large T A0211 575 TLLLLLIWFR 0.518 183 WB Large T A0211 198 FLTPHRHRVS 0.517 185 WB Large T A0211 528 TMNEYPVPKT 0.509 203 WB Large T A0211 17 GLERAAWGNL 0.502 219 WB Large T A0211 384 VLEQYMAGVA 0.492 244 WB Large T A0211 277 YAVETKCEDV 0.480 278 WB Large T A0211 124 STPPKKKRKV 0.477 287 WB Large T A0211 360 EMLTERFNHI 0.458 351 WB Large T A0211 171 ILYKKLMEKY 0.456 358 WB Large T A0211 369 ILDKMDLIFG 0.442 418 WB Large T A0211 215 KLCTFSFLIC 0.432 464 WB Large T A0211 461 ELGVAIDQYM 0.429 479 WB Large T A0211 501 YLDGSVKVNL 0.900 2 SB Large T A0212 405 VIFDFLHCVV 0.897 3 SB Large T A0212 56 TLYKKMEQDV 0.893 3 SB Large T A0212 291 GMYLEFQYNV 0.886 3 SB Large T A0212 497 SLRDYLDGSV 0.867 4 SB Large T A0212 383 AVLEQYMAGV 0.855 4 SB Large T A0212 525 GLVTMNEYPV 0.825 6 SB Large T A0212 361 MLTERFNHIL 0.824 6 SB Large T A0212 375 LIFGAHGNAV 0.806 8 SB Large T A0212 142 DLHQFLSQAV 0.795 9 SB Large T A0212 3 VLNREESMEL 0.788 9 SB Large T A0212 401 KMDSVIFDFL 0.784 10 SB Large T A0212 569 ILQSGMTLLL 0.783 10 SB Large T A0212 577 LLLLIWFRPV 0.783 10 SB Large T A0212 388 YMAGVAWLHC 0.765 12 SB Large T A0212 345 VLAKKRVDTL 0.754 14 SB Large T A0212 288 LLLGMYLEFQ 0.715 21 SB Large T A0212 287 FLLLGMYLEF 0.683 30 SB Large T A0212 563 FLLEKRILQS 0.666 37 SB Large T A0212 442 DLCGGKALNV 0.657 40 SB Large T A0212 397 CLLPKMDSVI 0.632 53 WB Large T A0212 12 LMDLLGLERA 0.604 72 WB Large T A0212 404 SVIFDFLHCV 0.604 72 WB Large T A0212 9 SMELMDLLGL 0.579 95 WB Large T A0212 603 RLDSEISMYT 0.573 101 WB Large T A0212 236 ALTRDPYHII 0.570 104 WB Large T A0212 277 YAVETKCEDV 0.569 106 WB Large T A0212 578 LLLIWFRPVA 0.558 119 WB Large T A0212 353 TLHMTREEML 0.552 126 WB Large T A0212 197 FFLTPHRHRV 0.549 131 WB Large T A0212 520 QIFPPGLVTM 0.543 139 WB Large T A0212 176 LMEKYSVTFI 0.536 150 WB Large T A0212 175 KLMEKYSVTF 0.528 165 WB Large T A0212 463 GVAIDQYMVV 0.500 222 WB Large T A0212 336 SICQQAVDTV 0.495 235 WB Large T A0212 457 RLTFELGVAI 0.489 252 WB Large T A0212 198 FLTPHRHRVS 0.484 266 WB Large T A0212 609 SMYTFSRMKY 0.480 276 WB Large T A0212 171 ILYKKLMEKY 0.477 285 WB Large T A0212 25 NLPLMRKAYL 0.477 287 WB Large T A0212 439 GLLDLCGGKA 0.476 288 WB Large T A0212 611 YTFSRMKYNI 0.472 304 WB Large T A0212 435 TLAAGLLDLC 0.461 342 WB Large T A0212 440 LLDLCGGKAL 0.459 349 WB Large T A0212 568 RILQSGMTLL 0.458 352 WB Large T A0212 360 EMLTERFNHI 0.457 354 WB Large T A0212 537 TLQARFVRQI 0.452 375 WB Large T A0212 17 GLERAAWGNL 0.430 474 WB Large T A0212 528 TMNEYPVPKT 0.428 488 WB Large T A0212 525 GLVTMNEYPV 0.882 3 SB Large T A0216 405 VIFDFLHCVV 0.863 4 SB Large T A0216 497 SLRDYLDGSV 0.861 4 SB Large T A0216 56 TLYKKMEQDV 0.842 5 SB Large T A0216 291 GMYLEFQYNV 0.841 5 SB Large T A0216 569 ILQSGMTLLL 0.838 5 SB Large T A0216 501 YLDGSVKVNL 0.833 6 SB Large T A0216 361 MLTERFNHIL 0.812 7 SB Large T A0216 142 DLHQFLSQAV 0.809 7 SB Large T A0216 401 KMDSVIFDFL 0.806 8 SB Large T A0216 442 DLCGGKALNV 0.802 8 SB Large T A0216 375 LIFGAHGNAV 0.773 11 SB Large T A0216 3 VLNREESMEL 0.768 12 SB Large T A0216 345 VLAKKRVDTL 0.765 12 SB Large T A0216 577 LLLLIWFRPV 0.743 16 SB Large T A0216 383 AVLEQYMAGV 0.739 16 SB Large T A0216 336 SICQQAVDTV 0.721 20 SB Large T A0216 25 NLPLMRKAYL 0.703 24 SB Large T A0216 288 LLLGMYLEFQ 0.679 32 SB Large T A0216 176 LMEKYSVTFI 0.675 33 SB Large T A0216 236 ALTRDPYHII 0.671 35 SB Large T A0216 353 TLHMTREEML 0.668 36 SB Large T A0216 404 SVIFDFLHCV 0.647 45 SB Large T A0216 603 RLDSEISMYT 0.630 54 WB Large T A0216 197 FFLTPHRHRV 0.615 64 WB Large T A0216 388 YMAGVAWLHC 0.602 73 WB Large T A0216 568 RILQSGMTLL 0.598 77 WB Large T A0216 156 TLACFAVYTT 0.567 108 WB Large T A0216 397 CLLPKMDSVI 0.562 114 WB Large T A0216 461 ELGVAIDQYM 0.550 130 WB Large T A0216 17 GLERAAWGNL 0.545 137 WB Large T A0216 103 DLFCHEDMFA 0.537 149 WB Large T A0216 463 GVAIDQYMVV 0.534 155 WB Large T A0216 537 TLQARFVRQI 0.528 165 WB Large T A0216 563 FLLEKRILQS 0.511 198 WB Large T A0216 545 QIDFRPKIYL 0.493 240 WB Large T A0216 12 LMDLLGLERA 0.484 265 WB Large T A0216 287 FLLLGMYLEF 0.483 270 WB Large T A0216 289 LLGMYLEFQY 0.482 270 WB Large T A0216 439 GLLDLCGGKA 0.477 287 WB Large T A0216 9 SMELMDLLGL 0.468 316 WB Large T A0216 673 HLCKGFQCFK 0.468 317 WB Large T A0216 520 QIFPPGLVTM 0.463 334 WB Large T A0216 190 CAGHNIIFFL 0.447 397 WB Large T A0216 440 LLDLCGGKAL 0.445 406 WB Large T A0216 124 STPPKKKRKV 0.438 439 WB Large T A0216 578 LLLIWFRPVA 0.428 485 WB Large T A0216 501 YLDGSVKVNL 0.885 3 SB Large T A0219 569 ILQSGMTLLL 0.833 6 SB Large T A0219 401 KMDSVIFDFL 0.761 13 SB Large T A0219 361 MLTERFNHIL 0.747 15 SB Large T A0219 405 VIFDFLHCVV 0.704 24 SB Large T A0219 291 GMYLEFQYNV 0.679 32 SB Large T A0219 142 DLHQFLSQAV 0.676 33 SB Large T A0219 577 LLLLIWFRPV 0.646 45 SB Large T A0219 525 GLVTMNEYPV 0.631 54 WB Large T A0219 497 SLRDYLDGSV 0.622 59 WB Large T A0219 388 YMAGVAWLHC 0.582 91 WB Large T A0219 3 VLNREESMEL 0.573 101 WB Large T A0219 288 LLLGMYLEFQ 0.572 102 WB Large T A0219 56 TLYKKMEQDV 0.570 104 WB Large T A0219 375 LIFGAHGNAV 0.565 110 WB Large T A0219 442 DLCGGKALNV 0.557 120 WB Large T A0219 383 AVLEQYMAGV 0.556 122 WB Large T A0219 236 ALTRDPYHII 0.545 137 WB Large T A0219 345 VLAKKRVDTL 0.515 189 WB Large T A0219 603 RLDSEISMYT 0.498 227 WB Large T A0219 12 LMDLLGLERA 0.486 260 WB Large T A0219 397 CLLPKMDSVI 0.475 293 WB Large T A0219 404 SVIFDFLHCV 0.474 294 WB Large T A0219 435 TLAAGLLDLC 0.459 347 WB Large T A0219 197 FFLTPHRHRV 0.449 389 WB Large T A0219 353 TLHMTREEML 0.433 463 WB Large T A0219 537 TLQARFVRQI 0.427 492 WB Large T A0219 170 QILYKKLMEK 0.764 12 SB Large T A0301 50 KMKRMNTLYK 0.754 14 SB Large T A0301 615 RMKYNICMGK 0.751 14 SB Large T A0301 608 ISMYTFSRMK 0.734 17 SB Large T A0301 609 SMYTFSRMKY 0.707 23 SB Large T A0301 527 VTMNEYPVPK 0.691 28 SB Large T A0301 673 HLCKGFQCFK 0.668 36 SB Large T A0301 27 PLMRKAYLKK 0.663 38 SB Large T A0301 157 LACFAVYTTK 0.654 42 SB Large T A0301 392 VAWLHCLLPK 0.582 92 WB Large T A0301 575 TLLLLLIWFR 0.574 100 WB Large T A0301 220 SFLICKGVNK 0.554 124 WB Large T A0301 22 AWGNLPLMRK 0.533 156 WB Large T A0301 326 IIFAESKNQK 0.519 181 WB Large T A0301 26 LPLMRKAYLK 0.500 222 WB Large T A0301 558 LQNSEFLLEK 0.484 265 WB Large T A0301 311 QPYHFKYHEK 0.465 326 WB Large T A0301 417 VPKRRYWLFK 0.462 338 WB Large T A0301 206 VSAINNFCQK 0.448 391 WB Large T A0301 448 ALNVNLPMER 0.447 396 WB Large T A0301 273 LITEYAVETK 0.446 399 WB Large T A0301 171 ILYKKLMEKY 0.433 462 WB Large T A0301 527 VTMNEYPVPK 0.811 7 SB Large T A1101 608 ISMYTFSRMK 0.760 13 SB Large T A1101 392 VAWLHCLLPK 0.708 23 SB Large T A1101 558 LQNSEFLLEK 0.705 24 SB Large T A1101 50 KMKRMNTLYK 0.700 25 SB Large T A1101 326 IIFAESKNQK 0.695 27 SB Large T A1101 206 VSAINNFCQK 0.692 28 SB Large T A1101 609 SMYTFSRMKY 0.665 37 SB Large T A1101 575 TLLLLLIWFR 0.648 45 SB Large T A1101 170 QILYKKLMEK 0.643 47 SB Large T A1101 157 LACFAVYTTK 0.635 51 WB Large T A1101 673 HLCKGFQCFK 0.622 59 WB Large T A1101 90 ESWWSSFNEK 0.565 110 WB Large T A1101 615 RMKYNICMGK 0.556 121 WB Large T A1101 121 SQHSTPPKKK 0.552 127 WB Large T A1101 504 GSVKVNLEKK 0.541 143 WB Large T A1101 339 QQAVDTVLAK 0.540 145 WB Large T A1101 340 QAVDTVLAKK 0.534 154 WB Large T A1101 448 ALNVNLPMER 0.528 165 WB Large T A1101 194 NIIFFLTPHR 0.516 188 WB Large T A1101 27 PLMRKAYLKK 0.478 284 WB Large T A1101 21 AAWGNLPLMR 0.475 293 WB Large T A1101 273 LITEYAVETK 0.470 310 WB Large T A1101 120 DSQHSTPPKK 0.450 383 WB Large T A1101 22 AWGNLPLMRK 0.449 387 WB Large T A1101 220 SFLICKGVNK 0.445 404 WB Large T A1101 468 QYMVVFEDVK 0.626 57 WB Large T A2301 151 VFSNRTLACF 0.608 69 WB Large T A2301 287 FLLLGMYLEF 0.575 99 WB Large T A2301 582 WFRPVADFSK 0.548 133 WB Large T A2301 57 LYKKMEQDVK 0.531 160 WB Large T A2301 574 MTLLLLLIWF 0.524 171 WB Large T A2301 83 TYGTEEWESW 0.500 224 WB Large T A2301 406 IFDFLHCVVF 0.486 260 WB Large T A2301 416 NVPKRRYWLF 0.477 288 WB Large T A2301 220 SFLICKGVNK 0.469 311 WB Large T A2301 159 CFAVYTTKEK 0.465 326 WB Large T A2301 203 RHRVSAINNF 0.458 351 WB Large T A2301 295 EFQYNVEECK 0.447 396 WB Large T A2301 175 KLMEKYSVTF 0.446 401 WB Large T A2301 91 SWWSSFNEKW 0.436 447 WB Large T A2301 464 VAIDQYMVVF 0.430 478 WB Large T A2301 212 FCQKLCTFSF 0.426 499 WB Large T A2301 151 VFSNRTLACF 0.606 71 WB Large T A2402 162 VYTTKEKAQI 0.518 183 WB Large T A2402 617 KYNICMGKCI 0.510 200 WB Large T A2402 416 NVPKRRYWLF 0.506 209 WB Large T A2402 406 IFDFLHCVVF 0.483 269 WB Large T A2402 83 TYGTEEWESW 0.472 301 WB Large T A2402 138 DFPSDLHQFL 0.430 477 WB Large T A2402 83 TYGTEEWESW 0.622 59 WB Large T A2403 513 KHLNKRTQIF 0.548 132 WB Large T A2403 287 FLLLGMYLEF 0.533 155 WB Large T A2403 212 FCQKLCTFSF 0.510 201 WB Large T A2403 162 VYTTKEKAQI 0.492 243 WB Large T A2403 175 KLMEKYSVTF 0.491 245 WB Large T A2403 151 VFSNRTLACF 0.479 280 WB Large T A2403 313 YHFKYHEKHF 0.456 358 WB Large T A2403 406 IFDFLHCVVF 0.453 370 WB Large T A2403 416 NVPKRRYWLF 0.449 389 WB Large T A2403 203 RHRVSAINNF 0.444 408 WB Large T A2403 574 MTLLLLLIWF 0.429 480 WB Large T A2403 164 TTKEKAQILY 0.552 127 WB Large T A2601 607 EISMYTFSRM 0.466 322 WB Large T A2601 607 EISMYTFSRM 0.857 4 SB Large T A2602 520 QIFPPGLVTM 0.811 7 SB Large T A2602 268 QVSWKLITEY 0.726 19 SB Large T A2602 164 TTKEKAQILY 0.721 20 SB Large T A2602 416 NVPKRRYWLF 0.714 22 SB Large T A2602 533 PVPKTLQARF 0.685 30 SB Large T A2602 64 DVKVAHQPDF 0.665 37 SB Large T A2602 280 ETKCEDVFLL 0.646 46 SB Large T A2602 285 DVFLLLGMYL 0.612 66 WB Large T A2602 368 HILDKMDLIF 0.589 85 WB Large T A2602 80 EVPTYGTEEW 0.587 86 WB Large T A2602 184 FISRHMCAGH 0.532 158 WB Large T A2602 163 YTTKEKAQIL 0.514 192 WB Large T A2602 284 EDVFLLLGMY 0.470 308 WB Large T A2602 138 DFPSDLHQFL 0.465 326 WB Large T A2602 611 YTFSRMKYNI 0.465 327 WB Large T A2602 574 MTLLLLLIWF 0.463 333 WB Large T A2602 464 VAIDQYMVVF 0.457 354 WB Large T A2602 404 SVIFDFLHCV 0.451 380 WB Large T A2602 609 SMYTFSRMKY 0.700 25 SB Large T A2902 413 VVFNVPKRRY 0.524 172 WB Large T A2902 171 ILYKKLMEKY 0.501 221 WB Large T A2902 289 LLGMYLEFQY 0.496 232 WB Large T A2902 75 TWNSSEVPTY 0.466 321 WB Large T A2902 268 QVSWKLITEY 0.455 364 WB Large T A2902 50 KMKRMNTLYK 0.848 5 SB Large T A3001 676 KGFQCFKRPK 0.733 17 SB Large T A3001 681 FKRPKTPPPK 0.723 20 SB Large T A3001 51 MKRMNTLYKK 0.685 30 SB Large T A3001 615 RMKYNICMGK 0.677 33 SB Large T A3001 527 VTMNEYPVPK 0.661 39 SB Large T A3001 417 VPKRRYWLFK 0.637 50 WB Large T A3001 121 SQHSTPPKKK 0.623 59 WB Large T A3001 582 WFRPVADFSK 0.622 59 WB Large T A3001 542 FVRQIDFRPK 0.556 121 WB Large T A3001 608 ISMYTFSRMK 0.552 126 WB Large T A3001 128 KKKRKVEDPK 0.548 132 WB Large T A3001 547 DFRPKIYLRK 0.507 207 WB Large T A3001 307 QKKDQPYHFK 0.501 220 WB Large T A3001 27 PLMRKAYLKK 0.500 224 WB Large T A3001 356 MTREEMLTER 0.494 238 WB Large T A3001 29 MRKAYLKKCK 0.488 255 WB Large T A3001 119 ADSQHSTPPK 0.460 344 WB Large T A3001 363 TERFNHILDK 0.445 405 WB Large T A3001 166 KEKAQILYKK 0.442 418 WB Large T A3001 164 TTKEKAQILY 0.439 432 WB Large T A3001 120 DSQHSTPPKK 0.428 485 WB Large T A3001 233 LYSALTRDPY 0.534 155 WB Large T A3002 609 SMYTFSRMKY 0.528 165 WB Large T A3002 268 QVSWKLITEY 0.485 262 WB Large T A3002 75 TWNSSEVPTY 0.446 400 WB Large T A3002 575 TLLLLLIWFR 0.750 14 SB Large T A3101 230 EYLLYSALTR 0.642 48 SB Large T A3101 50 KMKRMNTLYK 0.640 49 SB Large T A3101 674 LCKGFQCFKR 0.638 50 WB Large T A3101 609 SMYTFSRMKY 0.623 58 WB Large T A3101 615 RMKYNICMGK 0.604 72 WB Large T A3101 194 NIIFFLTPHR 0.586 88 WB Large T A3101 448 ALNVNLPMER 0.583 90 WB Large T A3101 673 HLCKGFQCFK 0.573 101 WB Large T A3101 146 FLSQAVFSNR 0.570 104 WB Large T A3101 412 CVVFNVPKRR 0.565 110 WB Large T A3101 196 IFFLTPHRHR 0.550 130 WB Large T A3101 356 MTREEMLTER 0.548 132 WB Large T A3101 349 KRVDTLHMTR 0.530 161 WB Large T A3101 220 SFLICKGVNK 0.524 172 WB Large T A3101 51 MKRMNTLYKK 0.468 316 WB Large T A3101 157 LACFAVYTTK 0.456 358 WB Large T A3101 535 PKTLQARFVR 0.445 403 WB Large T A3101 606 SEISMYTFSR 0.445 404 WB Large T A3101 594 QSRIVEWKER 0.442 417 WB Large T A3101 205 RVSAINNFCQ 0.434 458 WB Large T A3101 230 EYLLYSALTR 0.653 42 SB Large T A3301 575 TLLLLLIWFR 0.600 76 WB Large T A3301 674 LCKGFQCFKR 0.537 150 WB Large T A3301 196 IFFLTPHRHR 0.529 162 WB Large T A3301 194 NIIFFLTPHR 0.529 163 WB Large T A3301 11 ELMDLLGLER 0.512 196 WB Large T A3301 146 FLSQAVFSNR 0.482 271 WB Large T A3301 178 EKYSVTFISR 0.464 330 WB Large T A3301 547 DFRPKIYLRK 0.429 482 WB Large T A3301 Large T A3301 194 NIIFFLTPHR 0.866 4 SB Large T A6801 412 CVVFNVPKRR 0.785 10 SB Large T A6801 356 MTREEMLTER 0.784 10 SB Large T A6801 90 ESWWSSFNEK 0.756 13 SB Large T A6801 146 FLSQAVFSNR 0.739 16 SB Large T A6801 11 ELMDLLGLER 0.720 20 SB Large T A6801 178 EKYSVTFISR 0.713 22 SB Large T A6801 157 LACFAVYTTK 0.693 27 SB Large T A6801 608 ISMYTFSRMK 0.660 39 SB Large T A6801 673 HLCKGFQCFK 0.645 46 SB Large T A6801 230 EYLLYSALTR 0.644 47 SB Large T A6801 575 TLLLLLIWFR 0.643 47 SB Large T A6801 326 IIFAESKNQK 0.639 49 SB Large T A6801 273 LITEYAVETK 0.632 53 WB Large T A6801 206 VSAINNFCQK 0.629 55 WB Large T A6801 340 QAVDTVLAKK 0.623 59 WB Large T A6801 490 HGINNLDSLR 0.593 81 WB Large T A6801 475 DVKGTGAESK 0.581 93 WB Large T A6801 606 SEISMYTFSR 0.572 102 WB Large T A6801 592 DIQSRIVEWK 0.563 113 WB Large T A6801 311 QPYHFKYHEK 0.556 122 WB Large T A6801 527 VTMNEYPVPK 0.541 143 WB Large T A6801 295 EFQYNVEECK 0.539 146 WB Large T A6801 299 NVEECKKCQK 0.534 155 WB Large T A6801 159 CFAVYTTKEK 0.524 171 WB Large T A6801 296 FQYNVEECKK 0.510 200 WB Large T A6801 196 IFFLTPHRHR 0.505 212 WB Large T A6801 622 MGKCILDITR 0.480 277 WB Large T A6801 542 FVRQIDFRPK 0.478 282 WB Large T A6801 411 HCVVFNVPKR 0.476 290 WB Large T A6801 120 DSQHSTPPKK 0.461 341 WB Large T A6801 546 IDFRPKIYLR 0.437 443 WB Large T A6801 164 TTKEKAQILY 0.433 460 WB Large T A6801 404 SVIFDFLHCV 0.762 13 SB Large T A6802 611 YTFSRMKYNI 0.677 32 SB Large T A6802 285 DVFLLLGMYL 0.632 53 WB Large T A6802 322 FANAIIFAES 0.613 66 WB Large T A6802 280 ETKCEDVFLL 0.609 69 WB Large T A6802 462 LGVAIDQYMV 0.574 100 WB Large T A6802 607 EISMYTFSRM 0.562 114 WB Large T A6802 375 LIFGAHGNAV 0.557 120 WB Large T A6802 405 VIFDFLHCVV 0.536 151 WB Large T A6802 647 ESQSQCSSQV 0.517 185 WB Large T A6802 190 CAGHNIIFFL 0.488 253 WB Large T A6802 383 AVLEQYMAGV 0.479 281 WB Large T A6802 77 NSSEVPTYGT 0.467 320 WB Large T A6802 19 ERAAWGNLPL 0.452 375 WB Large T A6802 108 EDMFASDEEA 0.451 379 WB Large T A6802 265 ETKQVSWKLI 0.451 380 WB Large T A6802 207 SAINNFCQKL 0.440 428 WB Large T A6802 463 GVAIDQYMVV 0.433 459 WB Large T A6802 156 TLACFAVYTT 0.432 465 WB Large T A6802 383 AVLEQYMAGV 0.745 15 SB Large T A6901 404 SVIFDFLHCV 0.639 49 SB Large T A6901 611 YTFSRMKYNI 0.596 79 WB Large T A6901 375 LIFGAHGNAV 0.575 99 WB Large T A6901 405 VIFDFLHCVV 0.552 127 WB Large T A6901 360 EMLTERFNHI 0.545 137 WB Large T A6901 520 QIFPPGLVTM 0.541 143 WB Large T A6901 453 LPMERLTFEL 0.477 287 WB Large T A6901 434 TTLAAGLLDL 0.466 324 WB Large T A6901 277 YAVETKCEDV 0.458 352 WB Large T A6901 197 FFLTPHRHRV 0.452 374 WB Large T A6901 577 LLLLIWFRPV 0.435 451 WB Large T A6901 285 DVFLLLGMYL 0.431 470 WB Large T A6901 549 RPKIYLRKSL 0.785 10 SB Large T B0702 200 TPHRHRVSAI 0.752 14 SB Large T B0702 453 LPMERLTFEL 0.722 20 SB Large T B0702 427 GPIDSGKTTL 0.704 24 SB Large T B0702 486 LPSGHGINNL 0.573 101 WB Large T B0702 584 RPVADFSKDI 0.560 117 WB Large T B0702 549 RPKIYLRKSL 0.479 280 WB Large T B0801 200 TPHRHRVSAI 0.453 373 WB Large T B0801 544 RQIDFRPKIY 0.584 89 WB Large T B1501 188 HMCAGHNIIF 0.577 97 WB Large T B1501 175 KLMEKYSVTF 0.568 107 WB Large T B1501 609 SMYTFSRMKY 0.536 150 WB Large T B1501 148 SQAVFSNRTL 0.502 218 WB Large T B1501 268 QVSWKLITEY 0.478 284 WB Large T B1501 287 FLLLGMYLEF 0.475 292 WB Large T B1501 249 IQGGLKEHDF 0.467 318 WB Large T B1501 464 VAIDQYMVVF 0.445 406 WB Large T B1501 570 LQSGMTLLLL 0.439 434 WB Large T B1501 460 FELGVAIDQY 0.795 9 SB Large T B1801 87 EEWESWWSSF 0.653 42 SB Large T B1801 455 MERLTFELGV 0.576 98 WB Large T B1801 574 MTLLLLLIWF 0.498 227 WB Large T B1801 420 RRYWLFKGPI 0.605 71 WB Large T B2705 52 KRMNTLYKKM 0.591 83 WB Large T B2705 567 KRILQSGMTL 0.564 111 WB Large T B2705 349 KRVDTLHMTR 0.487 258 WB Large T B2705 517 KRTQIFPPGL 0.471 305 WB Large T B2705 464 VAIDQYMVVF 0.679 32 SB Large T B3501 453 LPMERLTFEL 0.600 75 WB Large T B3501 20 RAAWGNLPLM 0.595 80 WB Large T B3501 268 QVSWKLITEY 0.558 119 WB Large T B3501 486 LPSGHGINNL 0.549 131 WB Large T B3501 287 FLLLGMYLEF 0.479 279 WB Large T B3501 523 PPGLVTMNEY 0.479 281 WB Large T B3501 532 YPVPKTLQAR 0.470 310 WB Large T B3501 139 FPSDLHQFLS 0.459 347 WB Large T B3501 189 MCAGHNIIFF 0.451 379 WB Large T B3501 389 MAGVAWLHCL 0.449 390 WB Large T B3501 262 EPEETKQVSW 0.433 460 WB Large T B3501 317 YHEKHFANAI 0.608 69 WB Large T B3901 148 SQAVFSNRTL 0.545 137 WB Large T B3901 19 ERAAWGNLPL 0.539 147 WB Large T B3901 501 YLDGSVKVNL 0.498 228 WB Large T B3901 6 REESMELMDL 0.707 23 SB Large T B4001 561 SEFLLEKRIL 0.683 30 SB Large T B4001 279 VETKCEDVFL 0.502 218 WB Large T B4001 264 EETKQVSWKL 0.500 224 WB Large T B4001 7 EESMELMDLL 0.488 253 WB Large T B4001 455 MERLTFELGV 0.485 263 WB Large T B4001 561 SEFLLEKRIL 0.595 80 WB Large T B4002 7 EESMELMDLL 0.482 271 WB Large T B4002 229 KEYLLYSALT 0.482 272 WB Large T B4002 279 VETKCEDVFL 0.472 303 WB Large T B4002 87 EEWESWWSSF 0.458 353 WB Large T B4002 561 SEFLLEKRIL 0.496 233 WB Large T B4403 606 SEISMYTFSR 0.427 493 WB Large T B4403 453 LPMERLTFEL 0.695 27 SB Large T B5101 240 DPYHIIEESI 0.492 244 WB Large T B5101 486 LPSGHGINNL 0.447 397 WB Large T B5101 453 LPMERLTFEL 0.721 20 SB Large T B5301 262 EPEETKQVSW 0.716 21 SB Large T B5301 486 LPSGHGINNL 0.585 89 WB Large T B5301 427 GPIDSGKTTL 0.470 308 WB Large T B5301 200 TPHRHRVSAI 0.457 356 WB Large T B5301 139 FPSDLHQFLS 0.584 89 WB Large T B5401 26 LPLMRKAYLK 0.511 197 WB Large T B5401 160 FAVYTTKEKA 0.489 252 WB Large T B5401 453 LPMERLTFEL 0.483 267 WB Large T B5401 67 VAHQPDFGTW 0.448 393 WB Large T B5701 67 VAHQPDFGTW 0.537 149 WB Large T B5801 464 VAIDQYMVVF 0.503 216 WB Large T B5801 20 RAAWGNLPLM 0.485 263 WB Large T B5801 556 KSLQNSEFLL 0.475 293 WB Large T B5801 175 KLMEKYSVTF 0.437 440 WB Large T B5801 31 KAYLKKCKEF 0.431 473 WB Large T B5801 591 KDIQSRIVEW 0.430 474 WB Large T B5801 11-mers 163 YTTKEKAQILY 0.682 31 SB Large T A0101 388 YMAGVAWLHCL 0.862 4 SB Large T A0201 175 KLMEKYSVTFI 0.854 4 SB Large T A0201 576 LLLLLIWFRPV 0.708 23 SB Large T A0201 369 ILDKMDLIFGA 0.641 48 SB Large T A0201 569 ILQSGMTLLLL 0.609 68 WB Large T A0201 146 FLSQAVFSNRT 0.563 113 WB Large T A0201 198 FLTPHRHRVSA 0.558 119 WB Large T A0201 287 FLLLGMYLEFQ 0.530 162 WB Large T A0201 568 RILQSGMTLLL 0.506 209 WB Large T A0201 528 TMNEYPVPKTL 0.501 222 WB Large T A0201 439 GLLDLCGGKAL 0.469 312 WB Large T A0201 448 ALNVNLPMERL 0.469 313 WB Large T A0201 577 LLLLIWFRPVA 0.462 336 WB Large T A0201 11 ELMDLLGLERA 0.458 351 WB Large T A0201 217 CTFSFLICKGV 0.447 398 WB Large T A0201 152 FSNRTLACFAV 0.439 431 WB Large T A0201 269 VSWKLITEYAV 0.439 432 WB Large T A0201 570 LQSGMTLLLLL 0.434 457 WB Large T A0201 2 KVLNREESMEL 0.432 467 WB Large T A0201 388 YMAGVAWLHCL 0.869 4 SB Large T A0202 175 KLMEKYSVTFI 0.858 4 SB Large T A0202 189 MCAGHNIIFFL 0.726 19 SB Large T A0202 198 FLTPHRHRVSA 0.718 21 SB Large T A0202 146 FLSQAVFSNRT 0.718 21 SB Large T A0202 570 LQSGMTLLLLL 0.667 36 SB Large T A0202 569 ILQSGMTLLLL 0.666 36 SB Large T A0202 448 ALNVNLPMERL 0.624 58 WB Large T A0202 576 LLLLLIWFRPV 0.621 60 WB Large T A0202 152 FSNRTLACFAV 0.601 74 WB Large T A0202 287 FLLLGMYLEFQ 0.593 82 WB Large T A0202 528 TMNEYPVPKTL 0.587 87 WB Large T A0202 11 ELMDLLGLERA 0.582 92 WB Large T A0202 243 HIIEESIQGGL 0.571 103 WB Large T A0202 369 ILDKMDLIFGA 0.561 115 WB Large T A0202 212 FCQKLCTFSFL 0.560 116 WB Large T A0202 375 LIFGAHGNAVL 0.541 142 WB Large T A0202 461 ELGVAIDQYMV 0.541 143 WB Large T A0202 409 FLHCVVFNVPK 0.524 171 WB Large T A0202 439 GLLDLCGGKAL 0.519 181 WB Large T A0202 452 NLPMERLTFEL 0.515 189 WB Large T A0202 407 FDFLHCVVFNV 0.493 239 WB Large T A0202 3 VLNREESMELM 0.491 245 WB Large T A0202 268 QVSWKLITEYA 0.488 255 WB Large T A0202 290 LGMYLEFQYNV 0.481 273 WB Large T A0202 217 CTFSFLICKGV 0.464 330 WB Large T A0202 564 LLEKRILQSGM 0.447 398 WB Large T A0202 222 LICKGVNKEYL 0.436 448 WB Large T A0202 226 GVNKEYLLYSA 0.428 485 WB Large T A0202 388 YMAGVAWLHCL 0.868 4 SB Large T A0203 175 KLMEKYSVTFI 0.862 4 SB Large T A0203 198 FLTPHRHRVSA 0.779 10 SB Large T A0203 528 TMNEYPVPKTL 0.766 12 SB Large T A0203 576 LLLLLIWFRPV 0.728 19 SB Large T A0203 569 ILQSGMTLLLL 0.703 24 SB Large T A0203 146 FLSQAVFSNRT 0.702 25 SB Large T A0203 448 ALNVNLPMERL 0.668 36 SB Large T A0203 11 ELMDLLGLERA 0.652 42 SB Large T A0203 439 GLLDLCGGKAL 0.593 81 WB Large T A0203 268 QVSWKLITEYA 0.577 97 WB Large T A0203 570 LQSGMTLLLLL 0.548 132 WB Large T A0203 226 GVNKEYLLYSA 0.540 144 WB Large T A0203 243 HIIEESIQGGL 0.523 174 WB Large T A0203 375 LIFGAHGNAVL 0.522 176 WB Large T A0203 382 NAVLEQYMAGV 0.516 188 WB Large T A0203 217 CTFSFLICKGV 0.515 190 WB Large T A0203 374 DLIFGAHGNAV 0.511 197 WB Large T A0203 404 SVIFDFLHCVV 0.498 229 WB Large T A0203 152 FSNRTLACFAV 0.491 245 WB Large T A0203 3 VLNREESMELM 0.473 298 WB Large T A0203 287 FLLLGMYLEFQ 0.469 312 WB Large T A0203 452 NLPMERLTFEL 0.465 327 WB Large T A0203 369 ILDKMDLIFGA 0.464 328 WB Large T A0203 568 RILQSGMTLLL 0.457 356 WB Large T A0203 199 LTPHRHRVSAI 0.453 373 WB Large T A0203 471 VVFEDVKGTGA 0.450 383 WB Large T A0203 469 YMVVFEDVKGT 0.450 385 WB Large T A0203 388 YMAGVAWLHCL 0.691 28 SB Large T A0204 528 TMNEYPVPKTL 0.687 29 SB Large T A0204 175 KLMEKYSVTFI 0.670 35 SB Large T A0204 576 LLLLLIWFRPV 0.616 63 WB Large T A0204 198 FLTPHRHRVSA 0.583 91 WB Large T A0204 2 KVLNREESMEL 0.525 170 WB Large T A0204 569 ILQSGMTLLLL 0.449 386 WB Large T A0204 336 SICQQAVDTVL 0.431 472 WB Large T A0204 544 RQIDFRPKIYL 0.801 8 SB Large T A0206 388 YMAGVAWLHCL 0.796 9 SB Large T A0206 175 KLMEKYSVTFI 0.743 16 SB Large T A0206 576 LLLLLIWFRPV 0.738 16 SB Large T A0206 570 LQSGMTLLLLL 0.711 22 SB Large T A0206 198 FLTPHRHRVSA 0.706 24 SB Large T A0206 404 SVIFDFLHCVV 0.688 29 SB Large T A0206 152 FSNRTLACFAV 0.646 46 SB Large T A0206 568 RILQSGMTLLL 0.644 47 SB Large T A0206 369 ILDKMDLIFGA 0.622 59 WB Large T A0206 2 KVLNREESMEL 0.620 61 WB Large T A0206 148 SQAVFSNRTLA 0.618 62 WB Large T A0206 335 KSICQQAVDTV 0.568 106 WB Large T A0206 382 NAVLEQYMAGV 0.548 133 WB Large T A0206 519 TQIFPPGLVTM 0.539 146 WB Large T A0206 243 HIIEESIQGGL 0.519 182 WB Large T A0206 287 FLLLGMYLEFQ 0.515 191 WB Large T A0206 146 FLSQAVFSNRT 0.506 210 WB Large T A0206 569 ILQSGMTLLLL 0.487 256 WB Large T A0206 439 GLLDLCGGKAL 0.478 284 WB Large T A0206 213 CQKLCTFSFLI 0.469 312 WB Large T A0206 542 FVRQIDFRPKI 0.464 330 WB Large T A0206 267 KQVSWKLITEY 0.462 336 WB Large T A0206 471 VVFEDVKGTGA 0.460 343 WB Large T A0206 383 AVLEQYMAGVA 0.445 407 WB Large T A0206 577 LLLLIWFRPVA 0.444 408 WB Large T A0206 155 RTLACFAVYTT 0.442 419 WB Large T A0206 268 QVSWKLITEYA 0.438 437 WB Large T A0206 375 LIFGAHGNAVL 0.437 441 WB Large T A0206 452 NLPMERLTFEL 0.429 479 WB Large T A0206 296 FQYNVEECKKC 0.427 490 WB Large T A0206 388 YMAGVAWLHCL 0.966 1 SB Large T A0211 198 FLTPHRHRVSA 0.943 1 SB Large T A0211 576 LLLLLIWFRPV 0.898 3 SB Large T A0211 569 ILQSGMTLLLL 0.893 3 SB Large T A0211 439 GLLDLCGGKAL 0.887 3 SB Large T A0211 452 NLPMERLTFEL 0.875 3 SB Large T A0211 369 ILDKMDLIFGA 0.868 4 SB Large T A0211 528 TMNEYPVPKTL 0.858 4 SB Large T A0211 461 ELGVAIDQYMV 0.854 4 SB Large T A0211 287 FLLLGMYLEFQ 0.832 6 SB Large T A0211 454 PMERLTFELGV 0.823 6 SB Large T A0211 11 ELMDLLGLERA 0.815 7 SB Large T A0211 360 EMLTERFNHIL 0.779 10 SB Large T A0211 374 DLIFGAHGNAV 0.775 11 SB Large T A0211 175 KLMEKYSVTFI 0.773 11 SB Large T A0211 577 LLLLIWFRPVA 0.765 12 SB Large T A0211 568 RILQSGMTLLL 0.755 14 SB Large T A0211 288 LLLGMYLEFQY 0.753 14 SB Large T A0211 341 AVDTVLAKKRV 0.752 14 SB Large T A0211 448 ALNVNLPMERL 0.747 15 SB Large T A0211 375 LIFGAHGNAVL 0.691 28 SB Large T A0211 603 RLDSEISMYTF 0.681 31 SB Large T A0211 404 SVIFDFLHCVV 0.671 35 SB Large T A0211 12 LMDLLGLERAA 0.669 35 SB Large T A0211 146 FLSQAVFSNRT 0.648 45 SB Large T A0211 485 DLPSGHGINNL 0.644 47 SB Large T A0211 563 FLLEKRILQSG 0.601 74 WB Large T A0211 2 KVLNREESMEL 0.597 77 WB Large T A0211 501 YLDGSVKVNLE 0.596 78 WB Large T A0211 189 MCAGHNIIFFL 0.591 83 WB Large T A0211 428 PIDSGKTTLAA 0.577 97 WB Large T A0211 405 VIFDFLHCVVF 0.563 112 WB Large T A0211 196 IFFLTPHRHRV 0.551 128 WB Large T A0211 217 CTFSFLICKGV 0.550 130 WB Large T A0211 269 VSWKLITEYAV 0.549 132 WB Large T A0211 109 DMFASDEEATA 0.544 138 WB Large T A0211 544 RQIDFRPKIYL 0.542 141 WB Large T A0211 3 VLNREESMELM 0.535 153 WB Large T A0211 557 SLQNSEFLLEK 0.517 186 WB Large T A0211 533 PVPKTLQARFV 0.511 198 WB Large T A0211 243 HIIEESIQGGL 0.500 224 WB Large T A0211 401 KMDSVIFDFLH 0.486 260 WB Large T A0211 222 LICKGVNKEYL 0.462 338 WB Large T A0211 353 TLHMTREEMLT 0.459 349 WB Large T A0211 232 LLYSALTRDPY 0.435 449 WB Large T A0211 215 KLCTFSFLICK 0.435 452 WB Large T A0211 573 GMTLLLLLIWF 0.433 459 WB Large T A0211 423 WLFKGPIDSGK 0.428 487 WB Large T A0211 388 YMAGVAWLHCL 0.936 1 SB Large T A0212 198 FLTPHRHRVSA 0.906 2 SB Large T A0212 439 GLLDLCGGKAL 0.823 6 SB Large T A0212 528 TMNEYPVPKTL 0.817 7 SB Large T A0212 576 LLLLLIWFRPV 0.817 7 SB Large T A0212 454 PMERLTFELGV 0.806 8 SB Large T A0212 569 ILQSGMTLLLL 0.801 8 SB Large T A0212 287 FLLLGMYLEFQ 0.777 11 SB Large T A0212 369 ILDKMDLIFGA 0.756 13 SB Large T A0212 374 DLIFGAHGNAV 0.706 24 SB Large T A0212 360 EMLTERFNHIL 0.682 31 SB Large T A0212 461 ELGVAIDQYMV 0.658 40 SB Large T A0212 288 LLLGMYLEFQY 0.655 41 SB Large T A0212 11 ELMDLLGLERA 0.654 42 SB Large T A0212 452 NLPMERLTFEL 0.645 46 SB Large T A0212 563 FLLEKRILQSG 0.643 47 SB Large T A0212 375 LIFGAHGNAVL 0.631 54 WB Large T A0212 175 KLMEKYSVTFI 0.620 60 WB Large T A0212 577 LLLLIWFRPVA 0.601 74 WB Large T A0212 269 VSWKLITEYAV 0.598 77 WB Large T A0212 12 LMDLLGLERAA 0.577 96 WB Large T A0212 146 FLSQAVFSNRT 0.577 97 WB Large T A0212 448 ALNVNLPMERL 0.574 100 WB Large T A0212 341 AVDTVLAKKRV 0.549 132 WB Large T A0212 485 DLPSGHGINNL 0.537 149 WB Large T A0212 405 VIFDFLHCVVF 0.536 151 WB Large T A0212 3 VLNREESMELM 0.514 192 WB Large T A0212 423 WLFKGPIDSGK 0.499 225 WB Large T A0212 2 KVLNREESMEL 0.481 273 WB Large T A0212 404 SVIFDFLHCVV 0.458 350 WB Large T A0212 564 LLEKRILQSGM 0.452 374 WB Large T A0212 469 YMVVFEDVKGT 0.452 377 WB Large T A0212 243 HIIEESIQGGL 0.441 421 WB Large T A0212 222 LICKGVNKEYL 0.440 428 WB Large T A0212 217 CTFSFLICKGV 0.437 444 WB Large T A0212 196 IFFLTPHRHRV 0.436 445 WB Large T A0212 189 MCAGHNIIFFL 0.432 469 WB Large T A0212 471 VVFEDVKGTGA 0.426 495 WB Large T A0212 388 YMAGVAWLHCL 0.907 2 SB Large T A0216 198 FLTPHRHRVSA 0.867 4 SB Large T A0216 461 ELGVAIDQYMV 0.859 4 SB Large T A0216 569 ILQSGMTLLLL 0.824 6 SB Large T A0216 452 NLPMERLTFEL 0.778 11 SB Large T A0216 454 PMERLTFELGV 0.771 11 SB Large T A0216 576 LLLLLIWFRPV 0.754 14 SB Large T A0216 528 TMNEYPVPKTL 0.752 14 SB Large T A0216 374 DLIFGAHGNAV 0.737 17 SB Large T A0216 287 FLLLGMYLEFQ 0.712 22 SB Large T A0216 341 AVDTVLAKKRV 0.711 22 SB Large T A0216 369 ILDKMDLIFGA 0.696 26 SB Large T A0216 448 ALNVNLPMERL 0.693 27 SB Large T A0216 175 KLMEKYSVTFI 0.691 28 SB Large T A0216 439 GLLDLCGGKAL 0.678 32 SB Large T A0216 146 FLSQAVFSNRT 0.661 39 SB Large T A0216 11 ELMDLLGLERA 0.650 43 SB Large T A0216 485 DLPSGHGINNL 0.642 48 SB Large T A0216 375 LIFGAHGNAVL 0.639 49 SB Large T A0216 360 EMLTERFNHIL 0.631 54 WB Large T A0216 222 LICKGVNKEYL 0.620 60 WB Large T A0216 568 RILQSGMTLLL 0.559 118 WB Large T A0216 196 IFFLTPHRHRV 0.554 124 WB Large T A0216 533 PVPKTLQARFV 0.551 128 WB Large T A0216 404 SVIFDFLHCVV 0.528 165 WB Large T A0216 189 MCAGHNIIFFL 0.523 173 WB Large T A0216 288 LLLGMYLEFQY 0.517 186 WB Large T A0216 2 KVLNREESMEL 0.514 191 WB Large T A0216 577 LLLLIWFRPVA 0.493 240 WB Large T A0216 544 RQIDFRPKIYL 0.485 264 WB Large T A0216 269 VSWKLITEYAV 0.483 267 WB Large T A0216 161 AVYTTKEKAQI 0.475 293 WB Large T A0216 109 DMFASDEEATA 0.457 355 WB Large T A0216 388 YMAGVAWLHCL 0.952 1 SB Large T A0219 569 ILQSGMTLLLL 0.841 5 SB Large T A0219 198 FLTPHRHRVSA 0.685 30 SB Large T A0219 576 LLLLLIWFRPV 0.681 31 SB Large T A0219 287 FLLLGMYLEFQ 0.664 37 SB Large T A0219 461 ELGVAIDQYMV 0.655 41 SB Large T A0219 369 ILDKMDLIFGA 0.647 45 SB Large T A0219 11 ELMDLLGLERA 0.602 73 WB Large T A0219 454 PMERLTFELGV 0.584 90 WB Large T A0219 448 ALNVNLPMERL 0.562 114 WB Large T A0219 146 FLSQAVFSNRT 0.559 118 WB Large T A0219 374 DLIFGAHGNAV 0.556 121 WB Large T A0219 360 EMLTERFNHIL 0.537 149 WB Large T A0219 528 TMNEYPVPKTL 0.532 157 WB Large T A0219 485 DLPSGHGINNL 0.524 172 WB Large T A0219 452 NLPMERLTFEL 0.507 206 WB Large T A0219 341 AVDTVLAKKRV 0.499 226 WB Large T A0219 439 GLLDLCGGKAL 0.485 262 WB Large T A0219 189 MCAGHNIIFFL 0.462 337 WB Large T A0219 175 KLMEKYSVTFI 0.454 367 WB Large T A0219 269 VSWKLITEYAV 0.448 394 WB Large T A0219 156 TLACFAVYTTK 0.728 18 SB Large T A0301 409 FLHCVVFNVPK 0.709 23 SB Large T A0301 215 KLCTFSFLICK 0.671 35 SB Large T A0301 50 KMKRMNTLYKK 0.667 36 SB Large T A0301 391 GVAWLHCLLPK 0.656 41 SB Large T A0301 205 RVSAINNFCQK 0.650 44 SB Large T A0301 56 TLYKKMEQDVK 0.645 46 SB Large T A0301 507 KVNLEKKHLNK 0.586 88 WB Large T A0301 219 FSFLICKGVNK 0.581 92 WB Large T A0301 195 IIFFLTPHRHR 0.575 99 WB Large T A0301 164 TTKEKAQILYK 0.549 131 WB Large T A0301 557 SLQNSEFLLEK 0.539 146 WB Large T A0301 272 KLITEYAVETK 0.533 156 WB Large T A0301 21 AAWGNLPLMRK 0.508 205 WB Large T A0301 416 NVPKRRYWLFK 0.507 206 WB Large T A0301 608 ISMYTFSRMKY 0.491 247 WB Large T A0301 574 MTLLLLLIWFR 0.485 261 WB Large T A0301 673 HLCKGFQCFKR 0.459 348 WB Large T A0301 28 LMRKAYLKKCK 0.454 369 WB Large T A0301 244 IIEESIQGGLK 0.448 393 WB Large T A0301 497 SLRDYLDGSVK 0.443 416 WB Large T A0301 423 WLFKGPIDSGK 0.432 464 WB Large T A0301 401 KMDSVIFDFLH 0.427 490 WB Large T A0301 391 GVAWLHCLLPK 0.825 6 SB Large T A1101 215 KLCTFSFLICK 0.800 8 SB Large T A1101 557 SLQNSEFLLEK 0.791 9 SB Large T A1101 205 RVSAINNFCQK 0.784 10 SB Large T A1101 574 MTLLLLLIWFR 0.768 12 SB Large T A1101 21 AAWGNLPLMRK 0.742 16 SB Large T A1101 164 TTKEKAQILYK 0.721 20 SB Large T A1101 156 TLACFAVYTTK 0.719 20 SB Large T A1101 526 LVTMNEYPVPK 0.716 21 SB Large T A1101 507 KVNLEKKHLNK 0.706 24 SB Large T A1101 325 AIIFAESKNQK 0.702 25 SB Large T A1101 169 AQILYKKLMEK 0.699 25 SB Large T A1101 118 TADSQHSTPPK 0.677 32 SB Large T A1101 416 NVPKRRYWLFK 0.651 43 SB Large T A1101 56 TLYKKMEQDVK 0.640 49 SB Large T A1101 50 KMKRMNTLYKK 0.634 52 WB Large T A1101 447 KALNVNLPMER 0.627 56 WB Large T A1101 322 FANAIIFAESK 0.620 61 WB Large T A1101 608 ISMYTFSRMKY 0.609 68 WB Large T A1101 219 FSFLICKGVNK 0.594 80 WB Large T A1101 338 CQQAVDTVLAK 0.593 81 WB Large T A1101 362 LTERFNHILDK 0.588 86 WB Large T A1101 409 FLHCVVFNVPK 0.555 122 WB Large T A1101 195 IIFFLTPHRHR 0.547 134 WB Large T A1101 437 AAGLLDLCGGK 0.547 134 WB Large T A1101 20 RAAWGNLPLMR 0.531 160 WB Large T A1101 272 KLITEYAVETK 0.526 169 WB Large T A1101 607 EISMYTFSRMK 0.523 174 WB Large T A1101 244 IIEESIQGGLK 0.506 209 WB Large T A1101 339 QQAVDTVLAKK 0.471 307 WB Large T A1101 467 DQYMVVFEDVK 0.445 404 WB Large T A1101 497 SLRDYLDGSVK 0.436 448 WB Large T A1101 581 IWFRPVADFSK 0.434 454 WB Large T A1101 312 PYHFKYHEKHF 0.709 23 SB Large T A2301 286 VFLLLGMYLEF 0.704 24 SB Large T A2301 610 MYTFSRMKYNI 0.668 36 SB Large T A2301 581 IWFRPVADFSK 0.626 57 WB Large T A2301 500 DYLDGSVKVNL 0.598 77 WB Large T A2301 211 NFCQKLCTFSF 0.575 99 WB Large T A2301 83 TYGTEEWESWW 0.560 116 WB Large T A2301 187 RHMCAGHNIIF 0.491 245 WB Large T A2301 179 KYSVTFISRHM 0.485 263 WB Large T A2301 316 KYHEKHFANAI 0.478 282 WB Large T A2301 295 EFQYNVEECKK 0.478 283 WB Large T A2301 617 KYNICMGKCIL 0.477 288 WB Large T A2301 95 SFNEKWDEDLF 0.476 289 WB Large T A2301 553 YLRKSLQNSEF 0.468 316 WB Large T A2301 162 VYTTKEKAQIL 0.451 380 WB Large T A2301 405 VIFDFLHCVVF 0.442 417 WB Large T A2301 316 KYHEKHFANAI 0.677 33 SB Large T A2402 286 VFLLLGMYLEF 0.676 33 SB Large T A2402 312 PYHFKYHEKHF 0.617 62 WB Large T A2402 610 MYTFSRMKYNI 0.570 105 WB Large T A2402 83 TYGTEEWESWW 0.514 192 WB Large T A2402 179 KYSVTFISRHM 0.513 193 WB Large T A2402 162 VYTTKEKAQIL 0.482 272 WB Large T A2402 211 NFCQKLCTFSF 0.461 341 WB Large T A2402 286 VFLLLGMYLEF 0.742 16 SB Large T A2403 316 KYHEKHFANAI 0.713 22 SB Large T A2403 83 TYGTEEWESWW 0.653 42 SB Large T A2403 312 PYHFKYHEKHF 0.613 66 WB Large T A2403 397 CLLPKMDSVIF 0.571 103 WB Large T A2403 162 VYTTKEKAQIL 0.563 112 WB Large T A2403 365 RFNHILDKMDL 0.554 124 WB Large T A2403 553 YLRKSLQNSEF 0.528 165 WB Large T A2403 617 KYNICMGKCIL 0.509 202 WB Large T A2403 211 NFCQKLCTFSF 0.504 213 WB Large T A2403 95 SFNEKWDEDLF 0.478 285 WB Large T A2403 187 RHMCAGHNIIF 0.466 321 WB Large T A2403 163 YTTKEKAQILY 0.631 54 WB Large T A2601 8 ESMELMDLLGL 0.474 297 WB Large T A2601 163 YTTKEKAQILY 0.728 19 SB Large T A2602 150 AVFSNRTLACF 0.703 24 SB Large T A2602 170 QILYKKLMEKY 0.637 51 WB Large T A2602 405 VIFDFLHCVVF 0.629 55 WB Large T A2602 280 ETKCEDVFLLL 0.628 56 WB Large T A2602 463 GVAIDQYMVVF 0.624 58 WB Large T A2602 243 HIIEESIQGGL 0.535 153 WB Large T A2602 356 MTREEMLTERF 0.491 247 WB Large T A2602 142 DLHQFLSQAVF 0.472 304 WB Large T A2602 450 NVNLPMERLTF 0.453 372 WB Large T A2602 553 YLRKSLQNSEF 0.450 382 WB Large T A2602 74 GTWNSSEVPTY 0.435 453 WB Large T A2602 8 ESMELMDLLGL 0.433 462 WB Large T A2602 221 FLICKGVNKEY 0.621 60 WB Large T A2902 288 LLLGMYLEFQY 0.600 75 WB Large T A2902 163 YTTKEKAQILY 0.475 293 WB Large T A2902 286 VFLLLGMYLEF 0.470 307 WB Large T A2902 170 QILYKKLMEKY 0.430 478 WB Large T A2902 405 VIFDFLHCVVF 0.427 492 WB Large T A2902 50 KMKRMNTLYKK 0.760 13 SB Large T A3001 28 LMRKAYLKKCK 0.745 15 SB Large T A3001 164 TTKEKAQILYK 0.727 19 SB Large T A3001 507 KVNLEKKHLNK 0.707 23 SB Large T A3001 680 CFKRPKTPPPK 0.688 29 SB Large T A3001 409 FLHCVVFNVPK 0.668 36 SB Large T A3001 497 SLRDYLDGSVK 0.662 38 SB Large T A3001 158 ACFAVYTTKEK 0.661 39 SB Large T A3001 416 NVPKRRYWLFK 0.594 80 WB Large T A3001 541 RFVRQIDFRPK 0.587 87 WB Large T A3001 215 KLCTFSFLICK 0.567 107 WB Large T A3001 348 KKRVDTLHMTR 0.563 112 WB Large T A3001 205 RVSAINNFCQK 0.546 136 WB Large T A3001 526 LVTMNEYPVPK 0.536 151 WB Large T A3001 306 CQKKDQPYHFK 0.508 204 WB Large T A3001 118 TADSQHSTPPK 0.505 211 WB Large T A3001 272 KLITEYAVETK 0.489 252 WB Large T A3001 156 TLACFAVYTTK 0.486 259 WB Large T A3001 557 SLQNSEFLLEK 0.482 271 WB Large T A3001 169 AQILYKKLMEK 0.470 309 WB Large T A3001 539 QARFVRQIDFR 0.458 353 WB Large T A3001 581 IWFRPVADFSK 0.451 378 WB Large T A3001 574 MTLLLLLIWFR 0.433 462 WB Large T A3001 34 LKKCKEFHPDK 0.429 482 WB Large T A3001 267 KQVSWKLITEY 0.523 175 WB Large T A3002 170 QILYKKLMEKY 0.442 420 WB Large T A3002 574 MTLLLLLIWFR 0.869 4 SB Large T A3101 50 KMKRMNTLYKK 0.838 5 SB Large T A3101 447 KALNVNLPMER 0.794 9 SB Large T A3101 145 QFLSQAVFSNR 0.744 15 SB Large T A3101 195 IIFFLTPHRHR 0.736 17 SB Large T A3101 673 HLCKGFQCFKR 0.670 35 SB Large T A3101 539 QARFVRQIDFR 0.653 42 SB Large T A3101 355 HMTREEMLTER 0.647 45 SB Large T A3101 205 RVSAINNFCQK 0.637 50 WB Large T A3101 558 LQNSEFLLEKR 0.626 57 WB Large T A3101 541 RFVRQIDFRPK 0.624 58 WB Large T A3101 20 RAAWGNLPLMR 0.617 63 WB Large T A3101 121 SQHSTPPKKKR 0.607 70 WB Large T A3101 621 CMGKCILDITR 0.587 87 WB Large T A3101 177 MEKYSVTFISR 0.582 91 WB Large T A3101 215 KLCTFSFLICK 0.554 124 WB Large T A3101 164 TTKEKAQILYK 0.536 151 WB Large T A3101 680 CFKRPKTPPPK 0.526 169 WB Large T A3101 534 VPKTLQARFVR 0.518 183 WB Large T A3101 193 HNIIFFLTPHR 0.500 223 WB Large T A3101 507 KVNLEKKHLNK 0.492 244 WB Large T A3101 306 CQKKDQPYHFK 0.486 259 WB Large T A3101 526 LVTMNEYPVPK 0.467 319 WB Large T A3101 229 KEYLLYSALTR 0.466 321 WB Large T A3101 593 IQSRIVEWKER 0.449 389 WB Large T A3101 31 KAYLKKCKEFH 0.448 392 WB Large T A3101 545 QIDFRPKIYLR 0.448 393 WB Large T A3101 401 KMDSVIFDFLH 0.443 415 WB Large T A3101 605 DSEISMYTFSR 0.438 435 WB Large T A3101 28 LMRKAYLKKCK 0.433 461 WB Large T A3101 574 MTLLLLLIWFR 0.838 5 SB Large T A3301 195 IIFFLTPHRHR 0.685 30 SB Large T A3301 605 DSEISMYTFSR 0.684 30 SB Large T A3301 539 QARFVRQIDFR 0.650 44 SB Large T A3301 145 QFLSQAVFSNR 0.639 49 SB Large T A3301 355 HMTREEMLTER 0.625 57 WB Large T A3301 673 HLCKGFQCFKR 0.606 70 WB Large T A3301 531 EYPVPKTLQAR 0.582 92 WB Large T A3301 545 QIDFRPKIYLR 0.484 264 WB Large T A3301 285 DVFLLLGMYLE 0.462 337 WB Large T A3301 416 NVPKRRYWLFK 0.441 424 WB Large T A3301 177 MEKYSVTFISR 0.440 428 WB Large T A3301 574 MTLLLLLIWFR 0.820 7 SB Large T A6801 607 EISMYTFSRMK 0.808 7 SB Large T A6801 322 FANAIIFAESK 0.780 10 SB Large T A6801 605 DSEISMYTFSR 0.765 12 SB Large T A6801 195 IIFFLTPHRHR 0.762 13 SB Large T A6801 156 TLACFAVYTTK 0.756 14 SB Large T A6801 205 RVSAINNFCQK 0.712 22 SB Large T A6801 539 QARFVRQIDFR 0.695 27 SB Large T A6801 219 FSFLICKGVNK 0.676 33 SB Large T A6801 193 HNIIFFLTPHR 0.673 34 SB Large T A6801 673 HLCKGFQCFKR 0.665 37 SB Large T A6801 164 TTKEKAQILYK 0.656 41 SB Large T A6801 355 HMTREEMLTER 0.654 42 SB Large T A6801 526 LVTMNEYPVPK 0.641 48 SB Large T A6801 416 NVPKRRYWLFK 0.635 51 WB Large T A6801 340 QAVDTVLAKKR 0.620 61 WB Large T A6801 409 FLHCVVFNVPK 0.589 85 WB Large T A6801 20 RAAWGNLPLMR 0.562 114 WB Large T A6801 325 AIIFAESKNQK 0.554 124 WB Large T A6801 56 TLYKKMEQDVK 0.549 131 WB Large T A6801 163 YTTKEKAQILY 0.548 132 WB Large T A6801 467 DQYMVVFEDVK 0.534 155 WB Large T A6801 391 GVAWLHCLLPK 0.521 178 WB Large T A6801 608 ISMYTFSRMKY 0.493 240 WB Large T A6801 295 EFQYNVEECKK 0.489 251 WB Large T A6801 25 NLPLMRKAYLK 0.482 272 WB Large T A6801 447 KALNVNLPMER 0.477 288 WB Large T A6801 545 QIDFRPKIYLR 0.471 305 WB Large T A6801 362 LTERFNHILDK 0.463 332 WB Large T A6801 177 MEKYSVTFISR 0.463 335 WB Large T A6801 145 QFLSQAVFSNR 0.460 343 WB Large T A6801 423 WLFKGPIDSGK 0.456 361 WB Large T A6801 118 TADSQHSTPPK 0.435 450 WB Large T A6801 557 SLQNSEFLLEK 0.430 477 WB Large T A6801 189 MCAGHNIIFFL 0.792 9 SB Large T A6802 217 CTFSFLICKGV 0.752 14 SB Large T A6802 404 SVIFDFLHCVV 0.734 17 SB Large T A6802 382 NAVLEQYMAGV 0.680 31 SB Large T A6802 403 DSVIFDFLHCV 0.654 42 SB Large T A6802 8 ESMELMDLLGL 0.653 42 SB Large T A6802 152 FSNRTLACFAV 0.617 62 WB Large T A6802 290 LGMYLEFQYNV 0.606 70 WB Large T A6802 462 LGVAIDQYMVV 0.591 83 WB Large T A6802 268 QVSWKLITEYA 0.576 98 WB Large T A6802 280 ETKCEDVFLLL 0.573 101 WB Large T A6802 11 ELMDLLGLERA 0.570 105 WB Large T A6802 234 YSALTRDPYHI 0.549 132 WB Large T A6802 388 YMAGVAWLHCL 0.531 159 WB Large T A6802 243 HIIEESIQGGL 0.507 206 WB Large T A6802 181 SVTFISRHMCA 0.503 216 WB Large T A6802 407 FDFLHCVVFNV 0.489 251 WB Large T A6802 374 DLIFGAHGNAV 0.480 277 WB Large T A6802 542 FVRQIDFRPKI 0.446 400 WB Large T A6802 212 FCQKLCTFSFL 0.433 460 WB Large T A6802 461 ELGVAIDQYMV 0.429 484 WB Large T A6802 388 YMAGVAWLHCL 0.652 42 SB Large T A6901 461 ELGVAIDQYMV 0.575 99 WB Large T A6901 374 DLIFGAHGNAV 0.573 102 WB Large T A6901 8 ESMELMDLLGL 0.560 116 WB Large T A6901 152 FSNRTLACFAV 0.541 143 WB Large T A6901 11 ELMDLLGLERA 0.539 145 WB Large T A6901 576 LLLLLIWFRPV 0.519 182 WB Large T A6901 404 SVIFDFLHCVV 0.512 196 WB Large T A6901 360 EMLTERFNHIL 0.498 228 WB Large T A6901 189 MCAGHNIIFFL 0.474 297 WB Large T A6901 243 HIIEESIQGGL 0.472 303 WB Large T A6901 382 NAVLEQYMAGV 0.470 309 WB Large T A6901 217 CTFSFLICKGV 0.457 355 WB Large T A6901 269 VSWKLITEYAV 0.443 414 WB Large T A6901 55 NTLYKKMEQDV 0.432 464 WB Large T A6901 532 YPVPKTLQARF 0.646 46 SB Large T B0702 553 YLRKSLQNSEF 0.492 244 WB Large T B0801 267 KQVSWKLITEY 0.566 109 WB Large T B1501 538 LQARFVRQIDF 0.565 110 WB Large T B1501 553 YLRKSLQNSEF 0.561 116 WB Large T B1501 188 HMCAGHNIIFF 0.554 124 WB Large T B1501 388 YMAGVAWLHCL 0.542 141 WB Large T B1501 221 FLICKGVNKEY 0.541 142 WB Large T B1501 544 RQIDFRPKIYL 0.521 178 WB Large T B1501 579 LLIWFRPVADF 0.518 183 WB Large T B1501 519 TQIFPPGLVTM 0.480 276 WB Large T B1501 232 LLYSALTRDPY 0.478 283 WB Large T B1501 405 VIFDFLHCVVF 0.474 295 WB Large T B1501 608 ISMYTFSRMKY 0.450 384 WB Large T B1501 150 AVFSNRTLACF 0.434 457 WB Large T B1501 570 LQSGMTLLLLL 0.429 483 WB Large T B1501 668 HSQELHLCKGF 0.426 495 WB Large T B1501 86 TEEWESWWSSF 0.650 44 SB Large T B1801 460 FELGVAIDQYM 0.643 47 SB Large T B1801 318 HEKHFANAIIF 0.625 57 WB Large T B1801 18 LERAAWGNLPL 0.572 102 WB Large T B1801 79 SEVPTYGTEEW 0.556 122 WB Large T B1801 601 KERLDSEISMY 0.505 210 WB Large T B1801 664 SENPHSQELHL 0.497 230 WB Large T B1801 532 YPVPKTLQARF 0.461 341 WB Large T B1801 614 SRMKYNICMGK 0.547 134 WB Large T B2705 567 KRILQSGMTLL 0.507 207 WB Large T B2705 544 RQIDFRPKIYL 0.450 382 WB Large T B2705 548 FRPKIYLRKSL 0.450 385 WB Large T B2705 522 FPPGLVTMNEY 0.812 7 SB Large T B3501 532 YPVPKTLQARF 0.780 10 SB Large T B3501 277 YAVETKCEDVF 0.742 16 SB Large T B3501 399 LPKMDSVIFDF 0.560 116 WB Large T B3501 41 HPDKGGDEDKM 0.545 136 WB Large T B3501 392 VAWLHCLLPKM 0.532 158 WB Large T B3501 139 FPSDLHQFLSQ 0.494 238 WB Large T B3501 232 LLYSALTRDPY 0.453 371 WB Large T B3501 459 TFELGVAIDQY 0.442 417 WB Large T B3501 317 YHEKHFANAII 0.586 88 WB Large T B3901 388 YMAGVAWLHCL 0.549 130 WB Large T B3901 6 REESMELMDLL 0.673 34 SB Large T B4001 664 SENPHSQELHL 0.668 36 SB Large T B4001 18 LERAAWGNLPL 0.630 54 WB Large T B4001 385 LEQYMAGVAWL 0.562 114 WB Large T B4001 460 FELGVAIDQYM 0.552 126 WB Large T B4001 279 VETKCEDVFLL 0.540 145 WB Large T B4001 606 SEISMYTFSRM 0.498 228 WB Large T B4001 133 VEDPKDFPSDL 0.446 399 WB Large T B4001 166 KEKAQILYKKL 0.440 428 WB Large T B4001 47 DEDKMKRMNTL 0.434 458 WB Large T B4001 664 SENPHSQELHL 0.540 144 WB Large T B4002 6 REESMELMDLL 0.511 198 WB Large T B4002 264 EETKQVSWKLI 0.502 219 WB Large T B4002 318 HEKHFANAIIF 0.459 347 WB Large T B4002 359 EEMLTERFNHI 0.445 403 WB Large T B4002 279 VETKCEDVFLL 0.432 464 WB Large T B4002 79 SEVPTYGTEEW 0.512 196 WB Large T B4402 261 EEPEETKQVSW 0.484 267 WB Large T B4402 561 SEFLLEKRILQ 0.477 287 WB Large T B4403 664 SENPHSQELHL 0.464 331 WB Large T B4403 606 SEISMYTFSRM 0.457 356 WB Large T B4403 79 SEVPTYGTEEW 0.452 375 WB Large T B4403 261 EEPEETKQVSW 0.438 438 WB Large T B4403 359 EEMLTERFNHI 0.482 271 WB Large T B4501 115 EEATADSQHST 0.450 383 WB Large T B4501 453 LPMERLTFELG 0.470 309 WB Large T B5101 532 YPVPKTLQARF 0.433 463 WB Large T B5101 522 FPPGLVTMNEY 0.689 28 SB Large T B5301 532 YPVPKTLQARF 0.645 46 SB Large T B5301 399 LPKMDSVIFDF 0.555 122 WB Large T B5301 277 YAVETKCEDVF 0.474 296 WB Large T B5301 453 LPMERLTFELG 0.580 93 WB Large T B5401 522 FPPGLVTMNEY 0.544 138 WB Large T B5401 427 GPIDSGKTTLA 0.508 204 WB Large T B5401 82 PTYGTEEWESW 0.576 98 WB Large T B5701 90 ESWWSSFNEKW 0.678 32 SB Large T B5801 66 KVAHQPDFGTW 0.658 40 SB Large T B5801 572 SGMTLLLLLIW 0.539 146 WB Large T B5801 413 VVFNVPKRRYW 0.527 167 WB Large T B5801 277 YAVETKCEDVF 0.495 235 WB Large T B5801 608 ISMYTFSRMKY 0.487 258 WB Large T B5801 82 PTYGTEEWESW 0.458 353 WB Large T B5801 SEQ ID NOS.: 55454-58054

Preferred BK virus fragments of agnoprotein capable of interacting with one or more MHC class 1 molecules are listed in Table N.

TABLE N Prediction of BK virus Agnoprotein specific MHC class1, 8-, 9-, 10-, 11-mer peptide binders for 42 MHC class 1 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHC/ database. The MHC class 1 molecules for which no binders were found are not listed. Pro- affinity Bind tein pos peptide logscore (nM) Level Name Allele 8-mers 36 FIFILELL 0.641 48 SB Agno A0201 59 STTALPAV 0.453 373 WB Agno A0201 36 FIFILELL 0.785 10 SB Agno A0202 12 QLSRQASV 0.702 25 SB Agno A0202 12 QLSRQASV 0.712 22 SB Agno A0203 59 STTALPAV 0.537 149 WB Agno A0203 36 FIFILELL 0.524 171 WB Agno A0203 32 AQRIFIFI 0.503 216 WB Agno A0203 6 NLVVLRQL 0.431 473 WB Agno A0203 12 QLSRQASV 0.508 206 WB Agno A0204 59 STTALPAV 0.489 252 WB Agno A0204 32 AQRIFIFI 0.646 46 SB Agno A0206 36 FIFILELL 0.585 89 WB Agno A0206 59 STTALPAV 0.582 92 WB Agno A0206 12 QLSRQASV 0.479 281 WB Agno A0206 38 FILELLLE 0.474 297 WB Agno A0206 — 12 QLSRQASV 0.883 3 SB Agno A0211 36 FIFILELL 0.782 10 SB Agno A0211 59 STTALPAV 0.695 27 SB Agno A0211 6 NLVVLRQL 0.688 29 SB Agno A0211 12 QLSRQASV 0.825 6 SB Agno A0212 36 FIFILELL 0.705 24 SB Agno A0212 59 STTALPAV 0.504 214 WB Agno A0212 46 FCRGEDSV 0.502 219 WB Agno A0212 12 QLSRQASV 0.877 3 SB Agno A0216 36 FIFILELL 0.643 47 SB Agno A0216 6 NLVVLRQL 0.580 93 WB Agno A0216 59 STTALPAV 0.474 294 WB Agno A0216 1 FCEPKNLV 0.427 494 WB Agno A0216 12 QLSRQASV 0.746 15 SB Agno A0219 59 STTALPAV 0.455 364 WB Agno A0219 23 KTWTGTKK 0.662 38 SB Agno A0301 60 TTALPAVK 0.568 107 WB Agno A0301 8 VVLRQLSR 0.444 408 WB Agno A0301 13 LSRQASVK 0.436 444 WB Agno A0301 60 TTALPAVK 0.785 10 SB Agno A1101 23 KTWTGTKK 0.637 50 WB Agno A1101 8 VVLRQLSR 0.554 124 WB Agno A1101 16 QASVKVGK 0.458 351 WB Agno A1101 35 IFIFILEL 0.573 101 WB Agno A2301 31 RAQRIFIF 0.514 191 WB Agno A2301 37 IFILELLL 0.454 367 WB Agno A2301 37 IFILELLL 0.536 150 WB Agno A2402 35 IFIFILEL 0.478 284 WB Agno A2402 31 RAQRIFIF 0.431 472 WB Agno A2402 31 RAQRIFIF 0.449 386 WB Agno A2403 13 LSRQASVK 0.690 28 SB Agno A3001 23 KTWTGTKK 0.659 40 SB Agno A3001 27 GTKKRAQR 0.803 8 SB Agno A3101 23 KTWTGTKK 0.648 45 SB Agno A3101 8 VVLRQLSR 0.587 87 WB Agno A3101 41 ELLLEFCR 0.701 25 SB Agno A3301 27 GTKKRAQR 0.564 111 WB Agno A3301 8 VVLRQLSR 0.466 323 WB Agno A3301 60 TTALPAVK 0.774 11 SB Agno A6801 41 ELLLEFCR 0.627 56 WB Agno A6801 27 GTKKRAQR 0.537 150 WB Agno A6801 16 QASVKVGK 0.459 349 WB Agno A6801 51 DSVDGKNK 0.431 473 WB Agno A6801 59 STTALPAV 0.655 42 SB Agno A6802 33 QRIFIFIL 0.552 127 WB Agno A6802 36 FIFILELL 0.512 195 WB Agno A6802 59 STTALPAV 0.674 34 SB Agno A6901 36 FIFILELL 0.441 424 WB Agno A6901 63 LPAVKDSV 0.582 91 WB Agno B0702 3 EPKNLVVL 0.427 490 WB Agno B0702 33 QRIFIFIL 0.431 472 WB Agno B2705 3 EPKNLVVL 0.518 184 WB Agno B3501 63 LPAVKDSV 0.585 88 WB Agno B5101 3 EPKNLVVL 0.456 358 WB Agno B5301 63 LPAVKDSV 0.745 15 SB Agno B5401 31 RAQRIFIF 0.503 215 WB Agno B5801 9-mers 34 RIFIFILEL 0.674 34 SB Agno A0201 36 FIFILELLL 0.613 66 WB Agno A0201 11 RQLSRQASV 0.561 115 WB Agno A0201 62 ALPAVKDSV 0.503 215 WB Agno A0201 38 FILELLLEF 0.448 392 WB Agno A0201 36 FIFILELLL 0.698 26 SB Agno A0202 62 ALPAVKDSV 0.609 68 WB Agno A0202 34 RIFIFILEL 0.540 144 WB Agno A0202 11 RQLSRQASV 0.688 29 SB Agno A0203 62 ALPAVKDSV 0.667 36 SB Agno A0203 9 VLRQLSRQA 0.455 362 WB Agno A0203 34 RIFIFILEL 0.439 433 WB Agno A0203 62 ALPAVKDSV 0.515 190 WB Agno A0204 11 RQLSRQASV 0.855 4 SB Agno A0206 38 FILELLLEF 0.731 18 SB Agno A0206 62 ALPAVKDSV 0.588 86 WB Agno A0206 32 AQRIFIFIL 0.561 116 WB Agno A0206 58 KSTTALPAV 0.559 118 WB Agno A0206 34 RIFIFILEL 0.506 208 WB Agno A0206 31 RAQRIFIFI 0.487 256 WB Agno A0206 36 FIFILELLL 0.455 365 WB Agno A0206 62 ALPAVKDSV 0.927 2 SB Agno A0211 34 RIFIFILEL 0.836 5 SB Agno A0211 36 FIFILELLL 0.796 9 SB Agno A0211 38 FILELLLEF 0.621 60 WB Agno A0211 9 VLRQLSRQA 0.546 135 WB Agno A0211 11 RQLSRQASV 0.445 405 WB Agno A0211 62 ALPAVKDSV 0.904 2 SB Agno A0212 36 FIFILELLL 0.746 15 SB Agno A0212 34 RIFIFILEL 0.679 32 SB Agno A0212 38 FILELLLEF 0.614 65 WB Agno A0212 11 RQLSRQASV 0.545 138 WB Agno A0212 1 FCEPKNLVV 0.473 300 WB Agno A0212 42 LLLEFCRGE 0.465 327 WB Agno A0212 9 VLRQLSRQA 0.442 416 WB Agno A0212 62 ALPAVKDSV 0.922 2 SB Agno A0216 34 RIFIFILEL 0.732 18 SB Agno A0216 36 FIFILELLL 0.654 42 SB Agno A0216 11 RQLSRQASV 0.490 247 WB Agno A0216 62 ALPAVKDSV 0.778 11 SB Agno A0219 12 QLSRQASVK 0.643 47 SB Agno A0301 15 RQASVKVGK 0.538 148 WB Agno A0301 59 STTALPAVK 0.461 341 WB Agno A0301 59 STTALPAVK 0.825 6 SB Agno A1101 15 RQASVKVGK 0.624 58 WB Agno A1101 7 LVVLRQLSR 0.460 345 WB Agno A1101 35 IFIFILELL 0.514 192 WB Agno A2301 38 FILELLLEF 0.473 300 WB Agno A2301 35 IFIFILELL 0.610 67 WB Agno A2402 38 FILELLLEF 0.532 157 WB Agno A2403 38 FILELLLEF 0.598 77 WB Agno A2602 38 FILELLLEF 0.463 334 WB Agno A2902 21 VGKTWTGTK 0.528 165 WB Agno A3001 59 STTALPAVK 0.477 285 WB Agno A3001 29 KKRAQRIFI 0.452 377 WB Agno A3001 23 KTWTGTKKR 0.727 19 SB Agno A3101 15 RQASVKVGK 0.617 62 WB Agno A3101 26 TGTKKRAQR 0.524 172 WB Agno A3101 7 LVVLRQLSR 0.506 210 WB Agno A3101 59 STTALPAVK 0.486 260 WB Agno A3101 7 LVVLRQLSR 0.666 37 SB Agno A3301 3 EPKNLVVLR 0.510 201 WB Agno A3301 59 STTALPAVK 0.728 19 SB Agno A6801 3 EPKNLVVLR 0.667 36 SB Agno A6801 7 LVVLRQLSR 0.664 37 SB Agno A6801 31 RAQRIFIFI 0.609 68 WB Agno A6802 38 FILELLLEF 0.453 371 WB Agno B1801 15 RQASVKVGK 0.566 109 WB Agno B2705 30 KRAQRIFIF 0.523 174 WB Agno B2705 11 RQLSRQASV 0.449 390 WB Agno B2705 3 38 FILELLLEF 0.505 211 WB Agno B3501 2 CEPKNLVVL 0.521 179 WB Agno B4001 17 ASVKVGKTW 0.443 414 WB Agno B5701 17 ASVKVGKTW 0.572 103 WB Agno B5801 10-mers 34 RIFIFILELL 0.605 71 WB Agno A0201 38 FILELLLEFC 0.449 388 WB Agno A0201 34 RIFIFILELL 0.719 20 SB Agno A0202 38 FILELLLEFC 0.622 59 WB Agno A0202 12 QLSRQASVKV 0.449 386 WB Agno A0202 12 QLSRQASVKV 0.588 86 WB Agno A0203 34 RIFIFILELL 0.456 359 WB Agno A0203 12 QLSRQASVKV 0.503 215 WB Agno A0204 38 FILELLLEFC 0.656 41 SB Agno A0206 34 RIFIFILELL 0.549 131 WB Agno A0206 61 TALPAVKDSV 0.450 382 WB Agno A0206 12 QLSRQASVKV 0.859 4 SB Agno A0211 34 RIFIFILELL 0.772 11 SB Agno A0211 38 FILELLLEFC 0.626 57 WB Agno A0211 61 TALPAVKDSV 0.569 106 WB Agno A0211 12 QLSRQASVKV 0.754 14 SB Agno A0212 38 FILELLLEFC 0.627 56 WB Agno A0212 34 RIFIFILELL 0.497 231 WB Agno A0212 61 TALPAVKDSV 0.433 461 WB Agno A0212 12 QLSRQASVKV 0.843 5 SB Agno A0216 34 RIFIFILELL 0.581 92 WB Agno A0216 61 TALPAVKDSV 0.550 130 WB Agno A0216 12 QLSRQASVKV 0.632 53 WB Agno A0219 61 TALPAVKDSV 0.549 131 WB Agno A0219 11 RQLSRQASVK 0.636 51 WB Agno A0301 58 KSTTALPAVK 0.532 158 WB Agno A0301 20 KVGKTWTGTK 0.496 234 WB Agno A0301 62 ALPAVKDSVK 0.452 375 WB Agno A0301 58 KSTTALPAVK 0.688 29 SB Agno A1101 20 KVGKTWTGTK 0.671 35 SB Agno A1101 11 RQLSRQASVK 0.620 60 WB Agno A1101 62 ALPAVKDSVK 0.445 404 WB Agno A1101 37 IFILELLLEF 0.695 27 SB Agno A2301 35 IFIFILELLL 0.487 256 WB Agno A2301 37 IFILELLLEF 0.663 38 SB Agno A2402 35 IFIFILELLL 0.622 59 WB Agno A2402 37 IFILELLLEF 0.663 38 SB Agno A2403 37 IFILELLLEF 0.470 309 WB Agno A2902 20 KVGKTWTGTK 0.787 10 SB Agno A3001 58 KSTTALPAVK 0.557 120 WB Agno A3001 11 RQLSRQASVK 0.509 202 WB Agno A3001 6 NLVVLRQLSR 0.567 108 WB Agno A3101 39 ILELLLEFCR 0.521 177 WB Agno A3101 25 WTGTKKRAQR 0.504 214 WB Agno A3101 39 ILELLLEFCR 0.523 173 WB Agno A3301 6 NLVVLRQLSR 0.485 262 WB Agno A3301 6 NLVVLRQLSR 0.604 72 WB Agno A6801 39 ILELLLEFCR 0.479 279 WB Agno A6801 25 WTGTKKRAQR 0.465 326 WB Agno A6801 33 QRIFIFILEL 0.528 164 WB Agno A6802 61 TALPAVKDSV 0.473 301 WB Agno A6802 34 RIFIFILELL 0.467 321 WB Agno A6802 61 TALPAVKDSV 0.448 394 WB Agno A6901 11 RQLSRQASVK 0.534 154 WB Agno B2705 14 SRQASVKVGK 0.516 188 WB Agno B2705 33 QRIFIFILEL 0.469 312 WB Agno B2705 16 QASVKVGKTW 0.632 53 WB Agno B5801 11-mers 34 RIFIFILELLL 0.552 127 WB Agno A0201 11 RQLSRQASVKV 0.460 344 WB Agno A0201 43 LLEFCRGEDSV 0.586 87 WB Agno A0202 34 RIFIFILELLL 0.503 216 WB Agno A0202 9 VLRQLSRQASV 0.497 229 WB Agno A0202 9 VLRQLSRQASV 0.814 7 SB Agno A0203 11 RQLSRQASVKV 0.508 205 WB Agno A0203 43 LLEFCRGEDSV 0.483 267 WB Agno A0203 32 AQRIFIFILEL 0.446 400 WB Agno A0203 9 VLRQLSRQASV 0.447 398 WB Agno A0204 11 RQLSRQASVKV 0.776 11 SB Agno A0206 32 AQRIFIFILEL 0.584 90 WB Agno A0206 9 VLRQLSRQASV 0.887 3 SB Agno A0211 34 RIFIFILELLL 0.793 9 SB Agno A0211 43 LLEFCRGEDSV 0.747 15 SB Agno A0211 52 SVDGKNKSTTA 0.612 66 WB Agno A0211 11 RQLSRQASVKV 0.433 463 WB Agno A0211 36 FIFILELLLEF 0.429 481 WB Agno A0211 9 VLRQLSRQASV 0.876 3 SB Agno A0212 34 RIFIFILELLL 0.586 88 WB Agno A0212 43 LLEFCRGEDSV 0.585 89 WB Agno A0212 38 FILELLLEFCR 0.454 369 WB Agno A0212 11 RQLSRQASVKV 0.442 417 WB Agno A0212 9 VLRQLSRQASV 0.838 5 SB Agno A0216 43 LLEFCRGEDSV 0.725 19 SB Agno A0216 34 RIFIFILELLL 0.606 71 WB Agno A0216 60 TTALPAVKDSV 0.460 346 WB Agno A0216 52 SVDGKNKSTTA 0.455 365 WB Agno A0216 9 VLRQLSRQASV 0.674 33 SB Agno A0219 43 LLEFCRGEDSV 0.477 285 WB Agno A0219 20 KVGKTWTGTKK 0.660 39 SB Agno A0301 20 KVGKTWTGTKK 0.617 63 WB Agno A1101 61 TALPAVKDSVK 0.508 204 WB Agno A1101 36 FIFILELLLEF 0.535 152 WB Agno A2602 36 FIFILELLLEF 0.571 103 WB Agno A2902 13 LSRQASVKVGK 0.753 14 SB Agno A3001 20 KVGKTWTGTKK 0.713 22 SB Agno A3001 5 KNLVVLRQLSR 0.558 119 WB Agno A3101 24 TWTGTKKRAQR 0.496 232 WB Agno A3101 38 FILELLLEFCR 0.469 313 WB Agno A3101 38 FILELLLEFCR 0.616 63 WB Agno A3301 38 FILELLLEFCR 0.611 67 WB Agno A6801 24 TWTGTKKRAQR 0.442 419 WB Agno A6801 61 TALPAVKDSVK 0.439 434 WB Agno A6801 60 TTALPAVKDSV 0.850 5 SB Agno A6802 33 QRIFIFILELL 0.650 43 SB Agno A6802 60 TTALPAVKDSV 0.545 136 WB Agno A6901 32 AQRIFIFILEL 0.471 305 WB Agno B1501 36 FIFILELLLEF 0.436 448 WB Agno B1501 15 RQASVKVGKTW 0.427 491 WB Agno B1501 30 KRAQRIFIFIL 0.478 284 WB Agno B2705 36 FIFILELLLEF 0.451 378 WB Agno B3501 30 KRAQRIFIFIL 0.455 362 WB Agno B3901 15 RQASVKVGKTW 0.573 100 WB Agno B5801 SEQ ID NOS: 58055-58311

Preferred BK virus fragments capable of interacting with one or more MHC class 2 molecules are listed in Table O.

TABLE O Predicted MHC class 2 BK virus peptide sequences. Prediction of 13-, 14-, 15-,16-mers from all 6 reading frames of the genome (access no #V01108) obtained using the program displayed in FIG. 2. BK virus, reading frame 1 13 mers: FCKNCKRIGISPN; CKNCKRIGISPNS; KNCKRIGISPNSF; NCKRIGISPNSFA; CKRIGISPNSFAR; KRIGISPNSFARP; RIGISPNSFARPQ; IGISPNSFARPQK; GISPNSFARPQKK; ISPNSFARPQKKP; SPNSFARPQKKPP; PNSFARPQKKPPH; NSFARPQKKPPHP; SFARPQKKPPHPY; FARPQKKPPHPYY; ARPQKKPPHPYYL; RPQKKPPHPYYLR; PQKKPPHPYYLRE; QKKPPHPYYLRER; KKPPHPYYLRERV; KPPHPYYLRERVE; PPHPYYLRERVEA; PHPYYLRERVEAE; HPYYLRERVEAEA; PYYLRERVEAEAA; YYLRERVEAEAAS; YLRERVEAEAASA; LRERVEAEAASAS; RERVEAEAASASY; ERVEAEAASASYI; RVEAEAASASYIL; KKRPQGGAAYPWN; KRPQGGAAYPWNA; RPQGGAAYPWNAA; PQGGAAYPWNAAK; QGGAAYPWNAAKP; PQEGKCMTHRGMQ; QEGKCMTHRGMQP; EGKCMTHRGMQPN; GKCMTHRGMQPNH; KCMTHRGMQPNHD; CMTHRGMQPNHDL; MTHRGMQPNHDLR; THRGMQPNHDLRK; HRGMQPNHDLRKE; RGMQPNHDLRKES; GMQPNHDLRKESA; LTGRSCLPMECSQ; TGRSCLPMECSQT; GRSCLPMECSQTM; RSCLPMECSQTMT; SCLPMECSQTMTS; CLPMECSQTMTSG; LPMECSQTMTSGR; PMECSQTMTSGRK; MECSQTMTSGRKV; ECSQTMTSGRKVH; CSQTMTSGRKVHD; SQTMTSGRKVHDR; QTMTSGRKVHDRH; TMTSGRKVHDRHV; MTSGRKVHDRHVL; TSGRKVHDRHVLR; SGRKVHDRHVLRA; ESWPCPQLNWTKA; SWPCPQLNWTKAM; WPCPQLNWTKAMV; PCPQLNWTKAMVL; CPQLNWTKAMVLR; PQLNWTKAMVLRQ; QLNWTKAMVLRQL; LNWTKAMVLRQLS; NWTKAMVLRQLSR; WTKAMVLRQLSRQ; TKAMVLRQLSRQA; KAMVLRQLSRQAS; AMVLRQLSRQASV; MVLRQLSRQASVK; VLRQLSRQASVKV; LRQLSRQASVKVG; RQLSRQASVKVGK; QLSRQASVKVGKT; LSRQASVKVGKTW; SRQASVKVGKTWT; RQASVKVGKTWTG; QASVKVGKTWTGT; ASVKVGKTWTGTK; SVKVGKTWTGTKK; VKVGKTWTGTKKR; KVGKTWTGTKKRA; VGKTWTGTKKRAQ; GKTWTGTKKRAQR; KTWTGTKKRAQRI; TWTGTKKRAQRIF; WTGTKKRAQRIFI; TGTKKRAQRIFIF; GTKKRAQRIFIFI; TKKRAQRIFIFIL; KKRAQRIFIFILE; KRAQRIFIFILEL; RAQRIFIFILELL; AQRIFIFILELLL; QRIFIFILELLLE; RIFIFILELLLEF; IFIFILELLLEFC; FIFILELLLEFCR; IFILELLLEFCRG; FILELLLEFCRGE; ILELLLEFCRGED; LELLLEFCRGEDS; ELLLEFCRGEDSV; LLLEFCRGEDSVD; LLEFCRGEDSVDG; LEFCRGEDSVDGK; EFCRGEDSVDGKN; FCRGEDSVDGKNK; CRGEDSVDGKNKS; RGEDSVDGKNKST; GEDSVDGKNKSTT; EDSVDGKNKSTTA; DSVDGKNKSTTAL; SVDGKNKSTTALP; VDGKNKSTTALPA; DGKNKSTTALPAV; GKNKSTTALPAVK; KNKSTTALPAVKD; NKSTTALPAVKDS; KSTTALPAVKDSV; STTALPAVKDSVK; TTALPAVKDSVKD; TALPAVKDSVKDS; VSNPFFFVFPGSW; SNPFFFVFPGSWV; NPFFFVFPGSWVL; PFFFVFPGSWVLL; LPVYLRLLLPQDF; PVYLRLLLPQDFQ; VYLRLLLPQDFQW; YLRLLLPQDFQWL; LRLLLPQDFQWLK; RLLLPQDFQWLKL; LLLPQDFQWLKLL; LLPQDFQWLKLLL; LPQDFQWLKLLLG; PQDFQWLKLLLGR; QDFQWLKLLLGRL; DFQWLKLLLGRLL; FQWLKLLLGRLLL; QWLKLLLGRLLLL; LLVLLGLLLGLLL; GISSLMIGITKFP; ISSLMIGITKFPL; ASISNQAWLWNCL; SISNQAWLWNCLT; ISNQAWLWNCLTQ; SNQAWLWNCLTQM; NQAWLWNCLTQMS; QAWLWNCLTQMST; AWLWNCLTQMSTM; WLWNCLTQMSTMI; LWNCLTQMSTMIF; WNCLTQMSTMIFC; NCLTQMSTMIFCF; CLTQMSTMIFCFL; LTQMSTMIFCFLV; ILLLIIFNTLILG; LLLIIFNTLILGI; LLIIFNTLILGIG; LIIFNTLILGIGV; IIFNTLILGIGVL; IFNTLILGIGVLL; FNTLILGIGVLLC; NTLILGIGVLLCL; TLILGIGVLLCLL; LILGIGVLLCLLL; ILGIGVLLCLLLF; LGIGVLLCLLLFP; GIGVLLCLLLFPR; IGVLLCLLLFPRL; GVLLCLLLFPRLC; VLLCLLLFPRLCG; LLCLLLFPRLCGM; LCLLLFPRLCGML; CLLLFPRLCGMLL; LLLFPRLCGMLLG; LLFPRLCGMLLGM; LFPRLCGMLLGMI; FPRLCGMLLGMIY; PRLCGMLLGMIYL; RLCGMLLGMIYLL; PHRNCREEQKDFL; HRNCREEQKDFLE; RNCREEQKDFLET; NCREEQKDFLETP; CREEQKDFLETPW; REEQKDFLETPWL; EEQKDFLETPWLD; EQKDFLETPWLDF; QKDFLETPWLDFW; KDFLETPWLDFWR; DFLETPWLDFWRK; FLETPWLDFWRKL; LETPWLDFWRKLP; ETPWLDFWRKLPG; TPWLDFWRKLPGQ; PWLDFWRKLPGQL; TFIIIFNNIILIF; FIIIFNNIILIFP; IIIFNNIILIFPL; IIFNNIILIFPLL; IFNNIILIFPLLG; FNNIILIFPLLGP; NNIILIFPLLGPQ; NIILIFPLLGPQW; IILIFPLLGPQWL; ILIFPLLGPQWLD; LIFPLLGPQWLDK; LKGKVPVYILAIL; KGKVPVYILAILI; GKVPVYILAILIV; KKLLPQEVLIKEL; KLLPQEVLIKELL; LLPQEVLIKELLL; LPQEVLIKELLLN; PQEVLIKELLLNG; QEVLIKELLLNGC; EVLIKELLLNGCC; VLIKELLLNGCCL; LIKELLLNGCCLY; IKELLLNGCCLYF; HLLLKHMKMAPTK; LLLKHMKMAPTKR; LLKHMKMAPTKRK; LKHMKMAPTKRKG; KHMKMAPTKRKGE; HMKMAPTKRKGEC; MKMAPTKRKGECP; KMAPTKRKGECPG; MAPTKRKGECPGA; APTKRKGECPGAA; PTKRKGECPGAAP; TKRKGECPGAAPK; KRKGECPGAAPKK; RKGECPGAAPKKP; KGECPGAAPKKPK; GECPGAAPKKPKE; ECPGAAPKKPKEP; CPGAAPKKPKEPV; PGAAPKKPKEPVQ; GAAPKKPKEPVQV; AAPKKPKEPVQVP; APKKPKEPVQVPK; PKKPKEPVQVPKL; KKPKEPVQVPKLL; KPKEPVQVPKLLI; PKEPVQVPKLLIK; KEPVQVPKLLIKG; EPVQVPKLLIKGG; PVQVPKLLIKGGV; VQVPKLLIKGGVE; QVPKLLIKGGVEV; VPKLLIKGGVEVL; PKLLIKGGVEVLE; KLLIKGGVEVLEV; LLIKGGVEVLEVK; LIKGGVEVLEVKT; IKGGVEVLEVKTG; KGGVEVLEVKTGV; GGVEVLEVKTGVD; GVEVLEVKTGVDA; VEVLEVKTGVDAI; EVLEVKTGVDAIT; VLEVKTGVDAITE; LEVKTGVDAITEV; EVKTGVDAITEVE; VKTGVDAITEVEC; KTGVDAITEVECF; TGVDAITEVECFL; GVDAITEVECFLN; VDAITEVECFLNP; DAITEVECFLNPE; AITEVECFLNPEM; ITEVECFLNPEMG; TEVECFLNPEMGD; EVECFLNPEMGDP; VECFLNPEMGDPD; ECFLNPEMGDPDE; CFLNPEMGDPDEN; FLNPEMGDPDENL; LNPEMGDPDENLR; NPEMGDPDENLRG; PEMGDPDENLRGF; EMGDPDENLRGFS; MGDPDENLRGFSL; GDPDENLRGFSLK; DPDENLRGFSLKL; PDENLRGFSLKLS; DENLRGFSLKLSA; ENLRGFSLKLSAE; NLRGFSLKLSAEN; LRGFSLKLSAEND; RGFSLKLSAENDF; GFSLKLSAENDFS; FSLKLSAENDFSS; SLKLSAENDFSSD; LKLSAENDFSSDS; KLSAENDFSSDSP; LSAENDFSSDSPE; SAENDFSSDSPER; AENDFSSDSPERK; ENDFSSDSPERKM; NDFSSDSPERKML; DFSSDSPERKMLP; FSSDSPERKMLPC; SSDSPERKMLPCY; SDSPERKMLPCYS; DSPERKMLPCYST; SPERKMLPCYSTA; PERKMLPCYSTAR; ERKMLPCYSTARI; RKMLPCYSTARIP; KMLPCYSTARIPL; MLPCYSTARIPLP; LPCYSTARIPLPN; PCYSTARIPLPNL; CYSTARIPLPNLN; YSTARIPLPNLNE; STARIPLPNLNED; TARIPLPNLNEDL; ARIPLPNLNEDLT; RIPLPNLNEDLTC; IPLPNLNEDLTCG; PLPNLNEDLTCGN; LPNLNEDLTCGNL; PNLNEDLTCGNLL; NLNEDLTCGNLLM; LNEDLTCGNLLMW; NEDLTCGNLLMWE; EDLTCGNLLMWEA; DLTCGNLLMWEAV; LTCGNLLMWEAVT; TCGNLLMWEAVTV; CGNLLMWEAVTVQ; GNLLMWEAVTVQT; NLLMWEAVTVQTE; LLMWEAVTVQTEV; LMWEAVTVQTEVI; MWEAVTVQTEVIG; WEAVTVQTEVIGI; EAVTVQTEVIGIT; AVTVQTEVIGITS; VTVQTEVIGITSM; TVQTEVIGITSML; VQTEVIGITSMLN; QTEVIGITSMLNL; TEVIGITSMLNLH; EVIGITSMLNLHA; VIGITSMLNLHAG; IGITSMLNLHAGS; GITSMLNLHAGSQ; ITSMLNLHAGSQK; TSMLNLHAGSQKV; SMLNLHAGSQKVH; MLNLHAGSQKVHE; LNLHAGSQKVHEH; NLHAGSQKVHEHG; LHAGSQKVHEHGG; HAGSQKVHEHGGG; AGSQKVHEHGGGK; GSQKVHEHGGGKP; SQKVHEHGGGKPI; QKVHEHGGGKPIQ; KVHEHGGGKPIQG; VHEHGGGKPIQGS; HEHGGGKPIQGSN; EHGGGKPIQGSNF; HGGGKPIQGSNFH; GGGKPIQGSNFHF; GGKPIQGSNFHFF; GKPIQGSNFHFFA; KPIQGSNFHFFAV; PIQGSNFHFFAVG; IQGSNFHFFAVGG; QGSNFHFFAVGGE; GSNFHFFAVGGEP; SNFHFFAVGGEPL; NFHFFAVGGEPLE; FHFFAVGGEPLEM; HFFAVGGEPLEMQ; FFAVGGEPLEMQG; FAVGGEPLEMQGV; AVGGEPLEMQGVL; VGGEPLEMQGVLM; GGEPLEMQGVLMN; GEPLEMQGVLMNY; EPLEMQGVLMNYR; PLEMQGVLMNYRS; LEMQGVLMNYRSK; EMQGVLMNYRSKY; MQGVLMNYRSKYP; QGVLMNYRSKYPD; GVLMNYRSKYPDG; VLMNYRSKYPDGT; LMNYRSKYPDGTI; MNYRSKYPDGTIT; NYRSKYPDGTITP; YRSKYPDGTITPK; RSKYPDGTITPKN; SKYPDGTITPKNP; KYPDGTITPKNPT; YPDGTITPKNPTA; PDGTITPKNPTAQ; DGTITPKNPTAQS; GTITPKNPTAQSQ; TITPKNPTAQSQV; ITPKNPTAQSQVM; TPKNPTAQSQVMN; PKNPTAQSQVMNT; KNPTAQSQVMNTD; NPTAQSQVMNTDH; PTAQSQVMNTDHK; TAQSQVMNTDHKA; AQSQVMNTDHKAY; QSQVMNTDHKAYL; SQVMNTDHKAYLD; QVMNTDHKAYLDK; VMNTDHKAYLDKN; MNTDHKAYLDKNN; NTDHKAYLDKNNA; TDHKAYLDKNNAY; DHKAYLDKNNAYP; HKAYLDKNNAYPV; KAYLDKNNAYPVE; AYLDKNNAYPVEC; YLDKNNAYPVECW; LDKNNAYPVECWV; DKNNAYPVECWVP; KNNAYPVECWVPD; NNAYPVECWVPDP; NAYPVECWVPDPS; AYPVECWVPDPSR; YPVECWVPDPSRN; PVECWVPDPSRNE; VECWVPDPSRNEN; ECWVPDPSRNENA; CWVPDPSRNENAR; WVPDPSRNENARY; VPDPSRNENARYF; PDPSRNENARYFG; DPSRNENARYFGT; PSRNENARYFGTF; SRNENARYFGTFT; RNENARYFGTFTG; NENARYFGTFTGG; ENARYFGTFTGGE; NARYFGTFTGGEN; ARYFGTFTGGENV; RYFGTFTGGENVP; YFGTFTGGENVPP; FGTFTGGENVPPV; GTFTGGENVPPVL; TFTGGENVPPVLH; FTGGENVPPVLHV; TGGENVPPVLHVT; GGENVPPVLHVTN; GENVPPVLHVTNT; ENVPPVLHVTNTA; NVPPVLHVTNTAT; VPPVLHVTNTATT; PPVLHVTNTATTV; PVLHVTNTATTVL; VLHVTNTATTVLL; LHVTNTATTVLLD; HVTNTATTVLLDE; VTNTATTVLLDEQ; TNTATTVLLDEQG; NTATTVLLDEQGV; TATTVLLDEQGVG; ATTVLLDEQGVGP; TTVLLDEQGVGPL; TVLLDEQGVGPLC; VLLDEQGVGPLCK; LLDEQGVGPLCKA; LDEQGVGPLCKAD; DEQGVGPLCKADS; EQGVGPLCKADSL; QGVGPLCKADSLY; GVGPLCKADSLYV; VGPLCKADSLYVS; GPLCKADSLYVSA; PLCKADSLYVSAA; LCKADSLYVSAAD; CKADSLYVSAADI; KADSLYVSAADIC; ADSLYVSAADICG; DSLYVSAADICGL; SLYVSAADICGLF; LYVSAADICGLFT; YVSAADICGLFTN; VSAADICGLFTNS; SAADICGLFTNSS; AADICGLFTNSSG; ADICGLFTNSSGT; DICGLFTNSSGTQ; ICGLFTNSSGTQQ; CGLFTNSSGTQQW; GLFTNSSGTQQWR; LFTNSSGTQQWRG; FTNSSGTQQWRGL; TNSSGTQQWRGLA; NSSGTQQWRGLAR; SSGTQQWRGLARY; SGTQQWRGLARYF; GTQQWRGLARYFK; TQQWRGLARYFKI; QQWRGLARYFKIR; QWRGLARYFKIRL; WRGLARYFKIRLR; RGLARYFKIRLRK; GLARYFKIRLRKR; LARYFKIRLRKRS; ARYFKIRLRKRSV; RYFKIRLRKRSVK; YFKIRLRKRSVKN; FKIRLRKRSVKNP; KIRLRKRSVKNPY; IRLRKRSVKNPYP; RLRKRSVKNPYPI; LRKRSVKNPYPIS; RKRSVKNPYPISF; KRSVKNPYPISFL; RSVKNPYPISFLL; SVKNPYPISFLLS; VKNPYPISFLLSD; KNPYPISFLLSDL; NPYPISFLLSDLI; PYPISFLLSDLIN; YPISFLLSDLINR; PISFLLSDLINRR; ISFLLSDLINRRT; SFLLSDLINRRTQ; FLLSDLINRRTQR; LLSDLINRRTQRV; LSDLINRRTQRVD; SDLINRRTQRVDG; DLINRRTQRVDGQ; LINRRTQRVDGQP; INRRTQRVDGQPM; NRRTQRVDGQPMY; RRTQRVDGQPMYG; RTQRVDGQPMYGM; TQRVDGQPMYGME; QRVDGQPMYGMES; RVDGQPMYGMESQ; VDGQPMYGMESQV; DGQPMYGMESQVE; GQPMYGMESQVEE; QPMYGMESQVEEV; PMYGMESQVEEVR; MYGMESQVEEVRV; YGMESQVEEVRVF; GMESQVEEVRVFD; MESQVEEVRVFDG; ESQVEEVRVFDGT; SQVEEVRVFDGTE; QVEEVRVFDGTER; VEEVRVFDGTERL; EEVRVFDGTERLP; EVRVFDGTERLPG; VRVFDGTERLPGD; RVFDGTERLPGDP; VFDGTERLPGDPD; FDGTERLPGDPDM; DGTERLPGDPDMI; GTERLPGDPDMIR; TERLPGDPDMIRY; ERLPGDPDMIRYI; RLPGDPDMIRYID; LPGDPDMIRYIDK; PGDPDMIRYIDKQ; GDPDMIRYIDKQG; DPDMIRYIDKQGQ; PDMIRYIDKQGQL; DMIRYIDKQGQLQ; MIRYIDKQGQLQT; IRYIDKQGQLQTK; RYIDKQGQLQTKM; YIDKQGQLQTKML; TGAFIVHIHLINA; GAFIVHIHLINAA; AFIVHIHLINAAF; FIVHIHLINAAFV; ATFKLVLFWGWCF; TFKLVLFWGWCFR; FKLVLFWGWCFRP; KLVLFWGWCFRPF; LVLFWGWCFRPFK; VLFWGWCFRPFKT; LFWGWCFRPFKTL; FWGWCFRPFKTLK; WGWCFRPFKTLKA; GWCFRPFKTLKAF; WCFRPFKTLKAFT; CFRPFKTLKAFTQ; FRPFKTLKAFTQM; RPFKTLKAFTQMQ; PFKTLKAFTQMQL; FKTLKAFTQMQLL; KTLKAFTQMQLLT; TLKAFTQMQLLTM; LKAFTQMQLLTMG; KAFTQMQLLTMGV; ILFSCNIKNTFPH; LFSCNIKNTFPHA; FSCNIKNTFPHAY; SCNIKNTFPHAYI; CNIKNTFPHAYII; NIKNTFPHAYIIF; IKNTFPHAYIIFH; KNTFPHAYIIFHP; KSIHTYLRIQPFL; SIHTYLRIQPFLP; IHTYLRIQPFLPF; HTYLRIQPFLPFN; TYLRIQPFLPFNN; YLRIQPFLPFNNS; LRIQPFLPFNNSR; RIQPFLPFNNSRL; IQPFLPFNNSRLY; QPFLPFNNSRLYI; PFLPFNNSRLYIS; FLPFNNSRLYISC; LPFNNSRLYISCK; PFNNSRLYISCKI; FNNSRLYISCKIS; NNSRLYISCKISY; NSRLYISCKISYR; SRLYISCKISYRP; RLYISCKISYRPK; LYISCKISYRPKP; YISCKISYRPKPN; IYFGPKIYLSYKS; YFGPKIYLSYKSS; FGPKIYLSYKSSL; GPKIYLSYKSSLQ; PKIYLSYKSSLQG; KIYLSYKSSLQGF; IYLSYKSSLQGFR; YLSYKSSLQGFRD; LSYKSSLQGFRDR; SYKSSLQGFRDRI; YKSSLQGFRDRIL; KSSLQGFRDRILI; SSLQGFRDRILIH; SLQGFRDRILIHC; LQGFRDRILIHCN; QGFRDRILIHCNQ; GFRDRILIHCNQA; FRDRILIHCNQAW; RDRILIHCNQAWW; DRILIHCNQAWWK; RILIHCNQAWWKY; ILIHCNQAWWKYL; LIHCNQAWWKYLG; IHCNQAWWKYLGS; HCNQAWWKYLGSF; CNQAWWKYLGSFV; FSSCPFYIFKNNH; SSCPFYIFKNNHV; SCPFYIFKNNHVL; CPFYIFKNNHVLI; PFYIFKNNHVLIY; FYIFKNNHVLIYS; YIFKNNHVLIYSY; IFKNNHVLIYSYT; PVSSFRYIENNTV; VSSFRYIENNTVQ; SSFRYIENNTVQK; SFRYIENNTVQKI; FRYIENNTVQKIK; RYIENNTVQKIKY; YIENNTVQKIKYY; IENNTVQKIKYYR; ENNTVQKIKYYRI; NNTVQKIKYYRIH; NTVQKIKYYRIHF; TVQKIKYYRIHFR; QTVQPSNTCHILF; HFFPGHMKGIYSF; FFPGHMKGIYSFF; FPGHMKGIYSFFS; NCIYCLLTNTFLI; CIYCLLTNTFLIF; IYCLLTNTFLIFT; YCLLTNTFLIFTF; CLLTNTFLIFTFC; LLTNTFLIFTFCK; LTNTFLIFTFCKN; TNTFLIFTFCKNN; NTFLIFTFCKNNS; TFLIFTFCKNNSI; FLIFTFCKNNSIC; LIFTFCKNNSICK; IFTFCKNNSICKV; FTFCKNNSICKVL; TFCKNNSICKVLF; FCKNNSICKVLFM; CKNNSICKVLFMI; KNNSICKVLFMIL; NNSICKVLFMILK; NSICKVLFMILKV; SICKVLFMILKVI; ICKVLFMILKVIR; CKVLFMILKVIRL; KVLFMILKVIRLV; VLFMILKVIRLVF; LFMILKVIRLVFF; FMILKVIRLVFFL; MILKVIRLVFFLT; ILKVIRLVFFLTL; LKVIRLVFFLTLF; KVIRLVFFLTLFT; VIRLVFFLTLFTL; IRLVFFLTLFTLL; RLVFFLTLFTLLY; LVFFLTLFTLLYI; VFFLTLFTLLYIV; FFLTLFTLLYIVL; FLTLFTLLYIVLK; LTLFTLLYIVLKF; KHILTLCLYCILS; HILTLCLYCILSN; FPRHLLCFFRLFW; PRHLLCFFRLFWA; RHLLCFFRLFWAK; HLLCFFRLFWAKI; LLCFFRLFWAKIM; LCFFRLFWAKIML; CFFRLFWAKIMLL; APLNAFFYSMVWI; PLNAFFYSMVWIS; LNAFFYSMVWISS; KTKGTQLLTEIIN; TKGTQLLTEIINC; KGTQLLTEIINCR; GTQLLTEIINCRN; TQLLTEIINCRNS; QLLTEIINCRNSM; LLTEIINCRNSMS; LTEIINCRNSMSM; TEIINCRNSMSMW; EIINCRNSMSMWS; KEYNIMPSTHVST; EYNIMPSTHVSTN; YNIMPSTHVSTNK; NIMPSTHVSTNKS; IMPSTHVSTNKSY; MPSTHVSTNKSYR; PSTHVSTNKSYRI; STHVSTNKSYRIF; THVSTNKSYRIFF; HVSTNKSYRIFFH; VSTNKSYRIFFHK; STNKSYRIFFHKF; TNKSYRIFFHKFF; NKSYRIFFHKFFI; KSYRIFFHKFFIQ; SYRIFFHKFFIQN; YRIFFHKFFIQNL; RIFFHKFFIQNLS; IFFHKFFIQNLSF; FFHKFFIQNLSFF; FHKFFIQNLSFFF; HKFFIQNLSFFFS; KFFIQNLSFFFSS; FFIQNLSFFFSSI; FIQNLSFFFSSIH; IQNLSFFFSSIHS; QNLSFFFSSIHSK; NLSFFFSSIHSKA; LSFFFSSIHSKAG; SFFFSSIHSKAGK; FFFSSIHSKAGKG; FFSSIHSKAGKGS; FSSIHSKAGKGSI; SSIHSKAGKGSIT; SIHSKAGKGSITK; IHSKAGKGSITKY; HSKAGKGSITKYS; SKAGKGSITKYSL; KAGKGSITKYSLT; AGKGSITKYSLTK; GKGSITKYSLTKK; KGSITKYSLTKKL; GSITKYSLTKKLV; IRGKVFRVFYLSF; RGKVFRVFYLSFF; GKVFRVFYLSFFF; KVFRVFYLSFFFG; VFRVFYLSFFFGW; FRVFYLSFFFGWC; VLRICCCFFITGK; LRICCCFFITGKH; RICCCFFITGKHI; ICCCFFITGKHIF; CCCFFITGKHIFM; CCFFITGKHIFMA; CFFITGKHIFMAK; IFIPFFIKGTPPG; FIPFFIKGTPPGL; IPFFIKGTPPGLP; PFFIKGTPPGLPL; FFIKGTPPGLPLF; FIKGTPPGLPLFC; IKGTPPGLPLFCS; KGTPPGLPLFCSI; GTPPGLPLFCSIG; TPPGLPLFCSIGW; PPGLPLFCSIGWH; PGLPLFCSIGWHL; SFRSLKGVSPIIW; FRSLKGVSPIIWT; RSLKGVSPIIWTH; SLKGVSPIIWTHH; LKGVSPIIWTHHC; KGVSPIIWTHHCR; GVSPIIWTHHCRV; VSPIIWTHHCRVS; SPIIWTHHCRVSS; PIIWTHHCRVSSV; IIWTHHCRVSSVR; IWTHHCRVSSVRS; WTHHCRVSSVRSK; THHCRVSSVRSKP; HHCRVSSVRSKPN; HCRVSSVRSKPNH; CRVSSVRSKPNHC; RVSSVRSKPNHCV; VSSVRSKPNHCVK; SSVRSKPNHCVKQ; SVRSKPNHCVKQS; VRSKPNHCVKQSM; RSKPNHCVKQSMQ; QSIQTKGSFLKNF; SIQTKGSFLKNFL; IQTKGSFLKNFLF; QTKGSFLKNFLFK; TKGSFLKNFLFKC; KGSFLKNFLFKCL; GSFLKNFLFKCLN; SFLKNFLFKCLNL; FLKNFLFKCLNLS; HSMQGQCTEGFLE; SMQGQCTEGFLEQ; MQGQCTEGFLEQI; QGQCTEGFLEQIG; GQCTEGFLEQIGH; QCTEGFLEQIGHS; CTEGFLEQIGHSL; TEGFLEQIGHSLQ; EGFLEQIGHSLQY; GFLEQIGHSLQYR; FLEQIGHSLQYRV; LEQIGHSLQYRVS; EQIGHSLQYRVSG; QIGHSLQYRVSGQ; IGHSLQYRVSGQR; GHSLQYRVSGQRG; HSLQYRVSGQRGK; SLQYRVSGQRGKS; LQYRVSGQRGKSA; QYRVSGQRGKSAQ; YRVSGQRGKSAQT; RVSGQRGKSAQTS; VSGQRGKSAQTSE; SGQRGKSAQTSEL; GQRGKSAQTSELL; QRGKSAQTSELLQ; RGKSAQTSELLQV; GKSAQTSELLQVP; KSAQTSELLQVPK; SAQTSELLQVPKS; AQTSELLQVPKSG; ATFTSCSIFLYKV; TFTSCSIFLYKVF; FTSCSIFLYKVFI; TSCSIFLYKVFIL; SCSIFLYKVFILF; CSIFLYKVFILFI; SIFLYKVFILFIL; IFLYKVFILFILS; FLYKVFILFILSS; LYKVFILFILSSS; YKVFILFILSSSP; KVFILFILSSSPP; VFILFILSSSPPL; FILFILSSSPPLS; ILFILSSSPPLSG; AFLIKGRFPQAAL; FLIKGRFPQAALS; LIKGRFPQAALSR; IKGRFPQAALSRP; KGRFPQAALSRPK; GRFPQAALSRPKR; RFPQAALSRPKRS; FPQAALSRPKRSM; PQAALSRPKRSMS; QAALSRPKRSMSS; AALSRPKRSMSSM; ALSRPKRSMSSMD; LSRPKRSMSSMDS; SRPKRSMSSMDSS; RPKRSMSSMDSSL; PKRSMSSMDSSLL; KRSMSSMDSSLLR; RSMSSMDSSLLRT; SMSSMDSSLLRTL; MSSMDSSLLRTLS 14 mers: FCKNCKRIGISPNS; CKNCKRIGISPNSF; KNCKRIGISPNSFA; NCKRIGISPNSFAR; CKRIGISPNSFARP; KRIGISPNSFARPQ; RIGISPNSFARPQK; IGISPNSFARPQKK; GISPNSFARPQKKP; ISPNSFARPQKKPP; SPNSFARPQKKPPH; PNSFARPQKKPPHP; NSFARPQKKPPHPY; SFARPQKKPPHPYY; FARPQKKPPHPYYL; ARPQKKPPHPYYLR; RPQKKPPHPYYLRE; PQKKPPHPYYLRER; QKKPPHPYYLRERV; KKPPHPYYLRERVE; KPPHPYYLRERVEA; PPHPYYLRERVEAE; PHPYYLRERVEAEA; HPYYLRERVEAEAA; PYYLRERVEAEAAS; YYLRERVEAEAASA; YLRERVEAEAASAS; LRERVEAEAASASY; RERVEAEAASASYI; ERVEAEAASASYIL; KKRPQGGAAYPWNA; KRPQGGAAYPWNAA; RPQGGAAYPWNAAK; PQGGAAYPWNAAKP; PQEGKCMTHRGMQP; QEGKCMTHRGMQPN; EGKCMTHRGMQPNH; GKCMTHRGMQPNHD; KCMTHRGMQPNHDL; CMTHRGMQPNHDLR; MTHRGMQPNHDLRK; THRGMQPNHDLRKE; HRGMQPNHDLRKES; RGMQPNHDLRKESA; LTGRSCLPMECSQT; TGRSCLPMECSQTM; GRSCLPMECSQTMT; RSCLPMECSQTMTS; SCLPMECSQTMTSG; CLPMECSQTMTSGR; LPMECSQTMTSGRK; PMECSQTMTSGRKV; MECSQTMTSGRKVH; ECSQTMTSGRKVHD; CSQTMTSGRKVHDR; SQTMTSGRKVHDRH; QTMTSGRKVHDRHV; TMTSGRKVHDRHVL; MTSGRKVHDRHVLR; TSGRKVHDRHVLRA; ESWPCPQLNWTKAM; SWPCPQLNWTKAMV; WPCPQLNWTKAMVL; PCPQLNWTKAMVLR; CPQLNWTKAMVLRQ; PQLNWTKAMVLRQL; QLNWTKAMVLRQLS; LNWTKAMVLRQLSR; NWTKAMVLRQLSRQ; WTKAMVLRQLSRQA; TKAMVLRQLSRQAS; KAMVLRQLSRQASV; AMVLRQLSRQASVK; MVLRQLSRQASVKV; VLRQLSRQASVKVG; LRQLSRQASVKVGK; RQLSRQASVKVGKT; QLSRQASVKVGKTW; LSRQASVKVGKTWT; SRQASVKVGKTWTG; RQASVKVGKTWTGT; QASVKVGKTWTGTK; ASVKVGKTWTGTKK; SVKVGKTWTGTKKR; VKVGKTWTGTKKRA; KVGKTWTGTKKRAQ; VGKTWTGTKKRAQR; GKTWTGTKKRAQRI; KTWTGTKKRAQRIF; TWTGTKKRAQRIFI; WTGTKKRAQRIFIF; TGTKKRAQRIFIFI; GTKKRAQRIFIFIL; TKKRAQRIFIFILE; KKRAQRIFIFILEL; KRAQRIFIFILELL; RAQRIFIFILELLL; AQRIFIFILELLLE; QRIFIFILELLLEF; RIFIFILELLLEFC; IFIFILELLLEFCR; FIFILELLLEFCRG; IFILELLLEFCRGE; FILELLLEFCRGED; ILELLLEFCRGEDS; LELLLEFCRGEDSV; ELLLEFCRGEDSVD; LLLEFCRGEDSVDG; LLEFCRGEDSVDGK; LEFCRGEDSVDGKN; EFCRGEDSVDGKNK; FCRGEDSVDGKNKS; CRGEDSVDGKNKST; RGEDSVDGKNKSTT; GEDSVDGKNKSTTA; EDSVDGKNKSTTAL; DSVDGKNKSTTALP; SVDGKNKSTTALPA; VDGKNKSTTALPAV; DGKNKSTTALPAVK; GKNKSTTALPAVKD; KNKSTTALPAVKDS; NKSTTALPAVKDSV; KSTTALPAVKDSVK; STTALPAVKDSVKD; TTALPAVKDSVKDS; VSNPFFFVFPGSWV; SNPFFFVFPGSWVL; NPFFFVFPGSWVLL; LPVYLRLLLPQDFQ; PVYLRLLLPQDFQW; VYLRLLLPQDFQWL; YLRLLLPQDFQWLK; LRLLLPQDFQWLKL; RLLLPQDFQWLKLL; LLLPQDFQWLKLLL; LLPQDFQWLKLLLG; LPQDFQWLKLLLGR; PQDFQWLKLLLGRL; QDFQWLKLLLGRLL; DFQWLKLLLGRLLL; FQWLKLLLGRLLLL; GISSLMIGITKFPL; ASISNQAWLWNCLT; SISNQAWLWNCLTQ; ISNQAWLWNCLTQM; SNQAWLWNCLTQMS; NQAWLWNCLTQMST; QAWLWNCLTQMSTM; AWLWNCLTQMSTMI; WLWNCLTQMSTMIF; LWNCLTQMSTMIFC; WNCLTQMSTMIFCF; NCLTQMSTMIFCFL; CLTQMSTMIFCFLV; ILLLIIFNTLILGI; LLLIIFNTLILGIG; LLIIFNTLILGIGV; LIIFNTLILGIGVL; IIFNTLILGIGVLL; IFNTLILGIGVLLC; FNTLILGIGVLLCL; NTLILGIGVLLCLL; TLILGIGVLLCLLL; LILGIGVLLCLLLF; ILGIGVLLCLLLFP; LGIGVLLCLLLFPR; GIGVLLCLLLFPRL; IGVLLCLLLFPRLC; GVLLCLLLFPRLCG; VLLCLLLFPRLCGM; LLCLLLFPRLCGML; LCLLLFPRLCGMLL; CLLLFPRLCGMLLG; LLLFPRLCGMLLGM; LLFPRLCGMLLGMI; LFPRLCGMLLGMIY; FPRLCGMLLGMIYL; PRLCGMLLGMIYLL; PHRNCREEQKDFLE; HRNCREEQKDFLET; RNCREEQKDFLETP; NCREEQKDFLETPW; CREEQKDFLETPWL; REEQKDFLETPWLD; EEQKDFLETPWLDF; EQKDFLETPWLDFW; QKDFLETPWLDFWR; KDFLETPWLDFWRK; DFLETPWLDFWRKL; FLETPWLDFWRKLP; LETPWLDFWRKLPG; ETPWLDFWRKLPGQ; TPWLDFWRKLPGQL; TFIIIFNNIILIFP; FIIIFNNIILIFPL; IIIFNNIILIFPLL; IIFNNIILIFPLLG; IFNNIILIFPLLGP; FNNIILIFPLLGPQ; NNIILIFPLLGPQW; NIILIFPLLGPQWL; IILIFPLLGPQWLD; ILIFPLLGPQWLDK; LKGKVPVYILAILI; KGKVPVYILAILIV; KKLLPQEVLIKELL; KLLPQEVLIKELLL; LLPQEVLIKELLLN; LPQEVLIKELLLNG; PQEVLIKELLLNGC; QEVLIKELLLNGCC; EVLIKELLLNGCCL; VLIKELLLNGCCLY; LIKELLLNGCCLYF; HLLLKHMKMAPTKR; LLLKHMKMAPTKRK; LLKHMKMAPTKRKG; LKHMKMAPTKRKGE; KHMKMAPTKRKGEC; HMKMAPTKRKGECP; MKMAPTKRKGECPG; KMAPTKRKGECPGA; MAPTKRKGECPGAA; APTKRKGECPGAAP; PTKRKGECPGAAPK; TKRKGECPGAAPKK; KRKGECPGAAPKKP; RKGECPGAAPKKPK; KGECPGAAPKKPKE; GECPGAAPKKPKEP; ECPGAAPKKPKEPV; CPGAAPKKPKEPVQ; PGAAPKKPKEPVQV; GAAPKKPKEPVQVP; AAPKKPKEPVQVPK; APKKPKEPVQVPKL; PKKPKEPVQVPKLL; KKPKEPVQVPKLLI; KPKEPVQVPKLLIK; PKEPVQVPKLLIKG; KEPVQVPKLLIKGG; EPVQVPKLLIKGGV; PVQVPKLLIKGGVE; VQVPKLLIKGGVEV; QVPKLLIKGGVEVL; VPKLLIKGGVEVLE; PKLLIKGGVEVLEV; KLLIKGGVEVLEVK; LLIKGGVEVLEVKT; LIKGGVEVLEVKTG; IKGGVEVLEVKTGV; KGGVEVLEVKTGVD; GGVEVLEVKTGVDA; GVEVLEVKTGVDAI; VEVLEVKTGVDAIT; EVLEVKTGVDAITE; VLEVKTGVDAITEV; LEVKTGVDAITEVE; EVKTGVDAITEVEC; VKTGVDAITEVECF; KTGVDAITEVECFL; TGVDAITEVECFLN; GVDAITEVECFLNP; VDAITEVECFLNPE; DAITEVECFLNPEM; AITEVECFLNPEMG; ITEVECFLNPEMGD; TEVECFLNPEMGDP; EVECFLNPEMGDPD; VECFLNPEMGDPDE; ECFLNPEMGDPDEN; CFLNPEMGDPDENL; FLNPEMGDPDENLR; LNPEMGDPDENLRG; NPEMGDPDENLRGF; PEMGDPDENLRGFS; EMGDPDENLRGFSL; MGDPDENLRGFSLK; GDPDENLRGFSLKL; DPDENLRGFSLKLS; PDENLRGFSLKLSA; DENLRGFSLKLSAE; ENLRGFSLKLSAEN; NLRGFSLKLSAEND; LRGFSLKLSAENDF; RGFSLKLSAENDFS; GFSLKLSAENDFSS; FSLKLSAENDFSSD; SLKLSAENDFSSDS; LKLSAENDFSSDSP; KLSAENDFSSDSPE; LSAENDFSSDSPER; SAENDFSSDSPERK; AENDFSSDSPERKM; ENDFSSDSPERKML; NDFSSDSPERKMLP; DFSSDSPERKMLPC; FSSDSPERKMLPCY; SSDSPERKMLPCYS; SDSPERKMLPCYST; DSPERKMLPCYSTA; SPERKMLPCYSTAR; PERKMLPCYSTARI; ERKMLPCYSTARIP; RKMLPCYSTARIPL; KMLPCYSTARIPLP; MLPCYSTARIPLPN; LPCYSTARIPLPNL; PCYSTARIPLPNLN; CYSTARIPLPNLNE; YSTARIPLPNLNED; STARIPLPNLNEDL; TARIPLPNLNEDLT; ARIPLPNLNEDLTC; RIPLPNLNEDLTCG; IPLPNLNEDLTCGN; PLPNLNEDLTCGNL; LPNLNEDLTCGNLL; PNLNEDLTCGNLLM; NLNEDLTCGNLLMW; LNEDLTCGNLLMWE; NEDLTCGNLLMWEA; EDLTCGNLLMWEAV; DLTCGNLLMWEAVT; LTCGNLLMWEAVTV; TCGNLLMWEAVTVQ; CGNLLMWEAVTVQT; GNLLMWEAVTVQTE; NLLMWEAVTVQTEV; LLMWEAVTVQTEVI; LMWEAVTVQTEVIG; MWEAVTVQTEVIGI; WEAVTVQTEVIGIT; EAVTVQTEVIGITS; AVTVQTEVIGITSM; VTVQTEVIGITSML; TVQTEVIGITSMLN; VQTEVIGITSMLNL; QTEVIGITSMLNLH; TEVIGITSMLNLHA; EVIGITSMLNLHAG; VIGITSMLNLHAGS; IGITSMLNLHAGSQ; GITSMLNLHAGSQK; ITSMLNLHAGSQKV; TSMLNLHAGSQKVH; SMLNLHAGSQKVHE; MLNLHAGSQKVHEH; LNLHAGSQKVHEHG; NLHAGSQKVHEHGG; LHAGSQKVHEHGGG; HAGSQKVHEHGGGK; AGSQKVHEHGGGKP; GSQKVHEHGGGKPI; SQKVHEHGGGKPIQ; QKVHEHGGGKPIQG; KVHEHGGGKPIQGS; VHEHGGGKPIQGSN; HEHGGGKPIQGSNF; EHGGGKPIQGSNFH; HGGGKPIQGSNFHF; GGGKPIQGSNFHFF; GGKPIQGSNFHFFA; GKPIQGSNFHFFAV; KPIQGSNFHFFAVG; PIQGSNFHFFAVGG; IQGSNFHFFAVGGE; QGSNFHFFAVGGEP; GSNFHFFAVGGEPL; SNFHFFAVGGEPLE; NFHFFAVGGEPLEM; FHFFAVGGEPLEMQ; HFFAVGGEPLEMQG; FFAVGGEPLEMQGV; FAVGGEPLEMQGVL; AVGGEPLEMQGVLM; VGGEPLEMQGVLMN; GGEPLEMQGVLMNY; GEPLEMQGVLMNYR; EPLEMQGVLMNYRS; PLEMQGVLMNYRSK; LEMQGVLMNYRSKY; EMQGVLMNYRSKYP; MQGVLMNYRSKYPD; QGVLMNYRSKYPDG; GVLMNYRSKYPDGT; VLMNYRSKYPDGTI; LMNYRSKYPDGTIT; MNYRSKYPDGTITP; NYRSKYPDGTITPK; YRSKYPDGTITPKN; RSKYPDGTITPKNP; SKYPDGTITPKNPT; KYPDGTITPKNPTA; YPDGTITPKNPTAQ; PDGTITPKNPTAQS; DGTITPKNPTAQSQ; GTITPKNPTAQSQV; TITPKNPTAQSQVM; ITPKNPTAQSQVMN; TPKNPTAQSQVMNT; PKNPTAQSQVMNTD; KNPTAQSQVMNTDH; NPTAQSQVMNTDHK; PTAQSQVMNTDHKA; TAQSQVMNTDHKAY; AQSQVMNTDHKAYL; QSQVMNTDHKAYLD; SQVMNTDHKAYLDK; QVMNTDHKAYLDKN; VMNTDHKAYLDKNN; MNTDHKAYLDKNNA; NTDHKAYLDKNNAY; TDHKAYLDKNNAYP; DHKAYLDKNNAYPV; HKAYLDKNNAYPVE; KAYLDKNNAYPVEC; AYLDKNNAYPVECW; YLDKNNAYPVECWV; LDKNNAYPVECWVP; DKNNAYPVECWVPD; KNNAYPVECWVPDP; NNAYPVECWVPDPS; NAYPVECWVPDPSR; AYPVECWVPDPSRN; YPVECWVPDPSRNE; PVECWVPDPSRNEN; VECWVPDPSRNENA; ECWVPDPSRNENAR; CWVPDPSRNENARY; WVPDPSRNENARYF; VPDPSRNENARYFG; PDPSRNENARYFGT; DPSRNENARYFGTF; PSRNENARYFGTFT; SRNENARYFGTFTG; RNENARYFGTFTGG; NENARYFGTFTGGE; ENARYFGTFTGGEN; NARYFGTFTGGENV; ARYFGTFTGGENVP; RYFGTFTGGENVPP; YFGTFTGGENVPPV; FGTFTGGENVPPVL; GTFTGGENVPPVLH; TFTGGENVPPVLHV; FTGGENVPPVLHVT; TGGENVPPVLHVTN; GGENVPPVLHVTNT; GENVPPVLHVTNTA; ENVPPVLHVTNTAT; NVPPVLHVTNTATT; VPPVLHVTNTATTV; PPVLHVTNTATTVL; PVLHVTNTATTVLL; VLHVTNTATTVLLD; LHVTNTATTVLLDE; HVTNTATTVLLDEQ; VTNTATTVLLDEQG; TNTATTVLLDEQGV; NTATTVLLDEQGVG; TATTVLLDEQGVGP; ATTVLLDEQGVGPL; TTVLLDEQGVGPLC; TVLLDEQGVGPLCK; VLLDEQGVGPLCKA; LLDEQGVGPLCKAD; LDEQGVGPLCKADS; DEQGVGPLCKADSL; EQGVGPLCKADSLY; QGVGPLCKADSLYV; GVGPLCKADSLYVS; VGPLCKADSLYVSA; GPLCKADSLYVSAA; PLCKADSLYVSAAD; LCKADSLYVSAADI; CKADSLYVSAADIC; KADSLYVSAADICG; ADSLYVSAADICGL; DSLYVSAADICGLF; SLYVSAADICGLFT; LYVSAADICGLFTN; YVSAADICGLFTNS; VSAADICGLFTNSS; SAADICGLFTNSSG; AADICGLFTNSSGT; ADICGLFTNSSGTQ; DICGLFTNSSGTQQ; ICGLFTNSSGTQQW; CGLFTNSSGTQQWR; GLFTNSSGTQQWRG; LFTNSSGTQQWRGL; FTNSSGTQQWRGLA; TNSSGTQQWRGLAR; NSSGTQQWRGLARY; SSGTQQWRGLARYF; SGTQQWRGLARYFK; GTQQWRGLARYFKI; TQQWRGLARYFKIR; QQWRGLARYFKIRL; QWRGLARYFKIRLR; WRGLARYFKIRLRK; RGLARYFKIRLRKR; GLARYFKIRLRKRS; LARYFKIRLRKRSV; ARYFKIRLRKRSVK; RYFKIRLRKRSVKN; YFKIRLRKRSVKNP; FKIRLRKRSVKNPY; KIRLRKRSVKNPYP; IRLRKRSVKNPYPI; RLRKRSVKNPYPIS; LRKRSVKNPYPISF; RKRSVKNPYPISFL; KRSVKNPYPISFLL; RSVKNPYPISFLLS; SVKNPYPISFLLSD; VKNPYPISFLLSDL; KNPYPISFLLSDLI; NPYPISFLLSDLIN; PYPISFLLSDLINR; YPISFLLSDLINRR; PISFLLSDLINRRT; ISFLLSDLINRRTQ; SFLLSDLINRRTQR; FLLSDLINRRTQRV; LLSDLINRRTQRVD; LSDLINRRTQRVDG; SDLINRRTQRVDGQ; DLINRRTQRVDGQP; LINRRTQRVDGQPM; INRRTQRVDGQPMY; NRRTQRVDGQPMYG; RRTQRVDGQPMYGM; RTQRVDGQPMYGME; TQRVDGQPMYGMES; QRVDGQPMYGMESQ; RVDGQPMYGMESQV; VDGQPMYGMESQVE; DGQPMYGMESQVEE; GQPMYGMESQVEEV; QPMYGMESQVEEVR; PMYGMESQVEEVRV; MYGMESQVEEVRVF; YGMESQVEEVRVFD; GMESQVEEVRVFDG; MESQVEEVRVFDGT; ESQVEEVRVFDGTE; SQVEEVRVFDGTER; QVEEVRVFDGTERL; VEEVRVFDGTERLP; EEVRVFDGTERLPG; EVRVFDGTERLPGD; VRVFDGTERLPGDP; RVFDGTERLPGDPD; VFDGTERLPGDPDM; FDGTERLPGDPDMI; DGTERLPGDPDMIR; GTERLPGDPDMIRY; TERLPGDPDMIRYI; ERLPGDPDMIRYID; RLPGDPDMIRYIDK; LPGDPDMIRYIDKQ; PGDPDMIRYIDKQG; GDPDMIRYIDKQGQ; DPDMIRYIDKQGQL; PDMIRYIDKQGQLQ; DMIRYIDKQGQLQT; MIRYIDKQGQLQTK; IRYIDKQGQLQTKM; RYIDKQGQLQTKML; TGAFIVHIHLINAA; GAFIVHIHLINAAF; AFIVHIHLINAAFV; ATFKLVLFWGWCFR; TFKLVLFWGWCFRP; FKLVLFWGWCFRPF; KLVLFWGWCFRPFK; LVLFWGWCFRPFKT; VLFWGWCFRPFKTL; LFWGWCFRPFKTLK; FWGWCFRPFKTLKA; WGWCFRPFKTLKAF; GWCFRPFKTLKAFT; WCFRPFKTLKAFTQ; CFRPFKTLKAFTQM; FRPFKTLKAFTQMQ; RPFKTLKAFTQMQL; PFKTLKAFTQMQLL; FKTLKAFTQMQLLT; KTLKAFTQMQLLTM; TLKAFTQMQLLTMG; LKAFTQMQLLTMGV; ILFSCNIKNTFPHA; LFSCNIKNTFPHAY; FSCNIKNTFPHAYI; SCNIKNTFPHAYII; CNIKNTFPHAYIIF; NIKNTFPHAYIIFH; IKNTFPHAYIIFHP; KSIHTYLRIQPFLP; SIHTYLRIQPFLPF; IHTYLRIQPFLPFN; HTYLRIQPFLPFNN; TYLRIQPFLPFNNS; YLRIQPFLPFNNSR; LRIQPFLPFNNSRL; RIQPFLPFNNSRLY; IQPFLPFNNSRLYI; QPFLPFNNSRLYIS; PFLPFNNSRLYISC; FLPFNNSRLYISCK; LPFNNSRLYISCKI; PFNNSRLYISCKIS; FNNSRLYISCKISY; NNSRLYISCKISYR; NSRLYISCKISYRP; SRLYISCKISYRPK; RLYISCKISYRPKP; LYISCKISYRPKPN; IYFGPKIYLSYKSS; YFGPKIYLSYKSSL; FGPKIYLSYKSSLQ; GPKIYLSYKSSLQG; PKIYLSYKSSLQGF; KIYLSYKSSLQGFR; IYLSYKSSLQGFRD; YLSYKSSLQGFRDR; LSYKSSLQGFRDRI; SYKSSLQGFRDRIL; YKSSLQGFRDRILI; KSSLQGFRDRILIH; SSLQGFRDRILIHC; SLQGFRDRILIHCN; LQGFRDRILIHCNQ; QGFRDRILIHCNQA; GFRDRILIHCNQAW; FRDRILIHCNQAWW; RDRILIHCNQAWWK; DRILIHCNQAWWKY; RILIHCNQAWWKYL; ILIHCNQAWWKYLG; LIHCNQAWWKYLGS; IHCNQAWWKYLGSF; HCNQAWWKYLGSFV; FSSCPFYIFKNNHV; SSCPFYIFKNNHVL; SCPFYIFKNNHVLI; CPFYIFKNNHVLIY; PFYIFKNNHVLIYS; FYIFKNNHVLIYSY; YIFKNNHVLIYSYT; PVSSFRYIENNTVQ; VSSFRYIENNTVQK; SSFRYIENNTVQKI; SFRYIENNTVQKIK; FRYIENNTVQKIKY; RYIENNTVQKIKYY; YIENNTVQKIKYYR; IENNTVQKIKYYRI; ENNTVQKIKYYRIH; NNTVQKIKYYRIHF; NTVQKIKYYRIHFR; HFFPGHMKGIYSFF; FFPGHMKGIYSFFS; NCIYCLLTNTFLIF; CIYCLLTNTFLIFT; IYCLLTNTFLIFTF; YCLLTNTFLIFTFC; CLLTNTFLIFTFCK; LLTNTFLIFTFCKN; LTNTFLIFTFCKNN; TNTFLIFTFCKNNS; NTFLIFTFCKNNSI; TFLIFTFCKNNSIC; FLIFTFCKNNSICK; LIFTFCKNNSICKV; IFTFCKNNSICKVL; FTFCKNNSICKVLF; TFCKNNSICKVLFM; FCKNNSICKVLFMI; CKNNSICKVLFMIL; KNNSICKVLFMILK; NNSICKVLFMILKV; NSICKVLFMILKVI; SICKVLFMILKVIR; ICKVLFMILKVIRL; CKVLFMILKVIRLV; KVLFMILKVIRLVF; VLFMILKVIRLVFF; LFMILKVIRLVFFL; FMILKVIRLVFFLT; MILKVIRLVFFLTL; ILKVIRLVFFLTLF; LKVIRLVFFLTLFT; KVIRLVFFLTLFTL; VIRLVFFLTLFTLL; IRLVFFLTLFTLLY; RLVFFLTLFTLLYI; LVFFLTLFTLLYIV; VFFLTLFTLLYIVL; FFLTLFTLLYIVLK; FLTLFTLLYIVLKF; KHILTLCLYCILSN; FPRHLLCFFRLFWA; PRHLLCFFRLFWAK; RHLLCFFRLFWAKI; HLLCFFRLFWAKIM; LLCFFRLFWAKIML; LCFFRLFWAKIMLL; APLNAFFYSMVWIS; PLNAFFYSMVWISS; KTKGTQLLTEIINC; TKGTQLLTEIINCR; KGTQLLTEIINCRN; GTQLLTEIINCRNS; TQLLTEIINCRNSM; QLLTEIINCRNSMS; LLTEIINCRNSMSM; LTEIINCRNSMSMW; TEIINCRNSMSMWS; KEYNIMPSTHVSTN; EYNIMPSTHVSTNK; YNIMPSTHVSTNKS; NIMPSTHVSTNKSY; IMPSTHVSTNKSYR; MPSTHVSTNKSYRI; PSTHVSTNKSYRIF; STHVSTNKSYRIFF; THVSTNKSYRIFFH; HVSTNKSYRIFFHK; VSTNKSYRIFFHKF; STNKSYRIFFHKFF; TNKSYRIFFHKFFI; NKSYRIFFHKFFIQ; KSYRIFFHKFFIQN; SYRIFFHKFFIQNL; YRIFFHKFFIQNLS; RIFFHKFFIQNLSF; IFFHKFFIQNLSFF; FFHKFFIQNLSFFF; FHKFFIQNLSFFFS; HKFFIQNLSFFFSS; KFFIQNLSFFFSSI; FFIQNLSFFFSSIH; FIQNLSFFFSSIHS; IQNLSFFFSSIHSK; QNLSFFFSSIHSKA; NLSFFFSSIHSKAG; LSFFFSSIHSKAGK; SFFFSSIHSKAGKG; FFFSSIHSKAGKGS; FFSSIHSKAGKGSI; FSSIHSKAGKGSIT; SSIHSKAGKGSITK; SIHSKAGKGSITKY; IHSKAGKGSITKYS; HSKAGKGSITKYSL; SKAGKGSITKYSLT; KAGKGSITKYSLTK; AGKGSITKYSLTKK; GKGSITKYSLTKKL; KGSITKYSLTKKLV; IRGKVFRVFYLSFF; RGKVFRVFYLSFFF; GKVFRVFYLSFFFG; KVFRVFYLSFFFGW; VFRVFYLSFFFGWC; VLRICCCFFITGKH; LRICCCFFITGKHI; RICCCFFITGKHIF; ICCCFFITGKHIFM; CCCFFITGKHIFMA; CCFFITGKHIFMAK; IFIPFFIKGTPPGL; FIPFFIKGTPPGLP; IPFFIKGTPPGLPL; PFFIKGTPPGLPLF; FFIKGTPPGLPLFC; FIKGTPPGLPLFCS; IKGTPPGLPLFCSI; KGTPPGLPLFCSIG; GTPPGLPLFCSIGW; TPPGLPLFCSIGWH; PPGLPLFCSIGWHL; SFRSLKGVSPIIWT; FRSLKGVSPIIWTH; RSLKGVSPIIWTHH; SLKGVSPIIWTHHC; LKGVSPIIWTHHCR; KGVSPIIWTHHCRV; GVSPIIWTHHCRVS; VSPIIWTHHCRVSS; SPIIWTHHCRVSSV; PIIWTHHCRVSSVR; IIWTHHCRVSSVRS; IWTHHCRVSSVRSK; WTHHCRVSSVRSKP; THHCRVSSVRSKPN; HHCRVSSVRSKPNH; HCRVSSVRSKPNHC; CRVSSVRSKPNHCV; RVSSVRSKPNHCVK; VSSVRSKPNHCVKQ; SSVRSKPNHCVKQS; SVRSKPNHCVKQSM; VRSKPNHCVKQSMQ; QSIQTKGSFLKNFL; SIQTKGSFLKNFLF; IQTKGSFLKNFLFK; QTKGSFLKNFLFKC; TKGSFLKNFLFKCL; KGSFLKNFLFKCLN; GSFLKNFLFKCLNL; SFLKNFLFKCLNLS; HSMQGQCTEGFLEQ; SMQGQCTEGFLEQI; MQGQCTEGFLEQIG; QGQCTEGFLEQIGH; GQCTEGFLEQIGHS; QCTEGFLEQIGHSL; CTEGFLEQIGHSLQ; TEGFLEQIGHSLQY; EGFLEQIGHSLQYR; GFLEQIGHSLQYRV; FLEQIGHSLQYRVS; LEQIGHSLQYRVSG; EQIGHSLQYRVSGQ; QIGHSLQYRVSGQR; IGHSLQYRVSGQRG; GHSLQYRVSGQRGK; HSLQYRVSGQRGKS; SLQYRVSGQRGKSA; LQYRVSGQRGKSAQ; QYRVSGQRGKSAQT; YRVSGQRGKSAQTS; RVSGQRGKSAQTSE; VSGQRGKSAQTSEL; SGQRGKSAQTSELL; GQRGKSAQTSELLQ; QRGKSAQTSELLQV; RGKSAQTSELLQVP; GKSAQTSELLQVPK; KSAQTSELLQVPKS; SAQTSELLQVPKSG; ATFTSCSIFLYKVF; TFTSCSIFLYKVFI; FTSCSIFLYKVFIL; TSCSIFLYKVFILF; SCSIFLYKVFILFI; CSIFLYKVFILFIL; SIFLYKVFILFILS; IFLYKVFILFILSS; FLYKVFILFILSSS; LYKVFILFILSSSP; YKVFILFILSSSPP; KVFILFILSSSPPL; VFILFILSSSPPLS; FILFILSSSPPLSG; AFLIKGRFPQAALS; FLIKGRFPQAALSR; LIKGRFPQAALSRP; IKGRFPQAALSRPK; KGRFPQAALSRPKR; GRFPQAALSRPKRS; RFPQAALSRPKRSM; FPQAALSRPKRSMS; PQAALSRPKRSMSS; QAALSRPKRSMSSM; AALSRPKRSMSSMD; ALSRPKRSMSSMDS; LSRPKRSMSSMDSS; SRPKRSMSSMDSSL; RPKRSMSSMDSSLL; PKRSMSSMDSSLLR; KRSMSSMDSSLLRT; RSMSSMDSSLLRTL; SMSSMDSSLLRTLS 15 mers: FCKNCKRIGISPNSF; CKNCKRIGISPNSFA; KNCKRIGISPNSFAR; NCKRIGISPNSFARP; CKRIGISPNSFARPQ; KRIGISPNSFARPQK; RIGISPNSFARPQKK; IGISPNSFARPQKKP; GISPNSFARPQKKPP; ISPNSFARPQKKPPH; SPNSFARPQKKPPHP; PNSFARPQKKPPHPY; NSFARPQKKPPHPYY; SFARPQKKPPHPYYL; FARPQKKPPHPYYLR; ARPQKKPPHPYYLRE; RPQKKPPHPYYLRER; PQKKPPHPYYLRERV; QKKPPHPYYLRERVE; KKPPHPYYLRERVEA; KPPHPYYLRERVEAE; PPHPYYLRERVEAEA; PHPYYLRERVEAEAA; HPYYLRERVEAEAAS; PYYLRERVEAEAASA; YYLRERVEAEAASAS; YLRERVEAEAASASY; LRERVEAEAASASYI; RERVEAEAASASYIL; KKRPQGGAAYPWNAA; KRPQGGAAYPWNAAK; RPQGGAAYPWNAAKP; PQEGKCMTHRGMQPN; QEGKCMTHRGMQPNH; EGKCMTHRGMQPNHD; GKCMTHRGMQPNHDL; KCMTHRGMQPNHDLR; CMTHRGMQPNHDLRK; MTHRGMQPNHDLRKE; THRGMQPNHDLRKES; HRGMQPNHDLRKESA; LTGRSCLPMECSQTM; TGRSCLPMECSQTMT; GRSCLPMECSQTMTS; RSCLPMECSQTMTSG; SCLPMECSQTMTSGR; CLPMECSQTMTSGRK; LPMECSQTMTSGRKV; PMECSQTMTSGRKVH; MECSQTMTSGRKVHD; ECSQTMTSGRKVHDR; CSQTMTSGRKVHDRH; SQTMTSGRKVHDRHV; QTMTSGRKVHDRHVL; TMTSGRKVHDRHVLR; MTSGRKVHDRHVLRA; ESWPCPQLNWTKAMV; SWPCPQLNWTKAMVL; WPCPQLNWTKAMVLR; PCPQLNWTKAMVLRQ; CPQLNWTKAMVLRQL; PQLNWTKAMVLRQLS; QLNWTKAMVLRQLSR; LNWTKAMVLRQLSRQ; NWTKAMVLRQLSRQA; WTKAMVLRQLSRQAS; TKAMVLRQLSRQASV; KAMVLRQLSRQASVK; AMVLRQLSRQASVKV; MVLRQLSRQASVKVG; VLRQLSRQASVKVGK; LRQLSRQASVKVGKT; RQLSRQASVKVGKTW; QLSRQASVKVGKTWT; LSRQASVKVGKTWTG; SRQASVKVGKTWTGT; RQASVKVGKTWTGTK; QASVKVGKTWTGTKK; ASVKVGKTWTGTKKR; SVKVGKTWTGTKKRA; VKVGKTWTGTKKRAQ; KVGKTWTGTKKRAQR; VGKTWTGTKKRAQRI; GKTWTGTKKRAQRIF; KTWTGTKKRAQRIFI; TWTGTKKRAQRIFIF; WTGTKKRAQRIFIFI; TGTKKRAQRIFIFIL; GTKKRAQRIFIFILE; TKKRAQRIFIFILEL; KKRAQRIFIFILELL; KRAQRIFIFILELLL; RAQRIFIFILELLLE; AQRIFIFILELLLEF; QRIFIFILELLLEFC; RIFIFILELLLEFCR; IFIFILELLLEFCRG; FIFILELLLEFCRGE; IFILELLLEFCRGED; FILELLLEFCRGEDS; ILELLLEFCRGEDSV; LELLLEFCRGEDSVD; ELLLEFCRGEDSVDG; LLLEFCRGEDSVDGK; LLEFCRGEDSVDGKN; LEFCRGEDSVDGKNK; EFCRGEDSVDGKNKS; FCRGEDSVDGKNKST; CRGEDSVDGKNKSTT; RGEDSVDGKNKSTTA; GEDSVDGKNKSTTAL; EDSVDGKNKSTTALP; DSVDGKNKSTTALPA; SVDGKNKSTTALPAV; VDGKNKSTTALPAVK; DGKNKSTTALPAVKD; GKNKSTTALPAVKDS; KNKSTTALPAVKDSV; NKSTTALPAVKDSVK; KSTTALPAVKDSVKD; STTALPAVKDSVKDS; VSNPFFFVFPGSWVL; SNPFFFVFPGSWVLL; LPVYLRLLLPQDFQW; PVYLRLLLPQDFQWL; VYLRLLLPQDFQWLK; YLRLLLPQDFQWLKL; LRLLLPQDFQWLKLL; RLLLPQDFQWLKLLL; LLLPQDFQWLKLLLG; LLPQDFQWLKLLLGR; LPQDFQWLKLLLGRL; PQDFQWLKLLLGRLL; QDFQWLKLLLGRLLL; DFQWLKLLLGRLLLL; ASISNQAWLWNCLTQ; SISNQAWLWNCLTQM; ISNQAWLWNCLTQMS; SNQAWLWNCLTQMST; NQAWLWNCLTQMSTM; QAWLWNCLTQMSTMI; AWLWNCLTQMSTMIF; WLWNCLTQMSTMIFC; LWNCLTQMSTMIFCF; WNCLTQMSTMIFCFL; NCLTQMSTMIFCFLV; ILLLIIFNTLILGIG; LLLIIFNTLILGIGV; LLIIFNTLILGIGVL; LIIFNTLILGIGVLL; IIFNTLILGIGVLLC; IFNTLILGIGVLLCL; FNTLILGIGVLLCLL; NTLILGIGVLLCLLL; TLILGIGVLLCLLLF; LILGIGVLLCLLLFP; ILGIGVLLCLLLFPR; LGIGVLLCLLLFPRL; GIGVLLCLLLFPRLC; IGVLLCLLLFPRLCG; GVLLCLLLFPRLCGM; VLLCLLLFPRLCGML; LLCLLLFPRLCGMLL; LCLLLFPRLCGMLLG; CLLLFPRLCGMLLGM; LLLFPRLCGMLLGMI; LLFPRLCGMLLGMIY; LFPRLCGMLLGMIYL; FPRLCGMLLGMIYLL; PHRNCREEQKDFLET; HRNCREEQKDFLETP; RNCREEQKDFLETPW; NCREEQKDFLETPWL; CREEQKDFLETPWLD; REEQKDFLETPWLDF; EEQKDFLETPWLDFW; EQKDFLETPWLDFWR; QKDFLETPWLDFWRK; KDFLETPWLDFWRKL; DFLETPWLDFWRKLP; FLETPWLDFWRKLPG; LETPWLDFWRKLPGQ; ETPWLDFWRKLPGQL; TFIIIFNNIILIFPL; FIIIFNNIILIFPLL; IIIFNNIILIFPLLG; IIFNNIILIFPLLGP; IFNNIILIFPLLGPQ; FNNIILIFPLLGPQW; NNIILIFPLLGPQWL; NIILIFPLLGPQWLD; IILIFPLLGPQWLDK; LKGKVPVYILAILIV; KKLLPQEVLIKELLL; KLLPQEVLIKELLLN; LLPQEVLIKELLLNG; LPQEVLIKELLLNGC; PQEVLIKELLLNGCC; QEVLIKELLLNGCCL; EVLIKELLLNGCCLY; VLIKELLLNGCCLYF; HLLLKHMKMAPTKRK; LLLKHMKMAPTKRKG; LLKHMKMAPTKRKGE; LKHMKMAPTKRKGEC; KHMKMAPTKRKGECP; HMKMAPTKRKGECPG; MKMAPTKRKGECPGA; KMAPTKRKGECPGAA; MAPTKRKGECPGAAP; APTKRKGECPGAAPK; PTKRKGECPGAAPKK; TKRKGECPGAAPKKP; KRKGECPGAAPKKPK; RKGECPGAAPKKPKE; KGECPGAAPKKPKEP; GECPGAAPKKPKEPV; ECPGAAPKKPKEPVQ; CPGAAPKKPKEPVQV; PGAAPKKPKEPVQVP; GAAPKKPKEPVQVPK; AAPKKPKEPVQVPKL; APKKPKEPVQVPKLL; PKKPKEPVQVPKLLI; KKPKEPVQVPKLLIK; KPKEPVQVPKLLIKG; PKEPVQVPKLLIKGG; KEPVQVPKLLIKGGV; EPVQVPKLLIKGGVE; PVQVPKLLIKGGVEV; VQVPKLLIKGGVEVL; QVPKLLIKGGVEVLE; VPKLLIKGGVEVLEV; PKLLIKGGVEVLEVK; KLLIKGGVEVLEVKT; LLIKGGVEVLEVKTG; LIKGGVEVLEVKTGV; IKGGVEVLEVKTGVD; KGGVEVLEVKTGVDA; GGVEVLEVKTGVDAI; GVEVLEVKTGVDAIT; VEVLEVKTGVDAITE; EVLEVKTGVDAITEV; VLEVKTGVDAITEVE; LEVKTGVDAITEVEC; EVKTGVDAITEVECF; VKTGVDAITEVECFL; KTGVDAITEVECFLN; TGVDAITEVECFLNP; GVDAITEVECFLNPE; VDAITEVECFLNPEM; DAITEVECFLNPEMG; AITEVECFLNPEMGD; ITEVECFLNPEMGDP; TEVECFLNPEMGDPD; EVECFLNPEMGDPDE; VECFLNPEMGDPDEN; ECFLNPEMGDPDENL; CFLNPEMGDPDENLR; FLNPEMGDPDENLRG; LNPEMGDPDENLRGF; NPEMGDPDENLRGFS; PEMGDPDENLRGFSL; EMGDPDENLRGFSLK; MGDPDENLRGFSLKL; GDPDENLRGFSLKLS; DPDENLRGFSLKLSA; PDENLRGFSLKLSAE; DENLRGFSLKLSAEN; ENLRGFSLKLSAEND; NLRGFSLKLSAENDF; LRGFSLKLSAENDFS; RGFSLKLSAENDFSS; GFSLKLSAENDFSSD; FSLKLSAENDFSSDS; SLKLSAENDFSSDSP; LKLSAENDFSSDSPE; KLSAENDFSSDSPER; LSAENDFSSDSPERK; SAENDFSSDSPERKM; AENDFSSDSPERKML; ENDFSSDSPERKMLP; NDFSSDSPERKMLPC; DFSSDSPERKMLPCY; FSSDSPERKMLPCYS; SSDSPERKMLPCYST; SDSPERKMLPCYSTA; DSPERKMLPCYSTAR; SPERKMLPCYSTARI; PERKMLPCYSTARIP; ERKMLPCYSTARIPL; RKMLPCYSTARIPLP; KMLPCYSTARIPLPN; MLPCYSTARIPLPNL; LPCYSTARIPLPNLN; PCYSTARIPLPNLNE; CYSTARIPLPNLNED; YSTARIPLPNLNEDL; STARIPLPNLNEDLT; TARIPLPNLNEDLTC; ARIPLPNLNEDLTCG; RIPLPNLNEDLTCGN; IPLPNLNEDLTCGNL; PLPNLNEDLTCGNLL; LPNLNEDLTCGNLLM; PNLNEDLTCGNLLMW; NLNEDLTCGNLLMWE; LNEDLTCGNLLMWEA; NEDLTCGNLLMWEAV; EDLTCGNLLMWEAVT; DLTCGNLLMWEAVTV; LTCGNLLMWEAVTVQ; TCGNLLMWEAVTVQT; CGNLLMWEAVTVQTE; GNLLMWEAVTVQTEV; NLLMWEAVTVQTEVI; LLMWEAVTVQTEVIG; LMWEAVTVQTEVIGI; MWEAVTVQTEVIGIT; WEAVTVQTEVIGITS; EAVTVQTEVIGITSM; AVTVQTEVIGITSML; VTVQTEVIGITSMLN; TVQTEVIGITSMLNL; VQTEVIGITSMLNLH; QTEVIGITSMLNLHA; TEVIGITSMLNLHAG; EVIGITSMLNLHAGS; VIGITSMLNLHAGSQ; IGITSMLNLHAGSQK; GITSMLNLHAGSQKV; ITSMLNLHAGSQKVH; TSMLNLHAGSQKVHE; SMLNLHAGSQKVHEH; MLNLHAGSQKVHEHG; LNLHAGSQKVHEHGG; NLHAGSQKVHEHGGG; LHAGSQKVHEHGGGK; HAGSQKVHEHGGGKP; AGSQKVHEHGGGKPI; GSQKVHEHGGGKPIQ; SQKVHEHGGGKPIQG; QKVHEHGGGKPIQGS; KVHEHGGGKPIQGSN; VHEHGGGKPIQGSNF; HEHGGGKPIQGSNFH; EHGGGKPIQGSNFHF; HGGGKPIQGSNFHFF; GGGKPIQGSNFHFFA; GGKPIQGSNFHFFAV; GKPIQGSNFHFFAVG; KPIQGSNFHFFAVGG; PIQGSNFHFFAVGGE; IQGSNFHFFAVGGEP; QGSNFHFFAVGGEPL; GSNFHFFAVGGEPLE; SNFHFFAVGGEPLEM; NFHFFAVGGEPLEMQ; FHFFAVGGEPLEMQG; HFFAVGGEPLEMQGV; FFAVGGEPLEMQGVL; FAVGGEPLEMQGVLM; AVGGEPLEMQGVLMN; VGGEPLEMQGVLMNY; GGEPLEMQGVLMNYR; GEPLEMQGVLMNYRS; EPLEMQGVLMNYRSK; PLEMQGVLMNYRSKY; LEMQGVLMNYRSKYP; EMQGVLMNYRSKYPD; MQGVLMNYRSKYPDG; QGVLMNYRSKYPDGT; GVLMNYRSKYPDGTI; VLMNYRSKYPDGTIT; LMNYRSKYPDGTITP; MNYRSKYPDGTITPK; NYRSKYPDGTITPKN; YRSKYPDGTITPKNP; RSKYPDGTITPKNPT; SKYPDGTITPKNPTA; KYPDGTITPKNPTAQ; YPDGTITPKNPTAQS; PDGTITPKNPTAQSQ; DGTITPKNPTAQSQV; GTITPKNPTAQSQVM; TITPKNPTAQSQVMN; ITPKNPTAQSQVMNT; TPKNPTAQSQVMNTD; PKNPTAQSQVMNTDH; KNPTAQSQVMNTDHK; NPTAQSQVMNTDHKA; PTAQSQVMNTDHKAY; TAQSQVMNTDHKAYL; AQSQVMNTDHKAYLD; QSQVMNTDHKAYLDK; SQVMNTDHKAYLDKN; QVMNTDHKAYLDKNN; VMNTDHKAYLDKNNA; MNTDHKAYLDKNNAY; NTDHKAYLDKNNAYP; TDHKAYLDKNNAYPV; DHKAYLDKNNAYPVE; HKAYLDKNNAYPVEC; KAYLDKNNAYPVECW; AYLDKNNAYPVECWV; YLDKNNAYPVECWVP; LDKNNAYPVECWVPD; DKNNAYPVECWVPDP; KNNAYPVECWVPDPS; NNAYPVECWVPDPSR; NAYPVECWVPDPSRN; AYPVECWVPDPSRNE; YPVECWVPDPSRNEN; PVECWVPDPSRNENA; VECWVPDPSRNENAR; ECWVPDPSRNENARY; CWVPDPSRNENARYF; WVPDPSRNENARYFG; VPDPSRNENARYFGT; PDPSRNENARYFGTF; DPSRNENARYFGTFT; PSRNENARYFGTFTG; SRNENARYFGTFTGG; RNENARYFGTFTGGE; NENARYFGTFTGGEN; ENARYFGTFTGGENV; NARYFGTFTGGENVP; ARYFGTFTGGENVPP; RYFGTFTGGENVPPV; YFGTFTGGENVPPVL; FGTFTGGENVPPVLH; GTFTGGENVPPVLHV; TFTGGENVPPVLHVT; FTGGENVPPVLHVTN; TGGENVPPVLHVTNT; GGENVPPVLHVTNTA; GENVPPVLHVTNTAT; ENVPPVLHVTNTATT; NVPPVLHVTNTATTV; VPPVLHVTNTATTVL; PPVLHVTNTATTVLL; PVLHVTNTATTVLLD; VLHVTNTATTVLLDE; LHVTNTATTVLLDEQ; HVTNTATTVLLDEQG; VTNTATTVLLDEQGV; TNTATTVLLDEQGVG; NTATTVLLDEQGVGP; TATTVLLDEQGVGPL; ATTVLLDEQGVGPLC; TTVLLDEQGVGPLCK; TVLLDEQGVGPLCKA; VLLDEQGVGPLCKAD; LLDEQGVGPLCKADS; LDEQGVGPLCKADSL; DEQGVGPLCKADSLY; EQGVGPLCKADSLYV; QGVGPLCKADSLYVS; GVGPLCKADSLYVSA; VGPLCKADSLYVSAA; GPLCKADSLYVSAAD; PLCKADSLYVSAADI; LCKADSLYVSAADIC; CKADSLYVSAADICG; KADSLYVSAADICGL; ADSLYVSAADICGLF; DSLYVSAADICGLFT; SLYVSAADICGLFTN; LYVSAADICGLFTNS; YVSAADICGLFTNSS; VSAADICGLFTNSSG; SAADICGLFTNSSGT; AADICGLFTNSSGTQ; ADICGLFTNSSGTQQ; DICGLFTNSSGTQQW; ICGLFTNSSGTQQWR; CGLFTNSSGTQQWRG; GLFTNSSGTQQWRGL; LFTNSSGTQQWRGLA; FTNSSGTQQWRGLAR; TNSSGTQQWRGLARY; NSSGTQQWRGLARYF; SSGTQQWRGLARYFK; SGTQQWRGLARYFKI; GTQQWRGLARYFKIR; TQQWRGLARYFKIRL; QQWRGLARYFKIRLR; QWRGLARYFKIRLRK; WRGLARYFKIRLRKR; RGLARYFKIRLRKRS; GLARYFKIRLRKRSV; LARYFKIRLRKRSVK; ARYFKIRLRKRSVKN; RYFKIRLRKRSVKNP; YFKIRLRKRSVKNPY; FKIRLRKRSVKNPYP; KIRLRKRSVKNPYPI; IRLRKRSVKNPYPIS; RLRKRSVKNPYPISF; LRKRSVKNPYPISFL; RKRSVKNPYPISFLL; KRSVKNPYPISFLLS; RSVKNPYPISFLLSD; SVKNPYPISFLLSDL; VKNPYPISFLLSDLI; KNPYPISFLLSDLIN; NPYPISFLLSDLINR; PYPISFLLSDLINRR; YPISFLLSDLINRRT; PISFLLSDLINRRTQ; ISFLLSDLINRRTQR; SFLLSDLINRRTQRV; FLLSDLINRRTQRVD; LLSDLINRRTQRVDG; LSDLINRRTQRVDGQ; SDLINRRTQRVDGQP; DLINRRTQRVDGQPM; LINRRTQRVDGQPMY; INRRTQRVDGQPMYG; NRRTQRVDGQPMYGM; RRTQRVDGQPMYGME; RTQRVDGQPMYGMES; TQRVDGQPMYGMESQ; QRVDGQPMYGMESQV; RVDGQPMYGMESQVE; VDGQPMYGMESQVEE; DGQPMYGMESQVEEV; GQPMYGMESQVEEVR; QPMYGMESQVEEVRV; PMYGMESQVEEVRVF; MYGMESQVEEVRVFD; YGMESQVEEVRVFDG; GMESQVEEVRVFDGT; MESQVEEVRVFDGTE; ESQVEEVRVFDGTER; SQVEEVRVFDGTERL; QVEEVRVFDGTERLP; VEEVRVFDGTERLPG; EEVRVFDGTERLPGD; EVRVFDGTERLPGDP; VRVFDGTERLPGDPD; RVFDGTERLPGDPDM; VFDGTERLPGDPDMI; FDGTERLPGDPDMIR; DGTERLPGDPDMIRY; GTERLPGDPDMIRYI; TERLPGDPDMIRYID; ERLPGDPDMIRYIDK; RLPGDPDMIRYIDKQ; LPGDPDMIRYIDKQG; PGDPDMIRYIDKQGQ; GDPDMIRYIDKQGQL; DPDMIRYIDKQGQLQ; PDMIRYIDKQGQLQT; DMIRYIDKQGQLQTK; MIRYIDKQGQLQTKM; IRYIDKQGQLQTKML; TGAFIVHIHLINAAF; GAFIVHIHLINAAFV; ATFKLVLFWGWCFRP; TFKLVLFWGWCFRPF; FKLVLFWGWCFRPFK; KLVLFWGWCFRPFKT; LVLFWGWCFRPFKTL; VLFWGWCFRPFKTLK; LFWGWCFRPFKTLKA; FWGWCFRPFKTLKAF; WGWCFRPFKTLKAFT; GWCFRPFKTLKAFTQ; WCFRPFKTLKAFTQM; CFRPFKTLKAFTQMQ; FRPFKTLKAFTQMQL; RPFKTLKAFTQMQLL; PFKTLKAFTQMQLLT; FKTLKAFTQMQLLTM; KTLKAFTQMQLLTMG; TLKAFTQMQLLTMGV; ILFSCNIKNTFPHAY; LFSCNIKNTFPHAYI; FSCNIKNTFPHAYII; SCNIKNTFPHAYIIF; CNIKNTFPHAYIIFH; NIKNTFPHAYIIFHP; KSIHTYLRIQPFLPF; SIHTYLRIQPFLPFN; IHTYLRIQPFLPFNN; HTYLRIQPFLPFNNS; TYLRIQPFLPFNNSR; YLRIQPFLPFNNSRL; LRIQPFLPFNNSRLY; RIQPFLPFNNSRLYI; IQPFLPFNNSRLYIS; QPFLPFNNSRLYISC; PFLPFNNSRLYISCK; FLPFNNSRLYISCKI; LPFNNSRLYISCKIS; PFNNSRLYISCKISY; FNNSRLYISCKISYR; NNSRLYISCKISYRP; NSRLYISCKISYRPK; SRLYISCKISYRPKP; RLYISCKISYRPKPN; IYFGPKIYLSYKSSL; YFGPKIYLSYKSSLQ; FGPKIYLSYKSSLQG; GPKIYLSYKSSLQGF; PKIYLSYKSSLQGFR; KIYLSYKSSLQGFRD; IYLSYKSSLQGFRDR; YLSYKSSLQGFRDRI; LSYKSSLQGFRDRIL; SYKSSLQGFRDRILI; YKSSLQGFRDRILIH; KSSLQGFRDRILIHC; SSLQGFRDRILIHCN; SLQGFRDRILIHCNQ; LQGFRDRILIHCNQA; QGFRDRILIHCNQAW; GFRDRILIHCNQAWW; FRDRILIHCNQAWWK; RDRILIHCNQAWWKY; DRILIHCNQAWWKYL; RILIHCNQAWWKYLG; ILIHCNQAWWKYLGS; LIHCNQAWWKYLGSF; IHCNQAWWKYLGSFV; FSSCPFYIFKNNHVL; SSCPFYIFKNNHVLI; SCPFYIFKNNHVLIY; CPFYIFKNNHVLIYS; PFYIFKNNHVLIYSY; FYIFKNNHVLIYSYT; PVSSFRYIENNTVQK; VSSFRYIENNTVQKI; SSFRYIENNTVQKIK; SFRYIENNTVQKIKY; FRYIENNTVQKIKYY; RYIENNTVQKIKYYR; YIENNTVQKIKYYRI; IENNTVQKIKYYRIH; ENNTVQKIKYYRIHF; NNTVQKIKYYRIHFR; HFFPGHMKGIYSFFS; NCIYCLLTNTFLIFT; CIYCLLTNTFLIFTF; IYCLLTNTFLIFTFC; YCLLTNTFLIFTFCK; CLLTNTFLIFTFCKN; LLTNTFLIFTFCKNN; LTNTFLIFTFCKNNS; TNTFLIFTFCKNNSI; NTFLIFTFCKNNSIC; TFLIFTFCKNNSICK; FLIFTFCKNNSICKV; LIFTFCKNNSICKVL; IFTFCKNNSICKVLF; FTFCKNNSICKVLFM; TFCKNNSICKVLFMI; FCKNNSICKVLFMIL; CKNNSICKVLFMILK; KNNSICKVLFMILKV; NNSICKVLFMILKVI; NSICKVLFMILKVIR; SICKVLFMILKVIRL; ICKVLFMILKVIRLV; CKVLFMILKVIRLVF; KVLFMILKVIRLVFF; VLFMILKVIRLVFFL; LFMILKVIRLVFFLT; FMILKVIRLVFFLTL; MILKVIRLVFFLTLF; ILKVIRLVFFLTLFT; LKVIRLVFFLTLFTL; KVIRLVFFLTLFTLL; VIRLVFFLTLFTLLY; IRLVFFLTLFTLLYI; RLVFFLTLFTLLYIV; LVFFLTLFTLLYIVL; VFFLTLFTLLYIVLK; FFLTLFTLLYIVLKF; FPRHLLCFFRLFWAK; PRHLLCFFRLFWAKI; RHLLCFFRLFWAKIM; HLLCFFRLFWAKIML; LLCFFRLFWAKIMLL; APLNAFFYSMVWISS; KTKGTQLLTEIINCR; TKGTQLLTEIINCRN; KGTQLLTEIINCRNS; GTQLLTEIINCRNSM; TQLLTEIINCRNSMS; QLLTEIINCRNSMSM; LLTEIINCRNSMSMW; LTEIINCRNSMSMWS; KEYNIMPSTHVSTNK; EYNIMPSTHVSTNKS; YNIMPSTHVSTNKSY; NIMPSTHVSTNKSYR; IMPSTHVSTNKSYRI; MPSTHVSTNKSYRIF; PSTHVSTNKSYRIFF; STHVSTNKSYRIFFH; THVSTNKSYRIFFHK; HVSTNKSYRIFFHKF; VSTNKSYRIFFHKFF; STNKSYRIFFHKFFI; TNKSYRIFFHKFFIQ; NKSYRIFFHKFFIQN; KSYRIFFHKFFIQNL; SYRIFFHKFFIQNLS; YRIFFHKFFIQNLSF; RIFFHKFFIQNLSFF; IFFHKFFIQNLSFFF; FFHKFFIQNLSFFFS; FHKFFIQNLSFFFSS; HKFFIQNLSFFFSSI; KFFIQNLSFFFSSIH; FFIQNLSFFFSSIHS; FIQNLSFFFSSIHSK; IQNLSFFFSSIHSKA; QNLSFFFSSIHSKAG; NLSFFFSSIHSKAGK; LSFFFSSIHSKAGKG; SFFFSSIHSKAGKGS; FFFSSIHSKAGKGSI; FFSSIHSKAGKGSIT; FSSIHSKAGKGSITK; SSIHSKAGKGSITKY; SIHSKAGKGSITKYS; IHSKAGKGSITKYSL; HSKAGKGSITKYSLT; SKAGKGSITKYSLTK; KAGKGSITKYSLTKK; AGKGSITKYSLTKKL; GKGSITKYSLTKKLV; IRGKVFRVFYLSFFF; RGKVFRVFYLSFFFG; GKVFRVFYLSFFFGW; KVFRVFYLSFFFGWC; VLRICCCFFITGKHI; LRICCCFFITGKHIF; RICCCFFITGKHIFM; ICCCFFITGKHIFMA; CCCFFITGKHIFMAK; IFIPFFIKGTPPGLP; FIPFFIKGTPPGLPL; IPFFIKGTPPGLPLF; PFFIKGTPPGLPLFC; FFIKGTPPGLPLFCS; FIKGTPPGLPLFCSI; IKGTPPGLPLFCSIG; KGTPPGLPLFCSIGW; GTPPGLPLFCSIGWH; TPPGLPLFCSIGWHL; SFRSLKGVSPIIWTH; FRSLKGVSPIIWTHH; RSLKGVSPIIWTHHC; SLKGVSPIIWTHHCR; LKGVSPIIWTHHCRV; KGVSPIIWTHHCRVS; GVSPIIWTHHCRVSS; VSPIIWTHHCRVSSV; SPIIWTHHCRVSSVR; PIIWTHHCRVSSVRS; IIWTHHCRVSSVRSK; IWTHHCRVSSVRSKP; WTHHCRVSSVRSKPN; THHCRVSSVRSKPNH; HHCRVSSVRSKPNHC; HCRVSSVRSKPNHCV; CRVSSVRSKPNHCVK; RVSSVRSKPNHCVKQ; VSSVRSKPNHCVKQS; SSVRSKPNHCVKQSM; SVRSKPNHCVKQSMQ; QSIQTKGSFLKNFLF; SIQTKGSFLKNFLFK; IQTKGSFLKNFLFKC; QTKGSFLKNFLFKCL; TKGSFLKNFLFKCLN; KGSFLKNFLFKCLNL; GSFLKNFLFKCLNLS; HSMQGQCTEGFLEQI; SMQGQCTEGFLEQIG; MQGQCTEGFLEQIGH; QGQCTEGFLEQIGHS; GQCTEGFLEQIGHSL; QCTEGFLEQIGHSLQ; CTEGFLEQIGHSLQY; TEGFLEQIGHSLQYR; EGFLEQIGHSLQYRV; GFLEQIGHSLQYRVS; FLEQIGHSLQYRVSG; LEQIGHSLQYRVSGQ; EQIGHSLQYRVSGQR; QIGHSLQYRVSGQRG; IGHSLQYRVSGQRGK; GHSLQYRVSGQRGKS; HSLQYRVSGQRGKSA; SLQYRVSGQRGKSAQ; LQYRVSGQRGKSAQT; QYRVSGQRGKSAQTS; YRVSGQRGKSAQTSE; RVSGQRGKSAQTSEL; VSGQRGKSAQTSELL; SGQRGKSAQTSELLQ; GQRGKSAQTSELLQV; QRGKSAQTSELLQVP; RGKSAQTSELLQVPK; GKSAQTSELLQVPKS; KSAQTSELLQVPKSG; ATFTSCSIFLYKVFI; TFTSCSIFLYKVFIL; FTSCSIFLYKVFILF; TSCSIFLYKVFILFI; SCSIFLYKVFILFIL; CSIFLYKVFILFILS; SIFLYKVFILFILSS; IFLYKVFILFILSSS; FLYKVFILFILSSSP; LYKVFILFILSSSPP; YKVFILFILSSSPPL; KVFILFILSSSPPLS; VFILFILSSSPPLSG; AFLIKGRFPQAALSR; FLIKGRFPQAALSRP; LIKGRFPQAALSRPK; IKGRFPQAALSRPKR; KGRFPQAALSRPKRS; GRFPQAALSRPKRSM; RFPQAALSRPKRSMS; FPQAALSRPKRSMSS; PQAALSRPKRSMSSM; QAALSRPKRSMSSMD; AALSRPKRSMSSMDS; ALSRPKRSMSSMDSS; LSRPKRSMSSMDSSL; SRPKRSMSSMDSSLL; RPKRSMSSMDSSLLR; PKRSMSSMDSSLLRT; KRSMSSMDSSLLRTL; RSMSSMDSSLLRTLS 16 mers: FCKNCKRIGISPNSFA; CKNCKRIGISPNSFAR; KNCKRIGISPNSFARP; NCKRIGISPNSFARPQ; CKRIGISPNSFARPQK; KRIGISPNSFARPQKK; RIGISPNSFARPQKKP; IGISPNSFARPQKKPP; GISPNSFARPQKKPPH; ISPNSFARPQKKPPHP; SPNSFARPQKKPPHPY; PNSFARPQKKPPHPYY; NSFARPQKKPPHPYYL; SFARPQKKPPHPYYLR; FARPQKKPPHPYYLRE; ARPQKKPPHPYYLRER; RPQKKPPHPYYLRERV; PQKKPPHPYYLRERVE; QKKPPHPYYLRERVEA; KKPPHPYYLRERVEAE; KPPHPYYLRERVEAEA; PPHPYYLRERVEAEAA; PHPYYLRERVEAEAAS; HPYYLRERVEAEAASA; PYYLRERVEAEAASAS; YYLRERVEAEAASASY; YLRERVEAEAASASYI; LRERVEAEAASASYIL; KKRPQGGAAYPWNAAK; KRPQGGAAYPWNAAKP; PQEGKCMTHRGMQPNH; QEGKCMTHRGMQPNHD; EGKCMTHRGMQPNHDL; GKCMTHRGMQPNHDLR; KCMTHRGMQPNHDLRK; CMTHRGMQPNHDLRKE; MTHRGMQPNHDLRKES; THRGMQPNHDLRKESA; LTGRSCLPMECSQTMT; TGRSCLPMECSQTMTS; GRSCLPMECSQTMTSG; RSCLPMECSQTMTSGR; SCLPMECSQTMTSGRK; CLPMECSQTMTSGRKV; LPMECSQTMTSGRKVH; PMECSQTMTSGRKVHD; MECSQTMTSGRKVHDR; ECSQTMTSGRKVHDRH; CSQTMTSGRKVHDRHV; SQTMTSGRKVHDRHVL; QTMTSGRKVHDRHVLR; TMTSGRKVHDRHVLRA; ESWPCPQLNWTKAMVL; SWPCPQLNWTKAMVLR; WPCPQLNWTKAMVLRQ; PCPQLNWTKAMVLRQL; CPQLNWTKAMVLRQLS; PQLNWTKAMVLRQLSR; QLNWTKAMVLRQLSRQ; LNWTKAMVLRQLSRQA; NWTKAMVLRQLSRQAS; WTKAMVLRQLSRQASV; TKAMVLRQLSRQASVK; KAMVLRQLSRQASVKV; AMVLRQLSRQASVKVG; MVLRQLSRQASVKVGK; VLRQLSRQASVKVGKT; LRQLSRQASVKVGKTW; RQLSRQASVKVGKTWT; QLSRQASVKVGKTWTG; LSRQASVKVGKTWTGT; SRQASVKVGKTWTGTK; RQASVKVGKTWTGTKK; QASVKVGKTWTGTKKR; ASVKVGKTWTGTKKRA; SVKVGKTWTGTKKRAQ; VKVGKTWTGTKKRAQR; KVGKTWTGTKKRAQRI; VGKTWTGTKKRAQRIF; GKTWTGTKKRAQRIFI; KTWTGTKKRAQRIFIF; TWTGTKKRAQRIFIFI; WTGTKKRAQRIFIFIL; TGTKKRAQRIFIFILE; GTKKRAQRIFIFILEL; TKKRAQRIFIFILELL; KKRAQRIFIFILELLL; KRAQRIFIFILELLLE; RAQRIFIFILELLLEF; AQRIFIFILELLLEFC; QRIFIFILELLLEFCR; RIFIFILELLLEFCRG; IFIFILELLLEFCRGE; FIFILELLLEFCRGED; IFILELLLEFCRGEDS; FILELLLEFCRGEDSV; ILELLLEFCRGEDSVD; LELLLEFCRGEDSVDG; ELLLEFCRGEDSVDGK; LLLEFCRGEDSVDGKN; LLEFCRGEDSVDGKNK; LEFCRGEDSVDGKNKS; EFCRGEDSVDGKNKST; FCRGEDSVDGKNKSTT; CRGEDSVDGKNKSTTA; RGEDSVDGKNKSTTAL; GEDSVDGKNKSTTALP; EDSVDGKNKSTTALPA; DSVDGKNKSTTALPAV; SVDGKNKSTTALPAVK; VDGKNKSTTALPAVKD; DGKNKSTTALPAVKDS; GKNKSTTALPAVKDSV; KNKSTTALPAVKDSVK; NKSTTALPAVKDSVKD; KSTTALPAVKDSVKDS; VSNPFFFVFPGSWVLL; LPVYLRLLLPQDFQWL; PVYLRLLLPQDFQWLK; VYLRLLLPQDFQWLKL; YLRLLLPQDFQWLKLL; LRLLLPQDFQWLKLLL; RLLLPQDFQWLKLLLG; LLLPQDFQWLKLLLGR; LLPQDFQWLKLLLGRL; LPQDFQWLKLLLGRLL; PQDFQWLKLLLGRLLL; QDFQWLKLLLGRLLLL; ASISNQAWLWNCLTQM; SISNQAWLWNCLTQMS; ISNQAWLWNCLTQMST; SNQAWLWNCLTQMSTM; NQAWLWNCLTQMSTMI; QAWLWNCLTQMSTMIF; AWLWNCLTQMSTMIFC; WLWNCLTQMSTMIFCF; LWNCLTQMSTMIFCFL; WNCLTQMSTMIFCFLV; ILLLIIFNTLILGIGV; LLLIIFNTLILGIGVL; LLIIFNTLILGIGVLL; LIIFNTLILGIGVLLC; IIFNTLILGIGVLLCL; IFNTLILGIGVLLCLL; FNTLILGIGVLLCLLL; NTLILGIGVLLCLLLF; TLILGIGVLLCLLLFP; LILGIGVLLCLLLFPR; ILGIGVLLCLLLFPRL; LGIGVLLCLLLFPRLC; GIGVLLCLLLFPRLCG; IGVLLCLLLFPRLCGM; GVLLCLLLFPRLCGML; VLLCLLLFPRLCGMLL; LLCLLLFPRLCGMLLG; LCLLLFPRLCGMLLGM; CLLLFPRLCGMLLGMI; LLLFPRLCGMLLGMIY; LLFPRLCGMLLGMIYL; LFPRLCGMLLGMIYLL; PHRNCREEQKDFLETP; HRNCREEQKDFLETPW; RNCREEQKDFLETPWL; NCREEQKDFLETPWLD; CREEQKDFLETPWLDF; REEQKDFLETPWLDFW; EEQKDFLETPWLDFWR; EQKDFLETPWLDFWRK; QKDFLETPWLDFWRKL; KDFLETPWLDFWRKLP; DFLETPWLDFWRKLPG; FLETPWLDFWRKLPGQ; LETPWLDFWRKLPGQL; TFIIIFNNIILIFPLL; FIIIFNNIILIFPLLG; IIIFNNIILIFPLLGP; IIFNNIILIFPLLGPQ; IFNNIILIFPLLGPQW; FNNIILIFPLLGPQWL; NNIILIFPLLGPQWLD; NIILIFPLLGPQWLDK; KKLLPQEVLIKELLLN; KLLPQEVLIKELLLNG; LLPQEVLIKELLLNGC; LPQEVLIKELLLNGCC; PQEVLIKELLLNGCCL; QEVLIKELLLNGCCLY; EVLIKELLLNGCCLYF; HLLLKHMKMAPTKRKG; LLLKHMKMAPTKRKGE; LLKHMKMAPTKRKGEC; LKHMKMAPTKRKGECP; KHMKMAPTKRKGECPG; HMKMAPTKRKGECPGA; MKMAPTKRKGECPGAA; KMAPTKRKGECPGAAP; MAPTKRKGECPGAAPK; APTKRKGECPGAAPKK; PTKRKGECPGAAPKKP; TKRKGECPGAAPKKPK; KRKGECPGAAPKKPKE; RKGECPGAAPKKPKEP; KGECPGAAPKKPKEPV; GECPGAAPKKPKEPVQ; ECPGAAPKKPKEPVQV; CPGAAPKKPKEPVQVP; PGAAPKKPKEPVQVPK; GAAPKKPKEPVQVPKL; AAPKKPKEPVQVPKLL; APKKPKEPVQVPKLLI; PKKPKEPVQVPKLLIK; KKPKEPVQVPKLLIKG; KPKEPVQVPKLLIKGG; PKEPVQVPKLLIKGGV; KEPVQVPKLLIKGGVE; EPVQVPKLLIKGGVEV; PVQVPKLLIKGGVEVL; VQVPKLLIKGGVEVLE; QVPKLLIKGGVEVLEV; VPKLLIKGGVEVLEVK; PKLLIKGGVEVLEVKT; KLLIKGGVEVLEVKTG; LLIKGGVEVLEVKTGV; LIKGGVEVLEVKTGVD; IKGGVEVLEVKTGVDA; KGGVEVLEVKTGVDAI; GGVEVLEVKTGVDAIT; GVEVLEVKTGVDAITE; VEVLEVKTGVDAITEV; EVLEVKTGVDAITEVE; VLEVKTGVDAITEVEC; LEVKTGVDAITEVECF; EVKTGVDAITEVECFL; VKTGVDAITEVECFLN; KTGVDAITEVECFLNP; TGVDAITEVECFLNPE; GVDAITEVECFLNPEM; VDAITEVECFLNPEMG; DAITEVECFLNPEMGD; AITEVECFLNPEMGDP; ITEVECFLNPEMGDPD; TEVECFLNPEMGDPDE; EVECFLNPEMGDPDEN; VECFLNPEMGDPDENL; ECFLNPEMGDPDENLR; CFLNPEMGDPDENLRG; FLNPEMGDPDENLRGF; LNPEMGDPDENLRGFS; NPEMGDPDENLRGFSL; PEMGDPDENLRGFSLK; EMGDPDENLRGFSLKL; MGDPDENLRGFSLKLS; GDPDENLRGFSLKLSA; DPDENLRGFSLKLSAE; PDENLRGFSLKLSAEN; DENLRGFSLKLSAEND; ENLRGFSLKLSAENDF; NLRGFSLKLSAENDFS; LRGFSLKLSAENDFSS; RGFSLKLSAENDFSSD; GFSLKLSAENDFSSDS; FSLKLSAENDFSSDSP; SLKLSAENDFSSDSPE; LKLSAENDFSSDSPER; KLSAENDFSSDSPERK; LSAENDFSSDSPERKM; SAENDFSSDSPERKML; AENDFSSDSPERKMLP; ENDFSSDSPERKMLPC; NDFSSDSPERKMLPCY; DFSSDSPERKMLPCYS; FSSDSPERKMLPCYST; SSDSPERKMLPCYSTA; SDSPERKMLPCYSTAR; DSPERKMLPCYSTARI; SPERKMLPCYSTARIP; PERKMLPCYSTARIPL; ERKMLPCYSTARIPLP; RKMLPCYSTARIPLPN; KMLPCYSTARIPLPNL; MLPCYSTARIPLPNLN; LPCYSTARIPLPNLNE; PCYSTARIPLPNLNED; CYSTARIPLPNLNEDL; YSTARIPLPNLNEDLT; STARIPLPNLNEDLTC; TARIPLPNLNEDLTCG; ARIPLPNLNEDLTCGN; RIPLPNLNEDLTCGNL; IPLPNLNEDLTCGNLL; PLPNLNEDLTCGNLLM; LPNLNEDLTCGNLLMW; PNLNEDLTCGNLLMWE; NLNEDLTCGNLLMWEA; LNEDLTCGNLLMWEAV; NEDLTCGNLLMWEAVT; EDLTCGNLLMWEAVTV; DLTCGNLLMWEAVTVQ; LTCGNLLMWEAVTVQT; TCGNLLMWEAVTVQTE; CGNLLMWEAVTVQTEV; GNLLMWEAVTVQTEVI; NLLMWEAVTVQTEVIG; LLMWEAVTVQTEVIGI; LMWEAVTVQTEVIGIT; MWEAVTVQTEVIGITS; WEAVTVQTEVIGITSM; EAVTVQTEVIGITSML; AVTVQTEVIGITSMLN; VTVQTEVIGITSMLNL; TVQTEVIGITSMLNLH; VQTEVIGITSMLNLHA; QTEVIGITSMLNLHAG; TEVIGITSMLNLHAGS; EVIGITSMLNLHAGSQ; VIGITSMLNLHAGSQK; IGITSMLNLHAGSQKV; GITSMLNLHAGSQKVH; ITSMLNLHAGSQKVHE; TSMLNLHAGSQKVHEH; SMLNLHAGSQKVHEHG; MLNLHAGSQKVHEHGG; LNLHAGSQKVHEHGGG; NLHAGSQKVHEHGGGK; LHAGSQKVHEHGGGKP; HAGSQKVHEHGGGKPI; AGSQKVHEHGGGKPIQ; GSQKVHEHGGGKPIQG; SQKVHEHGGGKPIQGS; QKVHEHGGGKPIQGSN; KVHEHGGGKPIQGSNF; VHEHGGGKPIQGSNFH; HEHGGGKPIQGSNFHF; EHGGGKPIQGSNFHFF; HGGGKPIQGSNFHFFA; GGGKPIQGSNFHFFAV; GGKPIQGSNFHFFAVG; GKPIQGSNFHFFAVGG; KPIQGSNFHFFAVGGE; PIQGSNFHFFAVGGEP; IQGSNFHFFAVGGEPL; QGSNFHFFAVGGEPLE; GSNFHFFAVGGEPLEM; SNFHFFAVGGEPLEMQ; NFHFFAVGGEPLEMQG; FHFFAVGGEPLEMQGV; HFFAVGGEPLEMQGVL; FFAVGGEPLEMQGVLM; FAVGGEPLEMQGVLMN; AVGGEPLEMQGVLMNY; VGGEPLEMQGVLMNYR; GGEPLEMQGVLMNYRS; GEPLEMQGVLMNYRSK; EPLEMQGVLMNYRSKY; PLEMQGVLMNYRSKYP; LEMQGVLMNYRSKYPD; EMQGVLMNYRSKYPDG; MQGVLMNYRSKYPDGT; QGVLMNYRSKYPDGTI; GVLMNYRSKYPDGTIT; VLMNYRSKYPDGTITP; LMNYRSKYPDGTITPK; MNYRSKYPDGTITPKN; NYRSKYPDGTITPKNP; YRSKYPDGTITPKNPT; RSKYPDGTITPKNPTA; SKYPDGTITPKNPTAQ; KYPDGTITPKNPTAQS; YPDGTITPKNPTAQSQ; PDGTITPKNPTAQSQV; DGTITPKNPTAQSQVM; GTITPKNPTAQSQVMN; TITPKNPTAQSQVMNT; ITPKNPTAQSQVMNTD; TPKNPTAQSQVMNTDH; PKNPTAQSQVMNTDHK; KNPTAQSQVMNTDHKA; NPTAQSQVMNTDHKAY; PTAQSQVMNTDHKAYL; TAQSQVMNTDHKAYLD; AQSQVMNTDHKAYLDK; QSQVMNTDHKAYLDKN; SQVMNTDHKAYLDKNN; QVMNTDHKAYLDKNNA; VMNTDHKAYLDKNNAY; MNTDHKAYLDKNNAYP; NTDHKAYLDKNNAYPV; TDHKAYLDKNNAYPVE; DHKAYLDKNNAYPVEC; HKAYLDKNNAYPVECW; KAYLDKNNAYPVECWV; AYLDKNNAYPVECWVP; YLDKNNAYPVECWVPD; LDKNNAYPVECWVPDP; DKNNAYPVECWVPDPS; KNNAYPVECWVPDPSR; NNAYPVECWVPDPSRN; NAYPVECWVPDPSRNE; AYPVECWVPDPSRNEN; YPVECWVPDPSRNENA; PVECWVPDPSRNENAR; VECWVPDPSRNENARY; ECWVPDPSRNENARYF; CWVPDPSRNENARYFG; WVPDPSRNENARYFGT; VPDPSRNENARYFGTF; PDPSRNENARYFGTFT; DPSRNENARYFGTFTG; PSRNENARYFGTFTGG; SRNENARYFGTFTGGE; RNENARYFGTFTGGEN; NENARYFGTFTGGENV; ENARYFGTFTGGENVP; NARYFGTFTGGENVPP; ARYFGTFTGGENVPPV; RYFGTFTGGENVPPVL; YFGTFTGGENVPPVLH; FGTFTGGENVPPVLHV; GTFTGGENVPPVLHVT; TFTGGENVPPVLHVTN; FTGGENVPPVLHVTNT; TGGENVPPVLHVTNTA; GGENVPPVLHVTNTAT; GENVPPVLHVTNTATT; ENVPPVLHVTNTATTV; NVPPVLHVTNTATTVL; VPPVLHVTNTATTVLL; PPVLHVTNTATTVLLD; PVLHVTNTATTVLLDE; VLHVTNTATTVLLDEQ; LHVTNTATTVLLDEQG; HVTNTATTVLLDEQGV; VTNTATTVLLDEQGVG; TNTATTVLLDEQGVGP; NTATTVLLDEQGVGPL; TATTVLLDEQGVGPLC; ATTVLLDEQGVGPLCK; TTVLLDEQGVGPLCKA; TVLLDEQGVGPLCKAD; VLLDEQGVGPLCKADS; LLDEQGVGPLCKADSL; LDEQGVGPLCKADSLY; DEQGVGPLCKADSLYV; EQGVGPLCKADSLYVS; QGVGPLCKADSLYVSA; GVGPLCKADSLYVSAA; VGPLCKADSLYVSAAD; GPLCKADSLYVSAADI; PLCKADSLYVSAADIC; LCKADSLYVSAADICG; CKADSLYVSAADICGL; KADSLYVSAADICGLF; ADSLYVSAADICGLFT; DSLYVSAADICGLFTN; SLYVSAADICGLFTNS; LYVSAADICGLFTNSS; YVSAADICGLFTNSSG; VSAADICGLFTNSSGT; SAADICGLFTNSSGTQ; AADICGLFTNSSGTQQ; ADICGLFTNSSGTQQW; DICGLFTNSSGTQQWR; ICGLFTNSSGTQQWRG; CGLFTNSSGTQQWRGL; GLFTNSSGTQQWRGLA; LFTNSSGTQQWRGLAR; FTNSSGTQQWRGLARY; TNSSGTQQWRGLARYF; NSSGTQQWRGLARYFK; SSGTQQWRGLARYFKI; SGTQQWRGLARYFKIR; GTQQWRGLARYFKIRL; TQQWRGLARYFKIRLR; QQWRGLARYFKIRLRK; QWRGLARYFKIRLRKR; WRGLARYFKIRLRKRS; RGLARYFKIRLRKRSV; GLARYFKIRLRKRSVK; LARYFKIRLRKRSVKN; ARYFKIRLRKRSVKNP; RYFKIRLRKRSVKNPY; YFKIRLRKRSVKNPYP; FKIRLRKRSVKNPYPI; KIRLRKRSVKNPYPIS; IRLRKRSVKNPYPISF; RLRKRSVKNPYPISFL; LRKRSVKNPYPISFLL; RKRSVKNPYPISFLLS; KRSVKNPYPISFLLSD; RSVKNPYPISFLLSDL; SVKNPYPISFLLSDLI; VKNPYPISFLLSDLIN; KNPYPISFLLSDLINR; NPYPISFLLSDLINRR; PYPISFLLSDLINRRT; YPISFLLSDLINRRTQ; PISFLLSDLINRRTQR; ISFLLSDLINRRTQRV; SFLLSDLINRRTQRVD; FLLSDLINRRTQRVDG; LLSDLINRRTQRVDGQ; LSDLINRRTQRVDGQP; SDLINRRTQRVDGQPM; DLINRRTQRVDGQPMY; LINRRTQRVDGQPMYG; INRRTQRVDGQPMYGM; NRRTQRVDGQPMYGME; RRTQRVDGQPMYGMES; RTQRVDGQPMYGMESQ; TQRVDGQPMYGMESQV; QRVDGQPMYGMESQVE; RVDGQPMYGMESQVEE; VDGQPMYGMESQVEEV; DGQPMYGMESQVEEVR; GQPMYGMESQVEEVRV; QPMYGMESQVEEVRVF; PMYGMESQVEEVRVFD; MYGMESQVEEVRVFDG; YGMESQVEEVRVFDGT; GMESQVEEVRVFDGTE; MESQVEEVRVFDGTER; ESQVEEVRVFDGTERL; SQVEEVRVFDGTERLP; QVEEVRVFDGTERLPG; VEEVRVFDGTERLPGD; EEVRVFDGTERLPGDP; EVRVFDGTERLPGDPD; VRVFDGTERLPGDPDM; RVFDGTERLPGDPDMI; VFDGTERLPGDPDMIR; FDGTERLPGDPDMIRY; DGTERLPGDPDMIRYI; GTERLPGDPDMIRYID; TERLPGDPDMIRYIDK; ERLPGDPDMIRYIDKQ; RLPGDPDMIRYIDKQG; LPGDPDMIRYIDKQGQ; PGDPDMIRYIDKQGQL; GDPDMIRYIDKQGQLQ; DPDMIRYIDKQGQLQT; PDMIRYIDKQGQLQTK; DMIRYIDKQGQLQTKM; MIRYIDKQGQLQTKML; TGAFIVHIHLINAAFV; ATFKLVLFWGWCFRPF; TFKLVLFWGWCFRPFK; FKLVLFWGWCFRPFKT; KLVLFWGWCFRPFKTL; LVLFWGWCFRPFKTLK; VLFWGWCFRPFKTLKA; LFWGWCFRPFKTLKAF; FWGWCFRPFKTLKAFT; WGWCFRPFKTLKAFTQ; GWCFRPFKTLKAFTQM; WCFRPFKTLKAFTQMQ; CFRPFKTLKAFTQMQL; FRPFKTLKAFTQMQLL; RPFKTLKAFTQMQLLT; PFKTLKAFTQMQLLTM; FKTLKAFTQMQLLTMG; KTLKAFTQMQLLTMGV; ILFSCNIKNTFPHAYI; LFSCNIKNTFPHAYII; FSCNIKNTFPHAYIIF; SCNIKNTFPHAYIIFH; CNIKNTFPHAYIIFHP; KSIHTYLRIQPFLPFN; SIHTYLRIQPFLPFNN; IHTYLRIQPFLPFNNS; HTYLRIQPFLPFNNSR; TYLRIQPFLPFNNSRL; YLRIQPFLPFNNSRLY; LRIQPFLPFNNSRLYI; RIQPFLPFNNSRLYIS; IQPFLPFNNSRLYISC; QPFLPFNNSRLYISCK; PFLPFNNSRLYISCKI; FLPFNNSRLYISCKIS; LPFNNSRLYISCKISY; PFNNSRLYISCKISYR; FNNSRLYISCKISYRP; NNSRLYISCKISYRPK; NSRLYISCKISYRPKP; SRLYISCKISYRPKPN; IYFGPKIYLSYKSSLQ; YFGPKIYLSYKSSLQG; FGPKIYLSYKSSLQGF; GPKIYLSYKSSLQGFR; PKIYLSYKSSLQGFRD; KIYLSYKSSLQGFRDR; IYLSYKSSLQGFRDRI; YLSYKSSLQGFRDRIL; LSYKSSLQGFRDRILI; SYKSSLQGFRDRILIH; YKSSLQGFRDRILIHC; KSSLQGFRDRILIHCN; SSLQGFRDRILIHCNQ; SLQGFRDRILIHCNQA; LQGFRDRILIHCNQAW; QGFRDRILIHCNQAWW; GFRDRILIHCNQAWWK; FRDRILIHCNQAWWKY; RDRILIHCNQAWWKYL; DRILIHCNQAWWKYLG; RILIHCNQAWWKYLGS; ILIHCNQAWWKYLGSF; LIHCNQAWWKYLGSFV; FSSCPFYIFKNNHVLI; SSCPFYIFKNNHVLIY; SCPFYIFKNNHVLIYS; CPFYIFKNNHVLIYSY; PFYIFKNNHVLIYSYT; PVSSFRYIENNTVQKI; VSSFRYIENNTVQKIK; SSFRYIENNTVQKIKY; SFRYIENNTVQKIKYY; FRYIENNTVQKIKYYR; RYIENNTVQKIKYYRI; YIENNTVQKIKYYRIH; IENNTVQKIKYYRIHF; ENNTVQKIKYYRIHFR; NCIYCLLTNTFLIFTF; CIYCLLTNTFLIFTFC; IYCLLTNTFLIFTFCK; YCLLTNTFLIFTFCKN; CLLTNTFLIFTFCKNN; LLTNTFLIFTFCKNNS; LTNTFLIFTFCKNNSI; TNTFLIFTFCKNNSIC; NTFLIFTFCKNNSICK; TFLIFTFCKNNSICKV; FLIFTFCKNNSICKVL; LIFTFCKNNSICKVLF; IFTFCKNNSICKVLFM; FTFCKNNSICKVLFMI; TFCKNNSICKVLFMIL; FCKNNSICKVLFMILK; CKNNSICKVLFMILKV; KNNSICKVLFMILKVI; NNSICKVLFMILKVIR; NSICKVLFMILKVIRL; SICKVLFMILKVIRLV; ICKVLFMILKVIRLVF; CKVLFMILKVIRLVFF; KVLFMILKVIRLVFFL; VLFMILKVIRLVFFLT; LFMILKVIRLVFFLTL; FMILKVIRLVFFLTLF; MILKVIRLVFFLTLFT; ILKVIRLVFFLTLFTL; LKVIRLVFFLTLFTLL; KVIRLVFFLTLFTLLY; VIRLVFFLTLFTLLYI; IRLVFFLTLFTLLYIV; RLVFFLTLFTLLYIVL; LVFFLTLFTLLYIVLK; VFFLTLFTLLYIVLKF; FPRHLLCFFRLFWAKI; PRHLLCFFRLFWAKIM; RHLLCFFRLFWAKIML; HLLCFFRLFWAKIMLL; KTKGTQLLTEIINCRN; TKGTQLLTEIINCRNS; KGTQLLTEIINCRNSM; GTQLLTEIINCRNSMS; TQLLTEIINCRNSMSM; QLLTEIINCRNSMSMW; LLTEIINCRNSMSMWS; KEYNIMPSTHVSTNKS; EYNIMPSTHVSTNKSY; YNIMPSTHVSTNKSYR; NIMPSTHVSTNKSYRI; IMPSTHVSTNKSYRIF; MPSTHVSTNKSYRIFF; PSTHVSTNKSYRIFFH; STHVSTNKSYRIFFHK; THVSTNKSYRIFFHKF; HVSTNKSYRIFFHKFF; VSTNKSYRIFFHKFFI; STNKSYRIFFHKFFIQ; TNKSYRIFFHKFFIQN; NKSYRIFFHKFFIQNL; KSYRIFFHKFFIQNLS; SYRIFFHKFFIQNLSF; YRIFFHKFFIQNLSFF; RIFFHKFFIQNLSFFF; IFFHKFFIQNLSFFFS; FFHKFFIQNLSFFFSS; FHKFFIQNLSFFFSSI; HKFFIQNLSFFFSSIH; KFFIQNLSFFFSSIHS; FFIQNLSFFFSSIHSK; FIQNLSFFFSSIHSKA; IQNLSFFFSSIHSKAG; QNLSFFFSSIHSKAGK; NLSFFFSSIHSKAGKG; LSFFFSSIHSKAGKGS; SFFFSSIHSKAGKGSI; FFFSSIHSKAGKGSIT; FFSSIHSKAGKGSITK; FSSIHSKAGKGSITKY; SSIHSKAGKGSITKYS; SIHSKAGKGSITKYSL; IHSKAGKGSITKYSLT; HSKAGKGSITKYSLTK; SKAGKGSITKYSLTKK; KAGKGSITKYSLTKKL; AGKGSITKYSLTKKLV; IRGKVFRVFYLSFFFG; RGKVFRVFYLSFFFGW; GKVFRVFYLSFFFGWC; VLRICCCFFITGKHIF; LRICCCFFITGKHIFM; RICCCFFITGKHIFMA; ICCCFFITGKHIFMAK; IFIPFFIKGTPPGLPL; FIPFFIKGTPPGLPLF; IPFFIKGTPPGLPLFC; PFFIKGTPPGLPLFCS; FFIKGTPPGLPLFCSI; FIKGTPPGLPLFCSIG; IKGTPPGLPLFCSIGW; KGTPPGLPLFCSIGWH; GTPPGLPLFCSIGWHL; SFRSLKGVSPIIWTHH; FRSLKGVSPIIWTHHC; RSLKGVSPIIWTHHCR; SLKGVSPIIWTHHCRV; LKGVSPIIWTHHCRVS; KGVSPIIWTHHCRVSS; GVSPIIWTHHCRVSSV; VSPIIWTHHCRVSSVR; SPIIWTHHCRVSSVRS; PIIWTHHCRVSSVRSK; IIWTHHCRVSSVRSKP; IWTHHCRVSSVRSKPN; WTHHCRVSSVRSKPNH; THHCRVSSVRSKPNHC; HHCRVSSVRSKPNHCV; HCRVSSVRSKPNHCVK; CRVSSVRSKPNHCVKQ; RVSSVRSKPNHCVKQS; VSSVRSKPNHCVKQSM; SSVRSKPNHCVKQSMQ; QSIQTKGSFLKNFLFK; SIQTKGSFLKNFLFKC; IQTKGSFLKNFLFKCL; QTKGSFLKNFLFKCLN; TKGSFLKNFLFKCLNL; KGSFLKNFLFKCLNLS; HSMQGQCTEGFLEQIG; SMQGQCTEGFLEQIGH; MQGQCTEGFLEQIGHS; QGQCTEGFLEQIGHSL; GQCTEGFLEQIGHSLQ; QCTEGFLEQIGHSLQY; CTEGFLEQIGHSLQYR; TEGFLEQIGHSLQYRV; EGFLEQIGHSLQYRVS; GFLEQIGHSLQYRVSG; FLEQIGHSLQYRVSGQ; LEQIGHSLQYRVSGQR; EQIGHSLQYRVSGQRG; QIGHSLQYRVSGQRGK; IGHSLQYRVSGQRGKS; GHSLQYRVSGQRGKSA; HSLQYRVSGQRGKSAQ; SLQYRVSGQRGKSAQT; LQYRVSGQRGKSAQTS; QYRVSGQRGKSAQTSE; YRVSGQRGKSAQTSEL; RVSGQRGKSAQTSELL; VSGQRGKSAQTSELLQ; SGQRGKSAQTSELLQV; GQRGKSAQTSELLQVP; QRGKSAQTSELLQVPK; RGKSAQTSELLQVPKS; GKSAQTSELLQVPKSG; ATFTSCSIFLYKVFIL; TFTSCSIFLYKVFILF; FTSCSIFLYKVFILFI; TSCSIFLYKVFILFIL; SCSIFLYKVFILFILS; CSIFLYKVFILFILSS; SIFLYKVFILFILSSS; IFLYKVFILFILSSSP; FLYKVFILFILSSSPP; LYKVFILFILSSSPPL; YKVFILFILSSSPPLS; KVFILFILSSSPPLSG; AFLIKGRFPQAALSRP; FLIKGRFPQAALSRPK; LIKGRFPQAALSRPKR; IKGRFPQAALSRPKRS; KGRFPQAALSRPKRSM; GRFPQAALSRPKRSMS; RFPQAALSRPKRSMSS; FPQAALSRPKRSMSSM; PQAALSRPKRSMSSMD; QAALSRPKRSMSSMDS; AALSRPKRSMSSMDSS; ALSRPKRSMSSMDSSL; LSRPKRSMSSMDSSLL; SRPKRSMSSMDSSLLR; RPKRSMSSMDSSLLRT; PKRSMSSMDSSLLRTL; KRSMSSMDSSLLRTLS BK virus, reading frame 2 13 mers: GFPQIVLLGLRKS; FPQIVLLGLRKSL; PQIVLLGLRKSLH; QIVLLGLRKSLHT; IVLLGLRKSLHTL; VLLGLRKSLHTLT; LLGLRKSLHTLTT; EKGWRQRRPRPLI; KGWRQRRPRPLIY; GWRQRRPRPLIYY; WRQRRPRPLIYYK; RQRRPRPLIYYKK; QRRPRPLIYYKKK; RRPRPLIYYKKKG; RPRPLIYYKKKGH; PRPLIYYKKKGHR; RPLIYYKKKGHRE; PLIYYKKKGHREE; LIYYKKKGHREEL; IYYKKKGHREELL; YYKKKGHREELLT; YKKKGHREELLTH; KKKGHREELLTHG; KKGHREELLTHGM; KGHREELLTHGMQ; GHREELLTHGMQP; HREELLTHGMQPN; REELLTHGMQPNH; EELLTHGMQPNHD; ELLTHGMQPNHDL; LLTHGMQPNHDLR; LTHGMQPNHDLRK; THGMQPNHDLRKE; HGMQPNHDLRKES; GMQPNHDLRKESA; LTGECSQTMTSGR; TGECSQTMTSGRK; GECSQTMTSGRKV; ECSQTMTSGRKVH; CSQTMTSGRKVHD; SQTMTSGRKVHDS; QTMTSGRKVHDSQ; TMTSGRKVHDSQG; MTSGRKVHDSQGG; TSGRKVHDSQGGA; SGRKVHDSQGGAA; GRKVHDSQGGAAY; RKVHDSQGGAAYP; KVHDSQGGAAYPW; VHDSQGGAAYPWN; HDSQGGAAYPWNA; DSQGGAAYPWNAA; SQGGAAYPWNAAK; QGGAAYPWNAAKP; PQEGKCMTDMFCE; QEGKCMTDMFCEP; EGKCMTDMFCEPR; GKCMTDMFCEPRN; KCMTDMFCEPRNL; CMTDMFCEPRNLG; MTDMFCEPRNLGL; TDMFCEPRNLGLV; DMFCEPRNLGLVP; MFCEPRNLGLVPS; TGQRPWFCASCHD; GQRPWFCASCHDK; QRPWFCASCHDKL; RPWFCASCHDKLQ; KLVKPGLEQKKEL; LVKPGLEQKKELR; VKPGLEQKKELRG; KPGLEQKKELRGF; PGLEQKKELRGFL; GLEQKKELRGFLF; LEQKKELRGFLFL; EQKKELRGFLFLF; VIPFFLYFQVHGC; IPFFLYFQVHGCC; PFFLYFQVHGCCS; FFLYFQVHGCCSS; FLYFQVHGCCSST; LYFQVHGCCSSTF; YFQVHGCCSSTFG; FQVHGCCSSTFGG; QVHGCCSSTFGGP; VHGCCSSTFGGPS; HGCCSSTFGGPSC; GCCSSTFGGPSCQ; CCSSTFGGPSCQC; CSSTFGGPSCQCI; NCCWGGCCCYRSS; CCWGGCCCYRSSN; CWGGCCCYRSSNC; WGGCCCYRSSNCI; GGCCCYRSSNCIP; GCCCYRSSNCIPC; CCCYRSSNCIPCY; CCYRSSNCIPCYC; CYRSSNCIPCYCR; YRSSNCIPCYCRG; RSSNCIPCYCRGH; SSNCIPCYCRGHN; SNCIPCYCRGHNK; NCIPCYCRGHNKY; CIPCYCRGHNKYL; IPCYCRGHNKYLR; PCYCRGHNKYLRG; CYCRGHNKYLRGY; YCRGHNKYLRGYS; CRGHNKYLRGYSC; RGHNKYLRGYSCY; GHNKYLRGYSCYR; HNKYLRGYSCYRP; NKYLRGYSCYRPN; KYLRGYSCYRPNS; YLRGYSCYRPNSS; LRGYSCYRPNSSN; RGYSCYRPNSSNI; GYSCYRPNSSNIC; YSCYRPNSSNICC; SCYRPNSSNICCN; CYRPNSSNICCNC; YRPNSSNICCNCW; RPNSSNICCNCWC; PNSSNICCNCWCS; NSSNICCNCWCSW; SSNICCNCWCSWG; SNICCNCWCSWGY; NICCNCWCSWGYC; ICCNCWCSWGYCW; CCNCWCSWGYCWV; CNCWCSWGYCWVC; NCWCSWGYCWVCC; CWCSWGYCWVCCF; WCSWGYCWVCCFN; CSWGYCWVCCFNS; SWGYCWVCCFNSN; WGYCWVCCFNSNC; LGSQSFHCRPLSA; GSQSFHCRPLSAI; SQSFHCRPLSAIR; QSFHCRPLSAIRH; SFHCRPLSAIRHG; FHCRPLSAIRHGF; HCRPLSAIRHGFG; CRPLSAIRHGFGI; RPLSAIRHGFGIV; ALGSFFVCYYFPG; LGSFFVCYYFPGF; GSFFVCYYFPGFV; SFFVCYYFPGFVA; FFVCYYFPGFVAC; FVCYYFPGFVACY; YTFYNLTGIAEKN; TFYNLTGIAEKNR; FYNLTGIAEKNRK; YNLTGIAEKNRKI; NLTGIAEKNRKIF; IFGGNYLDNCKCP; FGGNYLDNCKCPY; GGNYLDNCKCPYK; GNYLDNCKCPYKL; NYLDNCKCPYKLL; QYRRSYTKNGLKK; YRRSYTKNGLKKS; RRSYTKNGLKKST; RSYTKNGLKKSTK; SYTKNGLKKSTKC; YTKNGLKKSTKCT; TKNGLKKSTKCTF; KNGLKKSTKCTFR; NGLKKSTKCTFRR; GLKKSTKCTFRRV; LKKSTKCTFRRVY; KKSTKCTFRRVYR; KSTKCTFRRVYRK; STKCTFRRVYRKN; TKCTFRRVYRKNY; KCTFRRVYRKNYC; CTFRRVYRKNYCP; TFRRVYRKNYCPR; FRRVYRKNYCPRR; RRVYRKNYCPRRC; SKNCSSMDVAFTS; KNCSSMDVAFTSR; NCSSMDVAFTSRP; CSSMDVAFTSRPV; SSMDVAFTSRPVR; SMDVAFTSRPVRD; MDVAFTSRPVRDC; DVAFTSRPVRDCN; VAFTSRPVRDCNT; AFTSRPVRDCNTC; FTSRPVRDCNTCS; RWPQPKEKESVQG; WPQPKEKESVQGQ; PQPKEKESVQGQL; QPKEKESVQGQLP; PKEKESVQGQLPK; KEKESVQGQLPKS; EKESVQGQLPKSQ; KESVQGQLPKSQR; ESVQGQLPKSQRN; SVQGQLPKSQRNP; VQGQLPKSQRNPC; QGQLPKSQRNPCK; GQLPKSQRNPCKC; QLPKSQRNPCKCQ; LPKSQRNPCKCQN; PKSQRNPCKCQNY; TQKWGIQMKTLGA; QKWGIQMKTLGAL; KWGIQMKTLGALV; VLKMTLAVIAQRE; LKMTLAVIAQREK; KMTLAVIAQREKC; MTLAVIAQREKCF; TLAVIAQREKCFP; LAVIAQREKCFPV; AVIAQREKCFPVT; VIAQREKCFPVTA; IAQREKCFPVTAQ; AQREKCFPVTAQQ; QREKCFPVTAQQE; REKCFPVTAQQEF; EKCFPVTAQQEFP; KCFPVTAQQEFPS; CFPVTAQQEFPSP; FPVTAQQEFPSPI; LACLTFMQGHKKC; ACLTFMQGHKKCM; CLTFMQGHKKCMS; LTFMQGHKKCMSM; TFMQGHKKCMSMV; FMQGHKKCMSMVE; MQGHKKCMSMVEE; QGHKKCMSMVEEN; GHKKCMSMVEENL; HKKCMSMVEENLF; KKCMSMVEENLFK; KCMSMVEENLFKA; CMSMVEENLFKAV; MSMVEENLFKAVI; SMVEENLFKAVIS; MVEENLFKAVIST; VEENLFKAVISTS; EENLFKAVISTSL; ENLFKAVISTSLL; ILTIRPIWTKTML; LTIRPIWTKTMLI; TIRPIWTKTMLIQ; IRPIWTKTMLIQL; RPIWTKTMLIQLS; PIWTKTMLIQLSA; IWTKTMLIQLSAG; WTKTMLIQLSAGY; TKTMLIQLSAGYL; KTMLIQLSAGYLI; TMLIQLSAGYLIP; MLIQLSAGYLIPV; LIQLSAGYLIPVE; IQLSAGYLIPVEM; QLSAGYLIPVEMK; LSAGYLIPVEMKM; SAGYLIPVEMKML; AGYLIPVEMKMLG; GYLIPVEMKMLGI; YLIPVEMKMLGIL; LIPVEMKMLGILG; IPVEMKMLGILGL; PVEMKMLGILGLS; VEMKMLGILGLSQ; EMKMLGILGLSQE; MKMLGILGLSQEG; KMLGILGLSQEGK; MLGILGLSQEGKM; LGILGLSQEGKMF; GILGLSQEGKMFP; ILGLSQEGKMFPQ; LGLSQEGKMFPQY; GLSQEGKMFPQYF; LSQEGKMFPQYFM; MNRVWGLFVKLIA; NRVWGLFVKLIAC; RVWGLFVKLIACM; VWGLFVKLIACMF; WGLFVKLIACMFQ; GLFVKLIACMFQL; LFVKLIACMFQLL; FVKLIACMFQLLI; VKLIACMFQLLIF; KLIACMFQLLIFV; LIACMFQLLIFVA; IACMFQLLIFVAC; ACMFQLLIFVACL; CMFQLLIFVACLL; MFQLLIFVACLLT; FQLLIFVACLLTA; QLLIFVACLLTAL; LLIFVACLLTALE; LIFVACLLTALEH; IFVACLLTALEHN; FVACLLTALEHNS; VACLLTALEHNSG; ACLLTALEHNSGE; CLLTALEHNSGEA; LLTALEHNSGEAL; LTALEHNSGEALQ; TALEHNSGEALQD; ALEHNSGEALQDI; LEHNSGEALQDIL; EHNSGEALQDILR; HNSGEALQDILRS; NSGEALQDILRSA; TGEPREWMGSLCM; GEPREWMGSLCMV; EPREWMGSLCMVW; PREWMGSLCMVWN; REWMGSLCMVWNP; EWMGSLCMVWNPR; KRLGCLMAQKDFQ; RLGCLMAQKDFQG; LGCLMAQKDFQGT; GCLMAQKDFQGTQ; CLMAQKDFQGTQI; DILTNRDNCKPKC; ILTNRDNCKPKCF; LTNRDNCKPKCFK; TNRDNCKPKCFKQ; NRDNCKPKCFKQV; RDNCKPKCFKQVL; DNCKPKCFKQVLL; NCKPKCFKQVLLL; CKPKCFKQVLLLY; KPKCFKQVLLLYI; PKCFKQVLLLYIY; KCFKQVLLLYIYI; MLLLYKPLLSLCY; LLLYKPLLSLCYF; LLYKPLLSLCYFG; LYKPLLSLCYFGG; YKPLLSLCYFGGG; KPLLSLCYFGGGV; PLLSLCYFGGGVL; LLSLCYFGGGVLG; LSLCYFGGGVLGL; SLCYFGGGVLGLL; LCYFGGGVLGLLK; CYFGGGVLGLLKH; LWGSDLWESSAGA; WGSDLWESSAGAE; GSDLWESSAGAEV; SDLWESSAGAEVS; DLWESSAGAEVSE; LWESSAGAEVSET; WESSAGAEVSETW; ESSAGAEVSETWE; SSAGAEVSETWEE; SAGAEVSETWEEH; AGAEVSETWEEHC; GAEVSETWEEHCD; AEVSETWEEHCDW; EVSETWEEHCDWD; VSETWEEHCDWDS; SETWEEHCDWDSV; ETWEEHCDWDSVL; TWEEHCDWDSVLD; WEEHCDWDSVLDP; EEHCDWDSVLDPC; EHCDWDSVLDPCP; HCDWDSVLDPCPE; CDWDSVLDPCPES; DWDSVLDPCPESS; WDSVLDPCPESSV; DSVLDPCPESSVS; SVLDPCPESSVSE; VLDPCPESSVSES; LDPCPESSVSESS; DPCPESSVSESSS; PCPESSVSESSSL; CPESSVSESSSLV; PESSVSESSSLVI; ESSVSESSSLVIS; SSVSESSSLVISR; SVSESSSLVISRI; VSESSSLVISRIH; SESSSLVISRIHF; ESSSLVISRIHFP; SSSLVISRIHFPM; SSLVISRIHFPMH; SLVISRIHFPMHI; LVISRIHFPMHIL; VISRIHFPMHILY; ISRIHFPMHILYF; SRIHFPMHILYFI; RIHFPMHILYFIL; IHFPMHILYFILE; HFPMHILYFILEK; FPMHILYFILEKV; PMHILYFILEKVY; MHILYFILEKVYI; HILYFILEKVYIL; ILYFILEKVYILI; LYFILEKVYILIS; YFILEKVYILISE; FILEKVYILISES; ILEKVYILISESS; LEKVYILISESSL; EKVYILISESSLS; KVYILISESSLSF; VYILISESSLSFH; YILISESSLSFHS; ILISESSLSFHST; LISESSLSFHSTI; ISESSLSFHSTIL; SESSLSFHSTILD; ESSLSFHSTILDC; SSLSFHSTILDCI; SLSFHSTILDCIS; LSFHSTILDCISV; SFHSTILDCISVA; FHSTILDCISVAK; HSTILDCISVAKS; STILDCISVAKSA; TILDCISVAKSAT; ILDCISVAKSATG; LDCISVAKSATGL; DCISVAKSATGLN; CISVAKSATGLNQ; ISVAKSATGLNQI; SVAKSATGLNQIS; VAKSATGLNQISS; AKSATGLNQISSS; KSATGLNQISSSN; SATGLNQISSSNK; ATGLNQISSSNKV; TGLNQISSSNKVI; GLNQISSSNKVIP; LNQISSSNKVIPL; NQISSSNKVIPLC; QISSSNKVIPLCK; ISSSNKVIPLCKI; SSSNKVIPLCKIL; SSNKVIPLCKILF; SNKVIPLCKILFS; NKVIPLCKILFSS; KVIPLCKILFSSK; VIPLCKILFSSKN; IPLCKILFSSKNS; PLCKILFSSKNSE; LCKILFSSKNSEF; CKILFSSKNSEFC; KILFSSKNSEFCK; ILFSSKNSEFCKD; LFSSKNSEFCKDF; FSSKNSEFCKDFL; SSKNSEFCKDFLK; SKNSEFCKDFLKY; KNSEFCKDFLKYI; NSEFCKDFLKYIL; SEFCKDFLKYILG; EFCKDFLKYILGL; FCKDFLKYILGLK; CKDFLKYILGLKS; KDFLKYILGLKSI; DFLKYILGLKSIC; FLKYILGLKSICL; LKYILGLKSICLT; KYILGLKSICLTN; YILGLKSICLTNL; ILGLKSICLTNLA; LGLKSICLTNLAC; GLKSICLTNLACR; LKSICLTNLACRV; KSICLTNLACRVL; SICLTNLACRVLG; ICLTNLACRVLGT; CLTNLACRVLGTG; LTNLACRVLGTGY; TNLACRVLGTGYS; NLACRVLGTGYSF; LACRVLGTGYSFI; ACRVLGTGYSFIV; CRVLGTGYSFIVT; RVLGTGYSFIVTK; VLGTGYSFIVTKP; LGTGYSFIVTKPG; GTGYSFIVTKPGG; TGYSFIVTKPGGN; GYSFIVTKPGGNI; YSFIVTKPGGNIW; SFIVTKPGGNIWV; FIVTKPGGNIWVL; IVTKPGGNIWVLL; VTKPGGNIWVLLF; TKPGGNIWVLLFK; KPGGNIWVLLFKC; PGGNIWVLLFKCF; GGNIWVLLFKCFF; GNIWVLLFKCFFS; NIWVLLFKCFFSK; IWVLLFKCFFSKF; WVLLFKCFFSKFT; VLLFKCFFSKFTL; LLFKCFFSKFTLT; LFKCFFSKFTLTL; FKCFFSKFTLTLP; KCFFSKFTLTLPS; CFFSKFTLTLPSK; SLKLSKLFIPCPE; LKLSKLFIPCPEG; KLSKLFIPCPEGK; LSKLFIPCPEGKS; SKLFIPCPEGKSF; KLFIPCPEGKSFD; LFIPCPEGKSFDS; FIPCPEGKSFDSA; IPCPEGKSFDSAP; PCPEGKSFDSAPV; CPEGKSFDSAPVP; PEGKSFDSAPVPF; EGKSFDSAPVPFT; GKSFDSAPVPFTS; KSFDSAPVPFTSS; SFDSAPVPFTSSK; FDSAPVPFTSSKT; DSAPVPFTSSKTT; SAPVPFTSSKTTM; APVPFTSSKTTMY; SIATPSSKVSLSM; IATPSSKVSLSMG; ATPSSKVSLSMGR; TPSSKVSLSMGRF; PSSKVSLSMGRFT; SSKVSLSMGRFTF; SKVSLSMGRFTFK; KVSLSMGRFTFKA; VSLSMGRFTFKAL; SLSMGRFTFKALP; LSMGRFTFKALPP; SMGRFTFKALPPH; MGRFTFKALPPHK; GRFTFKALPPHKS; RFTFKALPPHKSN; FTFKALPPHKSNN; TFKALPPHKSNNP; FKALPPHKSNNPA; KALPPHKSNNPAA; ALPPHKSNNPAAS; LPPHKSNNPAASV; PPHKSNNPAASVV; PHKSNNPAASVVF; HKSNNPAASVVFP; KSNNPAASVVFPL; SNNPAASVVFPLS; NNPAASVVFPLSM; NPAASVVFPLSMG; PAASVVFPLSMGP; AASVVFPLSMGPL; ASVVFPLSMGPLN; SVVFPLSMGPLNN; VVFPLSMGPLNNQ; VFPLSMGPLNNQY; FPLSMGPLNNQYL; PLSMGPLNNQYLL; LSMGPLNNQYLLL; SMGPLNNQYLLLG; MGPLNNQYLLLGT; GPLNNQYLLLGTL; PLNNQYLLLGTLK; LNNQYLLLGTLKT; NNQYLLLGTLKTI; NQYLLLGTLKTIQ; QYLLLGTLKTIQC; YLLLGTLKTIQCK; LLLGTLKTIQCKK; LLGTLKTIQCKKS; LGTLKTIQCKKSN; GTLKTIQCKKSNI; TLKTIQCKKSNIT; LKTIQCKKSNITE; KTIQCKKSNITES; TIQCKKSNITESI; IQCKKSNITESIL; QCKKSNITESILG; CKKSNITESILGS; KKSNITESILGSK; KSNITESILGSKQ; SNITESILGSKQC; NITESILGSKQCS; ITESILGSKQCSQ; TESILGSKQCSQA; ESILGSKQCSQAT; SILGSKQCSQATP; ILGSKQCSQATPA; LGSKQCSQATPAI; GSKQCSQATPAIY; SKQCSQATPAIYC; KQCSQATPAIYCS; QCSQATPAIYCSS; CSQATPAIYCSST; SQATPAIYCSSTA; QATPAIYCSSTAF; ATPAIYCSSTAFP; RVSTLFLAKTVST; VSTLFLAKTVSTA; STLFLAKTVSTAC; FLLSAKIIAFAKC; LLSAKIIAFAKCF; LSAKIIAFAKCFS; NSKYIPNNKNTSS; SKYIPNNKNTSSH; KYIPNNKNTSSHF; YIPNNKNTSSHFV; IPNNKNTSSHFVS; PNNKNTSSHFVST; NNKNTSSHFVSTA; NKNTSSHFVSTAY; KNTSSHFVSTAYS; NTSSHFVSTAYSV; TSSHFVSTAYSVI; SSHFVSTAYSVIN; SHFVSTAYSVINF; HFVSTAYSVINFQ; FVSTAYSVINFQD; VSTAYSVINFQDT; STAYSVINFQDTC; TAYSVINFQDTCF; AYSVINFQDTCFV; YSVINFQDTCFVS; SVINFQDTCFVSS; VINFQDTCFVSSG; INFQDTCFVSSGS; NFQDTCFVSSGSS; FQDTCFVSSGSSG; QDTCFVSSGSSGL; DTCFVSSGSSGLK; TCFVSSGSSGLKS; CFVSSGSSGLKSC; FVSSGSSGLKSCS; VSSGSSGLKSCSF; SSGSSGLKSCSFK; SGSSGLKSCSFKP; GSSGLKSCSFKPP; MLSSIVWYGSLVK; LSSIVWYGSLVKA; SSIVWYGSLVKAL; SIVWYGSLVKALY; IVWYGSLVKALYS; VWYGSLVKALYSK; WYGSLVKALYSKY; YGSLVKALYSKYS; GSLVKALYSKYSL; SLVKALYSKYSLL; LVKALYSKYSLLT; VKALYSKYSLLTP; KALYSKYSLLTPL; ALYSKYSLLTPLQ; LYSKYSLLTPLQI; YSKYSLLTPLQIK; SKYSLLTPLQIKK; KYSLLTPLQIKKL; YSLLTPLQIKKLK; SLLTPLQIKKLKV; LLTPLQIKKLKVH; LTPLQIKKLKVHS; TPLQIKKLKVHSF; QKLLIAETLCLCG; KLLIAETLCLCGV; LLIAETLCLCGVK; LIAETLCLCGVKK; IAETLCLCGVKKN; AETLCLCGVKKNI; ETLCLCGVKKNII; TLCLCGVKKNIIL; LCLCGVKKNIILC; CLCGVKKNIILCP; LCGVKKNIILCPA; CGVKKNIILCPAH; GVKKNIILCPAHM; VKKNIILCPAHMC; KKNIILCPAHMCL; KNIILCPAHMCLL; NIILCPAHMCLLI; IILCPAHMCLLIK; ILCPAHMCLLIKV; LCPAHMCLLIKVT; CPAHMCLLIKVTE; PAHMCLLIKVTEY; AHMCLLIKVTEYF; HMCLLIKVTEYFS; MCLLIKVTEYFSI; CLLIKVTEYFSIS; LLIKVTEYFSISF; LIKVTEYFSISFL; IKVTEYFSISFLY; KVTEYFSISFLYR; VTEYFSISFLYRI; AFSLVVYTAKQAR; FSLVVYTAKQARV; SLVVYTAKQARVL; LVVYTAKQARVLL; VVYTAKQARVLLL; VYTAKQARVLLLN; YTAKQARVLLLNT; TAKQARVLLLNTA; LRNWCRSEGKSLG; RNWCRSEGKSLGS; NWCRSEGKSLGSS; WCRSEGKSLGSST; CRSEGKSLGSSTF; RSEGKSLGSSTFL; SEGKSLGSSTFLF; EGKSLGSSTFLFF; GKSLGSSTFLFFL; KSLGSSTFLFFLG; SLGSSTFLFFLGG; LGSSTFLFFLGGV; GSSTFLFFLGGVE; SSTFLFFLGGVEC; ESAVASSSLANIS; SAVASSSLANISS; AVASSSLANISSW; VASSSLANISSWQ; ASSSLANISSWQN; SSSLANISSWQNK; SSLANISSWQNKS; SLANISSWQNKSS; LANISSWQNKSSS; ANISSWQNKSSSH; NISSWQNKSSSHF; ISSWQNKSSSHFS; SSWQNKSSSHFSL; SWQNKSSSHFSLK; WQNKSSSHFSLKE; QNKSSSHFSLKEL; NKSSSHFSLKELH; KSSSHFSLKELHQ; SSSHFSLKELHQD; SSHFSLKELHQDS; SHFSLKELHQDSH; HFSLKELHQDSHS; FSLKELHQDSHSS; SLKELHQDSHSSV; LKELHQDSHSSVP; VGTYKKNNYLGPF; GTYKKNNYLGPFN; TYKKNNYLGPFNI; YKKNNYLGPFNIL; KKNNYLGPFNILL; KNNYLGPFNILLF; NNYLGPFNILLFI; REFLQLFGPTIAE; EFLQLFGPTIAEF; FLQLFGPTIAEFL; LQLFGPTIAEFLQ; QLFGPTIAEFLQL; LFGPTIAEFLQLG; FGPTIAEFLQLGL; GPTIAEFLQLGLS; PTIAEFLQLGLSQ; TIAEFLQLGLSQT; IAEFLQLGLSQTT; AEFLQLGLSQTTV; SSQCSSNLSKPRA; SQCSSNLSKPRAL; QCSSNLSKPRALF; CSSNLSKPRALFL; SSNLSKPRALFLK; SNLSKPRALFLKI; NLSKPRALFLKIF; LSKPRALFLKIFY; SKPRALFLKIFYL; KPRALFLKIFYLN; PRALFLKIFYLNA; RALFLKIFYLNAL; ALFLKIFYLNALI; ADIACKGSAQKAF; DIACKGSAQKAFW; IACKGSAQKAFWN; ACKGSAQKAFWNK; AIPCSTGYLGKEE; IPCSTGYLGKEEN; PCSTGYLGKEENQ; CSTGYLGKEENQH; STGYLGKEENQHK; TGYLGKEENQHKP; GYLGKEENQHKPL; YLGKEENQHKPLS; LGKEENQHKPLSY; GKEENQHKPLSYS; KEENQHKPLSYSR; EENQHKPLSYSRF; ENQHKPLSYSRFQ; NQHKPLSYSRFQN; QHKPLSYSRFQNQ; HKPLSYSRFQNQA; KPLSYSRFQNQAD; PLSYSRFQNQADE; LSYSRFQNQADEL; SYSRFQNQADELP; YSRFQNQADELPL; SRFQNQADELPLH; RFQNQADELPLHP; FQNQADELPLHPA; QNQADELPLHPAP; NQADELPLHPAPF; QADELPLHPAPFF; ADELPLHPAPFFY; DELPLHPAPFFYT; ELPLHPAPFFYTK; LPLHPAPFFYTKY; PLHPAPFFYTKYS; LHPAPFFYTKYSF; HPAPFFYTKYSFS; PAPFFYTKYSFSS; APFFYTKYSFSSF; PFFYTKYSFSSFY; FFYTKYSFSSFYP; FYTKYSFSSFYPR; YTKYSFSSFYPRR; TKYSFSSFYPRRP; KYSFSSFYPRRPL; YSFSSFYPRRPLC; SFSSFYPRRPLCQ; FSSFYPRRPLCQG; SSFYPRRPLCQGE; SFYPRRPLCQGEI; FYPRRPLCQGEIP; YPRRPLCQGEIPY; PRRPLCQGEIPYT; RRPLCQGEIPYTS; RPLCQGEIPYTSL; PLCQGEIPYTSLN; LCQGEIPYTSLNK; CQGEIPYTSLNKL; QGEIPYTSLNKLF; GEIPYTSLNKLFS; EIPYTSLNKLFSL; IPYTSLNKLFSLR; PYTSLNKLFSLRE; YTSLNKLFSLRED; TSLNKLFSLREDF; SLNKLFSLREDFP; LNKLFSLREDFPR; NKLFSLREDFPRQ; KLFSLREDFPRQL; LFSLREDFPRQLF; FSLREDFPRQLFQ; SLREDFPRQLFQG; LREDFPRQLFQGL; REDFPRQLFQGLK; EDFPRQLFQGLKG; DFPRQLFQGLKGP 14 mers: GFPQIVLLGLRKSL; FPQIVLLGLRKSLH; PQIVLLGLRKSLHT; QIVLLGLRKSLHTL; IVLLGLRKSLHTLT; VLLGLRKSLHTLTT; EKGWRQRRPRPLIY; KGWRQRRPRPLIYY; GWRQRRPRPLIYYK; WRQRRPRPLIYYKK; RQRRPRPLIYYKKK; QRRPRPLIYYKKKG; RRPRPLIYYKKKGH; RPRPLIYYKKKGHR; PRPLIYYKKKGHRE; RPLIYYKKKGHREE; PLIYYKKKGHREEL; LIYYKKKGHREELL; IYYKKKGHREELLT; YYKKKGHREELLTH; YKKKGHREELLTHG; KKKGHREELLTHGM; KKGHREELLTHGMQ; KGHREELLTHGMQP; GHREELLTHGMQPN; HREELLTHGMQPNH; REELLTHGMQPNHD; EELLTHGMQPNHDL; ELLTHGMQPNHDLR; LLTHGMQPNHDLRK; LTHGMQPNHDLRKE; THGMQPNHDLRKES; HGMQPNHDLRKESA; LTGECSQTMTSGRK; TGECSQTMTSGRKV; GECSQTMTSGRKVH; ECSQTMTSGRKVHD; CSQTMTSGRKVHDS; SQTMTSGRKVHDSQ; QTMTSGRKVHDSQG; TMTSGRKVHDSQGG; MTSGRKVHDSQGGA; TSGRKVHDSQGGAA; SGRKVHDSQGGAAY; GRKVHDSQGGAAYP; RKVHDSQGGAAYPW; KVHDSQGGAAYPWN; VHDSQGGAAYPWNA; HDSQGGAAYPWNAA; DSQGGAAYPWNAAK; SQGGAAYPWNAAKP; PQEGKCMTDMFCEP; QEGKCMTDMFCEPR; EGKCMTDMFCEPRN; GKCMTDMFCEPRNL; KCMTDMFCEPRNLG; CMTDMFCEPRNLGL; MTDMFCEPRNLGLV; TDMFCEPRNLGLVP; DMFCEPRNLGLVPS; TGQRPWFCASCHDK; GQRPWFCASCHDKL; QRPWFCASCHDKLQ; KLVKPGLEQKKELR; LVKPGLEQKKELRG; VKPGLEQKKELRGF; KPGLEQKKELRGFL; PGLEQKKELRGFLF; GLEQKKELRGFLFL; LEQKKELRGFLFLF; VIPFFLYFQVHGCC; IPFFLYFQVHGCCS; PFFLYFQVHGCCSS; FFLYFQVHGCCSST; FLYFQVHGCCSSTF; LYFQVHGCCSSTFG; YFQVHGCCSSTFGG; FQVHGCCSSTFGGP; QVHGCCSSTFGGPS; VHGCCSSTFGGPSC; HGCCSSTFGGPSCQ; GCCSSTFGGPSCQC; CCSSTFGGPSCQCI; NCCWGGCCCYRSSN; CCWGGCCCYRSSNC; CWGGCCCYRSSNCI; WGGCCCYRSSNCIP; GGCCCYRSSNCIPC; GCCCYRSSNCIPCY; CCCYRSSNCIPCYC; CCYRSSNCIPCYCR; CYRSSNCIPCYCRG; YRSSNCIPCYCRGH; RSSNCIPCYCRGHN; SSNCIPCYCRGHNK; SNCIPCYCRGHNKY; NCIPCYCRGHNKYL; CIPCYCRGHNKYLR; IPCYCRGHNKYLRG; PCYCRGHNKYLRGY; CYCRGHNKYLRGYS; YCRGHNKYLRGYSC; CRGHNKYLRGYSCY; RGHNKYLRGYSCYR; GHNKYLRGYSCYRP; HNKYLRGYSCYRPN; NKYLRGYSCYRPNS; KYLRGYSCYRPNSS; YLRGYSCYRPNSSN; LRGYSCYRPNSSNI; RGYSCYRPNSSNIC; GYSCYRPNSSNICC; YSCYRPNSSNICCN; SCYRPNSSNICCNC; CYRPNSSNICCNCW; YRPNSSNICCNCWC; RPNSSNICCNCWCS; PNSSNICCNCWCSW; NSSNICCNCWCSWG; SSNICCNCWCSWGY; SNICCNCWCSWGYC; NICCNCWCSWGYCW; ICCNCWCSWGYCWV; CCNCWCSWGYCWVC; CNCWCSWGYCWVCC; NCWCSWGYCWVCCF; CWCSWGYCWVCCFN; WCSWGYCWVCCFNS; CSWGYCWVCCFNSN; SWGYCWVCCFNSNC; LGSQSFHCRPLSAI; GSQSFHCRPLSAIR; SQSFHCRPLSAIRH; QSFHCRPLSAIRHG; SFHCRPLSAIRHGF; FHCRPLSAIRHGFG; HCRPLSAIRHGFGI; CRPLSAIRHGFGIV; ALGSFFVCYYFPGF; LGSFFVCYYFPGFV; GSFFVCYYFPGFVA; SFFVCYYFPGFVAC; FFVCYYFPGFVACY; YTFYNLTGIAEKNR; TFYNLTGIAEKNRK; FYNLTGIAEKNRKI; YNLTGIAEKNRKIF; IFGGNYLDNCKCPY; FGGNYLDNCKCPYK; GGNYLDNCKCPYKL; GNYLDNCKCPYKLL; QYRRSYTKNGLKKS; YRRSYTKNGLKKST; RRSYTKNGLKKSTK; RSYTKNGLKKSTKC; SYTKNGLKKSTKCT; YTKNGLKKSTKCTF; TKNGLKKSTKCTFR; KNGLKKSTKCTFRR; NGLKKSTKCTFRRV; GLKKSTKCTFRRVY; LKKSTKCTFRRVYR; KKSTKCTFRRVYRK; KSTKCTFRRVYRKN; STKCTFRRVYRKNY; TKCTFRRVYRKNYC; KCTFRRVYRKNYCP; CTFRRVYRKNYCPR; TFRRVYRKNYCPRR; FRRVYRKNYCPRRC; SKNCSSMDVAFTSR; KNCSSMDVAFTSRP; NCSSMDVAFTSRPV; CSSMDVAFTSRPVR; SSMDVAFTSRPVRD; SMDVAFTSRPVRDC; MDVAFTSRPVRDCN; DVAFTSRPVRDCNT; VAFTSRPVRDCNTC; AFTSRPVRDCNTCS; RWPQPKEKESVQGQ; WPQPKEKESVQGQL; PQPKEKESVQGQLP; QPKEKESVQGQLPK; PKEKESVQGQLPKS; KEKESVQGQLPKSQ; EKESVQGQLPKSQR; KESVQGQLPKSQRN; ESVQGQLPKSQRNP; SVQGQLPKSQRNPC; VQGQLPKSQRNPCK; QGQLPKSQRNPCKC; GQLPKSQRNPCKCQ; QLPKSQRNPCKCQN; LPKSQRNPCKCQNY; TQKWGIQMKTLGAL; QKWGIQMKTLGALV; VLKMTLAVIAQREK; LKMTLAVIAQREKC; KMTLAVIAQREKCF; MTLAVIAQREKCFP; TLAVIAQREKCFPV; LAVIAQREKCFPVT; AVIAQREKCFPVTA; VIAQREKCFPVTAQ; IAQREKCFPVTAQQ; AQREKCFPVTAQQE; QREKCFPVTAQQEF; REKCFPVTAQQEFP; EKCFPVTAQQEFPS; KCFPVTAQQEFPSP; CFPVTAQQEFPSPI; LACLTFMQGHKKCM; ACLTFMQGHKKCMS; CLTFMQGHKKCMSM; LTFMQGHKKCMSMV; TFMQGHKKCMSMVE; FMQGHKKCMSMVEE; MQGHKKCMSMVEEN; QGHKKCMSMVEENL; GHKKCMSMVEENLF; HKKCMSMVEENLFK; KKCMSMVEENLFKA; KCMSMVEENLFKAV; CMSMVEENLFKAVI; MSMVEENLFKAVIS; SMVEENLFKAVIST; MVEENLFKAVISTS; VEENLFKAVISTSL; EENLFKAVISTSLL; ILTIRPIWTKTMLI; LTIRPIWTKTMLIQ; TIRPIWTKTMLIQL; IRPIWTKTMLIQLS; RPIWTKTMLIQLSA; PIWTKTMLIQLSAG; IWTKTMLIQLSAGY; WTKTMLIQLSAGYL; TKTMLIQLSAGYLI; KTMLIQLSAGYLIP; TMLIQLSAGYLIPV; MLIQLSAGYLIPVE; LIQLSAGYLIPVEM; IQLSAGYLIPVEMK; QLSAGYLIPVEMKM; LSAGYLIPVEMKML; SAGYLIPVEMKMLG; AGYLIPVEMKMLGI; GYLIPVEMKMLGIL; YLIPVEMKMLGILG; LIPVEMKMLGILGL; IPVEMKMLGILGLS; PVEMKMLGILGLSQ; VEMKMLGILGLSQE; EMKMLGILGLSQEG; MKMLGILGLSQEGK; KMLGILGLSQEGKM; MLGILGLSQEGKMF; LGILGLSQEGKMFP; GILGLSQEGKMFPQ; ILGLSQEGKMFPQY; LGLSQEGKMFPQYF; GLSQEGKMFPQYFM; MNRVWGLFVKLIAC; NRVWGLFVKLIACM; RVWGLFVKLIACMF; VWGLFVKLIACMFQ; WGLFVKLIACMFQL; GLFVKLIACMFQLL; LFVKLIACMFQLLI; FVKLIACMFQLLIF; VKLIACMFQLLIFV; KLIACMFQLLIFVA; LIACMFQLLIFVAC; IACMFQLLIFVACL; ACMFQLLIFVACLL; CMFQLLIFVACLLT; MFQLLIFVACLLTA; FQLLIFVACLLTAL; QLLIFVACLLTALE; LLIFVACLLTALEH; LIFVACLLTALEHN; IFVACLLTALEHNS; FVACLLTALEHNSG; VACLLTALEHNSGE; ACLLTALEHNSGEA; CLLTALEHNSGEAL; LLTALEHNSGEALQ; LTALEHNSGEALQD; TALEHNSGEALQDI; ALEHNSGEALQDIL; LEHNSGEALQDILR; EHNSGEALQDILRS; HNSGEALQDILRSA; TGEPREWMGSLCMV; GEPREWMGSLCMVW; EPREWMGSLCMVWN; PREWMGSLCMVWNP; REWMGSLCMVWNPR; KRLGCLMAQKDFQG; RLGCLMAQKDFQGT; LGCLMAQKDFQGTQ; GCLMAQKDFQGTQI; DILTNRDNCKPKCF; ILTNRDNCKPKCFK; LTNRDNCKPKCFKQ; TNRDNCKPKCFKQV; NRDNCKPKCFKQVL; RDNCKPKCFKQVLL; DNCKPKCFKQVLLL; NCKPKCFKQVLLLY; CKPKCFKQVLLLYI; KPKCFKQVLLLYIY; PKCFKQVLLLYIYI; MLLLYKPLLSLCYF; LLLYKPLLSLCYFG; LLYKPLLSLCYFGG; LYKPLLSLCYFGGG; YKPLLSLCYFGGGV; KPLLSLCYFGGGVL; PLLSLCYFGGGVLG; LLSLCYFGGGVLGL; LSLCYFGGGVLGLL; SLCYFGGGVLGLLK; LCYFGGGVLGLLKH; LWGSDLWESSAGAE; WGSDLWESSAGAEV; GSDLWESSAGAEVS; SDLWESSAGAEVSE; DLWESSAGAEVSET; LWESSAGAEVSETW; WESSAGAEVSETWE; ESSAGAEVSETWEE; SSAGAEVSETWEEH; SAGAEVSETWEEHC; AGAEVSETWEEHCD; GAEVSETWEEHCDW; AEVSETWEEHCDWD; EVSETWEEHCDWDS; VSETWEEHCDWDSV; SETWEEHCDWDSVL; ETWEEHCDWDSVLD; TWEEHCDWDSVLDP; WEEHCDWDSVLDPC; EEHCDWDSVLDPCP; EHCDWDSVLDPCPE; HCDWDSVLDPCPES; CDWDSVLDPCPESS; DWDSVLDPCPESSV; WDSVLDPCPESSVS; DSVLDPCPESSVSE; SVLDPCPESSVSES; VLDPCPESSVSESS; LDPCPESSVSESSS; DPCPESSVSESSSL; PCPESSVSESSSLV; CPESSVSESSSLVI; PESSVSESSSLVIS; ESSVSESSSLVISR; SSVSESSSLVISRI; SVSESSSLVISRIH; VSESSSLVISRIHF; SESSSLVISRIHFP; ESSSLVISRIHFPM; SSSLVISRIHFPMH; SSLVISRIHFPMHI; SLVISRIHFPMHIL; LVISRIHFPMHILY; VISRIHFPMHILYF; ISRIHFPMHILYFI; SRIHFPMHILYFIL; RIHFPMHILYFILE; IHFPMHILYFILEK; HFPMHILYFILEKV; FPMHILYFILEKVY; PMHILYFILEKVYI; MHILYFILEKVYIL; HILYFILEKVYILI; ILYFILEKVYILIS; LYFILEKVYILISE; YFILEKVYILISES; FILEKVYILISESS; ILEKVYILISESSL; LEKVYILISESSLS; EKVYILISESSLSF; KVYILISESSLSFH; VYILISESSLSFHS; YILISESSLSFHST; ILISESSLSFHSTI; LISESSLSFHSTIL; ISESSLSFHSTILD; SESSLSFHSTILDC; ESSLSFHSTILDCI; SSLSFHSTILDCIS; SLSFHSTILDCISV; LSFHSTILDCISVA; SFHSTILDCISVAK; FHSTILDCISVAKS; HSTILDCISVAKSA; STILDCISVAKSAT; TILDCISVAKSATG; ILDCISVAKSATGL; LDCISVAKSATGLN; DCISVAKSATGLNQ; CISVAKSATGLNQI; ISVAKSATGLNQIS; SVAKSATGLNQISS; VAKSATGLNQISSS; AKSATGLNQISSSN; KSATGLNQISSSNK; SATGLNQISSSNKV; ATGLNQISSSNKVI; TGLNQISSSNKVIP; GLNQISSSNKVIPL; LNQISSSNKVIPLC; NQISSSNKVIPLCK; QISSSNKVIPLCKI; ISSSNKVIPLCKIL; SSSNKVIPLCKILF; SSNKVIPLCKILFS; SNKVIPLCKILFSS; NKVIPLCKILFSSK; KVIPLCKILFSSKN; VIPLCKILFSSKNS; IPLCKILFSSKNSE; PLCKILFSSKNSEF; LCKILFSSKNSEFC; CKILFSSKNSEFCK; KILFSSKNSEFCKD; ILFSSKNSEFCKDF; LFSSKNSEFCKDFL; FSSKNSEFCKDFLK; SSKNSEFCKDFLKY; SKNSEFCKDFLKYI; KNSEFCKDFLKYIL; NSEFCKDFLKYILG; SEFCKDFLKYILGL; EFCKDFLKYILGLK; FCKDFLKYILGLKS; CKDFLKYILGLKSI; KDFLKYILGLKSIC; DFLKYILGLKSICL; FLKYILGLKSICLT; LKYILGLKSICLTN; KYILGLKSICLTNL; YILGLKSICLTNLA; ILGLKSICLTNLAC; LGLKSICLTNLACR; GLKSICLTNLACRV; LKSICLTNLACRVL; KSICLTNLACRVLG; SICLTNLACRVLGT; ICLTNLACRVLGTG; CLTNLACRVLGTGY; LTNLACRVLGTGYS; TNLACRVLGTGYSF; NLACRVLGTGYSFI; LACRVLGTGYSFIV; ACRVLGTGYSFIVT; CRVLGTGYSFIVTK; RVLGTGYSFIVTKP; VLGTGYSFIVTKPG; LGTGYSFIVTKPGG; GTGYSFIVTKPGGN; TGYSFIVTKPGGNI; GYSFIVTKPGGNIW; YSFIVTKPGGNIWV; SFIVTKPGGNIWVL; FIVTKPGGNIWVLL; IVTKPGGNIWVLLF; VTKPGGNIWVLLFK; TKPGGNIWVLLFKC; KPGGNIWVLLFKCF; PGGNIWVLLFKCFF; GGNIWVLLFKCFFS; GNIWVLLFKCFFSK; NIWVLLFKCFFSKF; IWVLLFKCFFSKFT; WVLLFKCFFSKFTL; VLLFKCFFSKFTLT; LLFKCFFSKFTLTL; LFKCFFSKFTLTLP; FKCFFSKFTLTLPS; KCFFSKFTLTLPSK; SLKLSKLFIPCPEG; LKLSKLFIPCPEGK; KLSKLFIPCPEGKS; LSKLFIPCPEGKSF; SKLFIPCPEGKSFD; KLFIPCPEGKSFDS; LFIPCPEGKSFDSA; FIPCPEGKSFDSAP; IPCPEGKSFDSAPV; PCPEGKSFDSAPVP; CPEGKSFDSAPVPF; PEGKSFDSAPVPFT; EGKSFDSAPVPFTS; GKSFDSAPVPFTSS; KSFDSAPVPFTSSK; SFDSAPVPFTSSKT; FDSAPVPFTSSKTT; DSAPVPFTSSKTTM; SAPVPFTSSKTTMY; SIATPSSKVSLSMG; IATPSSKVSLSMGR; ATPSSKVSLSMGRF; TPSSKVSLSMGRFT; PSSKVSLSMGRFTF; SSKVSLSMGRFTFK; SKVSLSMGRFTFKA; KVSLSMGRFTFKAL; VSLSMGRFTFKALP; SLSMGRFTFKALPP; LSMGRFTFKALPPH; SMGRFTFKALPPHK; MGRFTFKALPPHKS; GRFTFKALPPHKSN; RFTFKALPPHKSNN; FTFKALPPHKSNNP; TFKALPPHKSNNPA; FKALPPHKSNNPAA; KALPPHKSNNPAAS; ALPPHKSNNPAASV; LPPHKSNNPAASVV; PPHKSNNPAASVVF; PHKSNNPAASVVFP; HKSNNPAASVVFPL; KSNNPAASVVFPLS; SNNPAASVVFPLSM; NNPAASVVFPLSMG; NPAASVVFPLSMGP; PAASVVFPLSMGPL; AASVVFPLSMGPLN; ASVVFPLSMGPLNN; SVVFPLSMGPLNNQ; VVFPLSMGPLNNQY; VFPLSMGPLNNQYL; FPLSMGPLNNQYLL; PLSMGPLNNQYLLL; LSMGPLNNQYLLLG; SMGPLNNQYLLLGT; MGPLNNQYLLLGTL; GPLNNQYLLLGTLK; PLNNQYLLLGTLKT; LNNQYLLLGTLKTI; NNQYLLLGTLKTIQ; NQYLLLGTLKTIQC; QYLLLGTLKTIQCK; YLLLGTLKTIQCKK; LLLGTLKTIQCKKS; LLGTLKTIQCKKSN; LGTLKTIQCKKSNI; GTLKTIQCKKSNIT; TLKTIQCKKSNITE; LKTIQCKKSNITES; KTIQCKKSNITESI; TIQCKKSNITESIL; IQCKKSNITESILG; QCKKSNITESILGS; CKKSNITESILGSK; KKSNITESILGSKQ; KSNITESILGSKQC; SNITESILGSKQCS; NITESILGSKQCSQ; ITESILGSKQCSQA; TESILGSKQCSQAT; ESILGSKQCSQATP; SILGSKQCSQATPA; ILGSKQCSQATPAI; LGSKQCSQATPAIY; GSKQCSQATPAIYC; SKQCSQATPAIYCS; KQCSQATPAIYCSS; QCSQATPAIYCSST; CSQATPAIYCSSTA; SQATPAIYCSSTAF; QATPAIYCSSTAFP; RVSTLFLAKTVSTA; VSTLFLAKTVSTAC; FLLSAKIIAFAKCF; LLSAKIIAFAKCFS; NSKYIPNNKNTSSH; SKYIPNNKNTSSHF; KYIPNNKNTSSHFV; YIPNNKNTSSHFVS; IPNNKNTSSHFVST; PNNKNTSSHFVSTA; NNKNTSSHFVSTAY; NKNTSSHFVSTAYS; KNTSSHFVSTAYSV; NTSSHFVSTAYSVI; TSSHFVSTAYSVIN; SSHFVSTAYSVINF; SHFVSTAYSVINFQ; HFVSTAYSVINFQD; FVSTAYSVINFQDT; VSTAYSVINFQDTC; STAYSVINFQDTCF; TAYSVINFQDTCFV; AYSVINFQDTCFVS; YSVINFQDTCFVSS; SVINFQDTCFVSSG; VINFQDTCFVSSGS; INFQDTCFVSSGSS; NFQDTCFVSSGSSG; FQDTCFVSSGSSGL; QDTCFVSSGSSGLK; DTCFVSSGSSGLKS; TCFVSSGSSGLKSC; CFVSSGSSGLKSCS; FVSSGSSGLKSCSF; VSSGSSGLKSCSFK; SSGSSGLKSCSFKP; SGSSGLKSCSFKPP; MLSSIVWYGSLVKA; LSSIVWYGSLVKAL; SSIVWYGSLVKALY; SIVWYGSLVKALYS; IVWYGSLVKALYSK; VWYGSLVKALYSKY; WYGSLVKALYSKYS; YGSLVKALYSKYSL; GSLVKALYSKYSLL; SLVKALYSKYSLLT; LVKALYSKYSLLTP; VKALYSKYSLLTPL; KALYSKYSLLTPLQ; ALYSKYSLLTPLQI; LYSKYSLLTPLQIK; YSKYSLLTPLQIKK; SKYSLLTPLQIKKL; KYSLLTPLQIKKLK; YSLLTPLQIKKLKV; SLLTPLQIKKLKVH; LLTPLQIKKLKVHS; LTPLQIKKLKVHSF; QKLLIAETLCLCGV; KLLIAETLCLCGVK; LLIAETLCLCGVKK; LIAETLCLCGVKKN; IAETLCLCGVKKNI; AETLCLCGVKKNII; ETLCLCGVKKNIIL; TLCLCGVKKNIILC; LCLCGVKKNIILCP; CLCGVKKNIILCPA; LCGVKKNIILCPAH; CGVKKNIILCPAHM; GVKKNIILCPAHMC; VKKNIILCPAHMCL; KKNIILCPAHMCLL; KNIILCPAHMCLLI; NIILCPAHMCLLIK; IILCPAHMCLLIKV; ILCPAHMCLLIKVT; LCPAHMCLLIKVTE; CPAHMCLLIKVTEY; PAHMCLLIKVTEYF; AHMCLLIKVTEYFS; HMCLLIKVTEYFSI; MCLLIKVTEYFSIS; CLLIKVTEYFSISF; LLIKVTEYFSISFL; LIKVTEYFSISFLY; IKVTEYFSISFLYR; KVTEYFSISFLYRI; AFSLVVYTAKQARV; FSLVVYTAKQARVL; SLVVYTAKQARVLL; LVVYTAKQARVLLL; VVYTAKQARVLLLN; VYTAKQARVLLLNT; YTAKQARVLLLNTA; LRNWCRSEGKSLGS; RNWCRSEGKSLGSS; NWCRSEGKSLGSST; WCRSEGKSLGSSTF; CRSEGKSLGSSTFL; RSEGKSLGSSTFLF; SEGKSLGSSTFLFF; EGKSLGSSTFLFFL; GKSLGSSTFLFFLG; KSLGSSTFLFFLGG; SLGSSTFLFFLGGV; LGSSTFLFFLGGVE; GSSTFLFFLGGVEC; ESAVASSSLANISS; SAVASSSLANISSW; AVASSSLANISSWQ; VASSSLANISSWQN; ASSSLANISSWQNK; SSSLANISSWQNKS; SSLANISSWQNKSS; SLANISSWQNKSSS; LANISSWQNKSSSH; ANISSWQNKSSSHF; NISSWQNKSSSHFS; ISSWQNKSSSHFSL; SSWQNKSSSHFSLK; SWQNKSSSHFSLKE; WQNKSSSHFSLKEL; QNKSSSHFSLKELH; NKSSSHFSLKELHQ; KSSSHFSLKELHQD; SSSHFSLKELHQDS; SSHFSLKELHQDSH; SHFSLKELHQDSHS; HFSLKELHQDSHSS; FSLKELHQDSHSSV; SLKELHQDSHSSVP; VGTYKKNNYLGPFN; GTYKKNNYLGPFNI; TYKKNNYLGPFNIL; YKKNNYLGPFNILL; KKNNYLGPFNILLF; KNNYLGPFNILLFI; REFLQLFGPTIAEF; EFLQLFGPTIAEFL; FLQLFGPTIAEFLQ; LQLFGPTIAEFLQL; QLFGPTIAEFLQLG; LFGPTIAEFLQLGL; FGPTIAEFLQLGLS; GPTIAEFLQLGLSQ; PTIAEFLQLGLSQT; TIAEFLQLGLSQTT; IAEFLQLGLSQTTV; SSQCSSNLSKPRAL; SQCSSNLSKPRALF; QCSSNLSKPRALFL; CSSNLSKPRALFLK; SSNLSKPRALFLKI; SNLSKPRALFLKIF; NLSKPRALFLKIFY; LSKPRALFLKIFYL; SKPRALFLKIFYLN; KPRALFLKIFYLNA; PRALFLKIFYLNAL; RALFLKIFYLNALI; ADIACKGSAQKAFW; DIACKGSAQKAFWN; IACKGSAQKAFWNK; AIPCSTGYLGKEEN; IPCSTGYLGKEENQ; PCSTGYLGKEENQH; CSTGYLGKEENQHK; STGYLGKEENQHKP; TGYLGKEENQHKPL; GYLGKEENQHKPLS; YLGKEENQHKPLSY; LGKEENQHKPLSYS; GKEENQHKPLSYSR; KEENQHKPLSYSRF; EENQHKPLSYSRFQ; ENQHKPLSYSRFQN; NQHKPLSYSRFQNQ; QHKPLSYSRFQNQA; HKPLSYSRFQNQAD; KPLSYSRFQNQADE; PLSYSRFQNQADEL; LSYSRFQNQADELP; SYSRFQNQADELPL; YSRFQNQADELPLH; SRFQNQADELPLHP; RFQNQADELPLHPA; FQNQADELPLHPAP; QNQADELPLHPAPF; NQADELPLHPAPFF; QADELPLHPAPFFY; ADELPLHPAPFFYT; DELPLHPAPFFYTK; ELPLHPAPFFYTKY; LPLHPAPFFYTKYS; PLHPAPFFYTKYSF; LHPAPFFYTKYSFS; HPAPFFYTKYSFSS; PAPFFYTKYSFSSF; APFFYTKYSFSSFY; PFFYTKYSFSSFYP; FFYTKYSFSSFYPR; FYTKYSFSSFYPRR; YTKYSFSSFYPRRP; TKYSFSSFYPRRPL; KYSFSSFYPRRPLC; YSFSSFYPRRPLCQ; SFSSFYPRRPLCQG; FSSFYPRRPLCQGE; SSFYPRRPLCQGEI; SFYPRRPLCQGEIP; FYPRRPLCQGEIPY; YPRRPLCQGEIPYT; PRRPLCQGEIPYTS; RRPLCQGEIPYTSL; RPLCQGEIPYTSLN; PLCQGEIPYTSLNK; LCQGEIPYTSLNKL; CQGEIPYTSLNKLF; QGEIPYTSLNKLFS; GEIPYTSLNKLFSL; EIPYTSLNKLFSLR; IPYTSLNKLFSLRE; PYTSLNKLFSLRED; YTSLNKLFSLREDF; TSLNKLFSLREDFP; SLNKLFSLREDFPR; LNKLFSLREDFPRQ; NKLFSLREDFPRQL; KLFSLREDFPRQLF; LFSLREDFPRQLFQ; FSLREDFPRQLFQG; SLREDFPRQLFQGL; LREDFPRQLFQGLK; REDFPRQLFQGLKG; EDFPRQLFQGLKGP 15 mers: GFPQIVLLGLRKSLH; FPQIVLLGLRKSLHT; PQIVLLGLRKSLHTL; QIVLLGLRKSLHTLT; IVLLGLRKSLHTLTT; EKGWRQRRPRPLIYY; KGWRQRRPRPLIYYK; GWRQRRPRPLIYYKK; WRQRRPRPLIYYKKK; RQRRPRPLIYYKKKG; QRRPRPLIYYKKKGH; RRPRPLIYYKKKGHR; RPRPLIYYKKKGHRE; PRPLIYYKKKGHREE; RPLIYYKKKGHREEL; PLIYYKKKGHREELL; LIYYKKKGHREELLT; IYYKKKGHREELLTH; YYKKKGHREELLTHG; YKKKGHREELLTHGM; KKKGHREELLTHGMQ; KKGHREELLTHGMQP; KGHREELLTHGMQPN; GHREELLTHGMQPNH; HREELLTHGMQPNHD; REELLTHGMQPNHDL; EELLTHGMQPNHDLR; ELLTHGMQPNHDLRK; LLTHGMQPNHDLRKE; LTHGMQPNHDLRKES; THGMQPNHDLRKESA; LTGECSQTMTSGRKV; TGECSQTMTSGRKVH; GECSQTMTSGRKVHD; ECSQTMTSGRKVHDS; CSQTMTSGRKVHDSQ; SQTMTSGRKVHDSQG; QTMTSGRKVHDSQGG; TMTSGRKVHDSQGGA; MTSGRKVHDSQGGAA; TSGRKVHDSQGGAAY; SGRKVHDSQGGAAYP; GRKVHDSQGGAAYPW; RKVHDSQGGAAYPWN; KVHDSQGGAAYPWNA; VHDSQGGAAYPWNAA; HDSQGGAAYPWNAAK; DSQGGAAYPWNAAKP; PQEGKCMTDMFCEPR; QEGKCMTDMFCEPRN; EGKCMTDMFCEPRNL; GKCMTDMFCEPRNLG; KCMTDMFCEPRNLGL; CMTDMFCEPRNLGLV; MTDMFCEPRNLGLVP; TDMFCEPRNLGLVPS; TGQRPWFCASCHDKL; GQRPWFCASCHDKLQ; KLVKPGLEQKKELRG; LVKPGLEQKKELRGF; VKPGLEQKKELRGFL; KPGLEQKKELRGFLF; PGLEQKKELRGFLFL; GLEQKKELRGFLFLF; VIPFFLYFQVHGCCS; IPFFLYFQVHGCCSS; PFFLYFQVHGCCSST; FFLYFQVHGCCSSTF; FLYFQVHGCCSSTFG; LYFQVHGCCSSTFGG; YFQVHGCCSSTFGGP; FQVHGCCSSTFGGPS; QVHGCCSSTFGGPSC; VHGCCSSTFGGPSCQ; HGCCSSTFGGPSCQC; GCCSSTFGGPSCQCI; NCCWGGCCCYRSSNC; CCWGGCCCYRSSNCI; CWGGCCCYRSSNCIP; WGGCCCYRSSNCIPC; GGCCCYRSSNCIPCY; GCCCYRSSNCIPCYC; CCCYRSSNCIPCYCR; CCYRSSNCIPCYCRG; CYRSSNCIPCYCRGH; YRSSNCIPCYCRGHN; RSSNCIPCYCRGHNK; SSNCIPCYCRGHNKY; SNCIPCYCRGHNKYL; NCIPCYCRGHNKYLR; CIPCYCRGHNKYLRG; IPCYCRGHNKYLRGY; PCYCRGHNKYLRGYS; CYCRGHNKYLRGYSC; YCRGHNKYLRGYSCY; CRGHNKYLRGYSCYR; RGHNKYLRGYSCYRP; GHNKYLRGYSCYRPN; HNKYLRGYSCYRPNS; NKYLRGYSCYRPNSS; KYLRGYSCYRPNSSN; YLRGYSCYRPNSSNI; LRGYSCYRPNSSNIC; RGYSCYRPNSSNICC; GYSCYRPNSSNICCN; YSCYRPNSSNICCNC; SCYRPNSSNICCNCW; CYRPNSSNICCNCWC; YRPNSSNICCNCWCS; RPNSSNICCNCWCSW; PNSSNICCNCWCSWG; NSSNICCNCWCSWGY; SSNICCNCWCSWGYC; SNICCNCWCSWGYCW; NICCNCWCSWGYCWV; ICCNCWCSWGYCWVC; CCNCWCSWGYCWVCC; CNCWCSWGYCWVCCF; NCWCSWGYCWVCCFN; CWCSWGYCWVCCFNS; WCSWGYCWVCCFNSN; CSWGYCWVCCFNSNC; LGSQSFHCRPLSAIR; GSQSFHCRPLSAIRH; SQSFHCRPLSAIRHG; QSFHCRPLSAIRHGF; SFHCRPLSAIRHGFG; FHCRPLSAIRHGFGI; HCRPLSAIRHGFGIV; ALGSFFVCYYFPGFV; LGSFFVCYYFPGFVA; GSFFVCYYFPGFVAC; SFFVCYYFPGFVACY; YTFYNLTGIAEKNRK; TFYNLTGIAEKNRKI; FYNLTGIAEKNRKIF; IFGGNYLDNCKCPYK; FGGNYLDNCKCPYKL; GGNYLDNCKCPYKLL; QYRRSYTKNGLKKST; YRRSYTKNGLKKSTK; RRSYTKNGLKKSTKC; RSYTKNGLKKSTKCT; SYTKNGLKKSTKCTF; YTKNGLKKSTKCTFR; TKNGLKKSTKCTFRR; KNGLKKSTKCTFRRV; NGLKKSTKCTFRRVY; GLKKSTKCTFRRVYR; LKKSTKCTFRRVYRK; KKSTKCTFRRVYRKN; KSTKCTFRRVYRKNY; STKCTFRRVYRKNYC; TKCTFRRVYRKNYCP; KCTFRRVYRKNYCPR; CTFRRVYRKNYCPRR; TFRRVYRKNYCPRRC; SKNCSSMDVAFTSRP; KNCSSMDVAFTSRPV; NCSSMDVAFTSRPVR; CSSMDVAFTSRPVRD; SSMDVAFTSRPVRDC; SMDVAFTSRPVRDCN; MDVAFTSRPVRDCNT; DVAFTSRPVRDCNTC; VAFTSRPVRDCNTCS; RWPQPKEKESVQGQL; WPQPKEKESVQGQLP; PQPKEKESVQGQLPK; QPKEKESVQGQLPKS; PKEKESVQGQLPKSQ; KEKESVQGQLPKSQR; EKESVQGQLPKSQRN; KESVQGQLPKSQRNP; ESVQGQLPKSQRNPC; SVQGQLPKSQRNPCK; VQGQLPKSQRNPCKC; QGQLPKSQRNPCKCQ; GQLPKSQRNPCKCQN; QLPKSQRNPCKCQNY; TQKWGIQMKTLGALV; VLKMTLAVIAQREKC; LKMTLAVIAQREKCF; KMTLAVIAQREKCFP; MTLAVIAQREKCFPV; TLAVIAQREKCFPVT; LAVIAQREKCFPVTA; AVIAQREKCFPVTAQ; VIAQREKCFPVTAQQ; IAQREKCFPVTAQQE; AQREKCFPVTAQQEF; QREKCFPVTAQQEFP; REKCFPVTAQQEFPS; EKCFPVTAQQEFPSP; KCFPVTAQQEFPSPI; LACLTFMQGHKKCMS; ACLTFMQGHKKCMSM; CLTFMQGHKKCMSMV; LTFMQGHKKCMSMVE; TFMQGHKKCMSMVEE; FMQGHKKCMSMVEEN; MQGHKKCMSMVEENL; QGHKKCMSMVEENLF; GHKKCMSMVEENLFK; HKKCMSMVEENLFKA; KKCMSMVEENLFKAV; KCMSMVEENLFKAVI; CMSMVEENLFKAVIS; MSMVEENLFKAVIST; SMVEENLFKAVISTS; MVEENLFKAVISTSL; VEENLFKAVISTSLL; ILTIRPIWTKTMLIQ; LTIRPIWTKTMLIQL; TIRPIWTKTMLIQLS; IRPIWTKTMLIQLSA; RPIWTKTMLIQLSAG; PIWTKTMLIQLSAGY; IWTKTMLIQLSAGYL; WTKTMLIQLSAGYLI; TKTMLIQLSAGYLIP; KTMLIQLSAGYLIPV; TMLIQLSAGYLIPVE; MLIQLSAGYLIPVEM; LIQLSAGYLIPVEMK; IQLSAGYLIPVEMKM; QLSAGYLIPVEMKML; LSAGYLIPVEMKMLG; SAGYLIPVEMKMLGI; AGYLIPVEMKMLGIL; GYLIPVEMKMLGILG; YLIPVEMKMLGILGL; LIPVEMKMLGILGLS; IPVEMKMLGILGLSQ; PVEMKMLGILGLSQE; VEMKMLGILGLSQEG; EMKMLGILGLSQEGK; MKMLGILGLSQEGKM; KMLGILGLSQEGKMF; MLGILGLSQEGKMFP; LGILGLSQEGKMFPQ; GILGLSQEGKMFPQY; ILGLSQEGKMFPQYF; LGLSQEGKMFPQYFM; MNRVWGLFVKLIACM; NRVWGLFVKLIACMF; RVWGLFVKLIACMFQ; VWGLFVKLIACMFQL; WGLFVKLIACMFQLL; GLFVKLIACMFQLLI; LFVKLIACMFQLLIF; FVKLIACMFQLLIFV; VKLIACMFQLLIFVA; KLIACMFQLLIFVAC; LIACMFQLLIFVACL; IACMFQLLIFVACLL; ACMFQLLIFVACLLT; CMFQLLIFVACLLTA; MFQLLIFVACLLTAL; FQLLIFVACLLTALE; QLLIFVACLLTALEH; LLIFVACLLTALEHN; LIFVACLLTALEHNS; IFVACLLTALEHNSG; FVACLLTALEHNSGE; VACLLTALEHNSGEA; ACLLTALEHNSGEAL; CLLTALEHNSGEALQ; LLTALEHNSGEALQD; LTALEHNSGEALQDI; TALEHNSGEALQDIL; ALEHNSGEALQDILR; LEHNSGEALQDILRS; EHNSGEALQDILRSA; TGEPREWMGSLCMVW; GEPREWMGSLCMVWN; EPREWMGSLCMVWNP; PREWMGSLCMVWNPR; KRLGCLMAQKDFQGT; RLGCLMAQKDFQGTQ; LGCLMAQKDFQGTQI; DILTNRDNCKPKCFK; ILTNRDNCKPKCFKQ; LTNRDNCKPKCFKQV; TNRDNCKPKCFKQVL; NRDNCKPKCFKQVLL; RDNCKPKCFKQVLLL; DNCKPKCFKQVLLLY; NCKPKCFKQVLLLYI; CKPKCFKQVLLLYIY; KPKCFKQVLLLYIYI; MLLLYKPLLSLCYFG; LLLYKPLLSLCYFGG; LLYKPLLSLCYFGGG; LYKPLLSLCYFGGGV; YKPLLSLCYFGGGVL; KPLLSLCYFGGGVLG; PLLSLCYFGGGVLGL; LLSLCYFGGGVLGLL; LSLCYFGGGVLGLLK; SLCYFGGGVLGLLKH; LWGSDLWESSAGAEV; WGSDLWESSAGAEVS; GSDLWESSAGAEVSE; SDLWESSAGAEVSET; DLWESSAGAEVSETW; LWESSAGAEVSETWE; WESSAGAEVSETWEE; ESSAGAEVSETWEEH; SSAGAEVSETWEEHC; SAGAEVSETWEEHCD; AGAEVSETWEEHCDW; GAEVSETWEEHCDWD; AEVSETWEEHCDWDS; EVSETWEEHCDWDSV; VSETWEEHCDWDSVL; SETWEEHCDWDSVLD; ETWEEHCDWDSVLDP; TWEEHCDWDSVLDPC; WEEHCDWDSVLDPCP; EEHCDWDSVLDPCPE; EHCDWDSVLDPCPES; HCDWDSVLDPCPESS; CDWDSVLDPCPESSV; DWDSVLDPCPESSVS; WDSVLDPCPESSVSE; DSVLDPCPESSVSES; SVLDPCPESSVSESS; VLDPCPESSVSESSS; LDPCPESSVSESSSL; DPCPESSVSESSSLV; PCPESSVSESSSLVI; CPESSVSESSSLVIS; PESSVSESSSLVISR; ESSVSESSSLVISRI; SSVSESSSLVISRIH; SVSESSSLVISRIHF; VSESSSLVISRIHFP; SESSSLVISRIHFPM; ESSSLVISRIHFPMH; SSSLVISRIHFPMHI; SSLVISRIHFPMHIL; SLVISRIHFPMHILY; LVISRIHFPMHILYF; VISRIHFPMHILYFI; ISRIHFPMHILYFIL; SRIHFPMHILYFILE; RIHFPMHILYFILEK; IHFPMHILYFILEKV; HFPMHILYFILEKVY; FPMHILYFILEKVYI; PMHILYFILEKVYIL; MHILYFILEKVYILI; HILYFILEKVYILIS; ILYFILEKVYILISE; LYFILEKVYILISES; YFILEKVYILISESS; FILEKVYILISESSL; ILEKVYILISESSLS; LEKVYILISESSLSF; EKVYILISESSLSFH; KVYILISESSLSFHS; VYILISESSLSFHST; YILISESSLSFHSTI; ILISESSLSFHSTIL; LISESSLSFHSTILD; ISESSLSFHSTILDC; SESSLSFHSTILDCI; ESSLSFHSTILDCIS; SSLSFHSTILDCISV; SLSFHSTILDCISVA; LSFHSTILDCISVAK; SFHSTILDCISVAKS; FHSTILDCISVAKSA; HSTILDCISVAKSAT; STILDCISVAKSATG; TILDCISVAKSATGL; ILDCISVAKSATGLN; LDCISVAKSATGLNQ; DCISVAKSATGLNQI; CISVAKSATGLNQIS; ISVAKSATGLNQISS; SVAKSATGLNQISSS; VAKSATGLNQISSSN; AKSATGLNQISSSNK; KSATGLNQISSSNKV; SATGLNQISSSNKVI; ATGLNQISSSNKVIP; TGLNQISSSNKVIPL; GLNQISSSNKVIPLC; LNQISSSNKVIPLCK; NQISSSNKVIPLCKI; QISSSNKVIPLCKIL; ISSSNKVIPLCKILF; SSSNKVIPLCKILFS; SSNKVIPLCKILFSS; SNKVIPLCKILFSSK; NKVIPLCKILFSSKN; KVIPLCKILFSSKNS; VIPLCKILFSSKNSE; IPLCKILFSSKNSEF; PLCKILFSSKNSEFC; LCKILFSSKNSEFCK; CKILFSSKNSEFCKD; KILFSSKNSEFCKDF; ILFSSKNSEFCKDFL; LFSSKNSEFCKDFLK; FSSKNSEFCKDFLKY; SSKNSEFCKDFLKYI; SKNSEFCKDFLKYIL; KNSEFCKDFLKYILG; NSEFCKDFLKYILGL; SEFCKDFLKYILGLK; EFCKDFLKYILGLKS; FCKDFLKYILGLKSI; CKDFLKYILGLKSIC; KDFLKYILGLKSICL; DFLKYILGLKSICLT; FLKYILGLKSICLTN; LKYILGLKSICLTNL; KYILGLKSICLTNLA; YILGLKSICLTNLAC; ILGLKSICLTNLACR; LGLKSICLTNLACRV; GLKSICLTNLACRVL; LKSICLTNLACRVLG; KSICLTNLACRVLGT; SICLTNLACRVLGTG; ICLTNLACRVLGTGY; CLTNLACRVLGTGYS; LTNLACRVLGTGYSF; TNLACRVLGTGYSFI; NLACRVLGTGYSFIV; LACRVLGTGYSFIVT; ACRVLGTGYSFIVTK; CRVLGTGYSFIVTKP; RVLGTGYSFIVTKPG; VLGTGYSFIVTKPGG; LGTGYSFIVTKPGGN; GTGYSFIVTKPGGNI; TGYSFIVTKPGGNIW; GYSFIVTKPGGNIWV; YSFIVTKPGGNIWVL; SFIVTKPGGNIWVLL; FIVTKPGGNIWVLLF; IVTKPGGNIWVLLFK; VTKPGGNIWVLLFKC; TKPGGNIWVLLFKCF; KPGGNIWVLLFKCFF; PGGNIWVLLFKCFFS; GGNIWVLLFKCFFSK; GNIWVLLFKCFFSKF; NIWVLLFKCFFSKFT; IWVLLFKCFFSKFTL; WVLLFKCFFSKFTLT; VLLFKCFFSKFTLTL; LLFKCFFSKFTLTLP; LFKCFFSKFTLTLPS; FKCFFSKFTLTLPSK; SLKLSKLFIPCPEGK; LKLSKLFIPCPEGKS; KLSKLFIPCPEGKSF; LSKLFIPCPEGKSFD; SKLFIPCPEGKSFDS; KLFIPCPEGKSFDSA; LFIPCPEGKSFDSAP; FIPCPEGKSFDSAPV; IPCPEGKSFDSAPVP; PCPEGKSFDSAPVPF; CPEGKSFDSAPVPFT; PEGKSFDSAPVPFTS; EGKSFDSAPVPFTSS; GKSFDSAPVPFTSSK; KSFDSAPVPFTSSKT; SFDSAPVPFTSSKTT; FDSAPVPFTSSKTTM; DSAPVPFTSSKTTMY; SIATPSSKVSLSMGR; IATPSSKVSLSMGRF; ATPSSKVSLSMGRFT; TPSSKVSLSMGRFTF; PSSKVSLSMGRFTFK; SSKVSLSMGRFTFKA; SKVSLSMGRFTFKAL; KVSLSMGRFTFKALP; VSLSMGRFTFKALPP; SLSMGRFTFKALPPH; LSMGRFTFKALPPHK; SMGRFTFKALPPHKS; MGRFTFKALPPHKSN; GRFTFKALPPHKSNN; RFTFKALPPHKSNNP; FTFKALPPHKSNNPA; TFKALPPHKSNNPAA; FKALPPHKSNNPAAS; KALPPHKSNNPAASV; ALPPHKSNNPAASVV; LPPHKSNNPAASVVF; PPHKSNNPAASVVFP; PHKSNNPAASVVFPL; HKSNNPAASVVFPLS; KSNNPAASVVFPLSM; SNNPAASVVFPLSMG; NNPAASVVFPLSMGP; NPAASVVFPLSMGPL; PAASVVFPLSMGPLN; AASVVFPLSMGPLNN; ASVVFPLSMGPLNNQ; SVVFPLSMGPLNNQY; VVFPLSMGPLNNQYL; VFPLSMGPLNNQYLL; FPLSMGPLNNQYLLL; PLSMGPLNNQYLLLG; LSMGPLNNQYLLLGT; SMGPLNNQYLLLGTL; MGPLNNQYLLLGTLK; GPLNNQYLLLGTLKT; PLNNQYLLLGTLKTI; LNNQYLLLGTLKTIQ; NNQYLLLGTLKTIQC; NQYLLLGTLKTIQCK; QYLLLGTLKTIQCKK; YLLLGTLKTIQCKKS; LLLGTLKTIQCKKSN; LLGTLKTIQCKKSNI; LGTLKTIQCKKSNIT; GTLKTIQCKKSNITE; TLKTIQCKKSNITES; LKTIQCKKSNITESI; KTIQCKKSNITESIL; TIQCKKSNITESILG; IQCKKSNITESILGS; QCKKSNITESILGSK; CKKSNITESILGSKQ; KKSNITESILGSKQC; KSNITESILGSKQCS; SNITESILGSKQCSQ; NITESILGSKQCSQA; ITESILGSKQCSQAT; TESILGSKQCSQATP; ESILGSKQCSQATPA; SILGSKQCSQATPAI; ILGSKQCSQATPAIY; LGSKQCSQATPAIYC; GSKQCSQATPAIYCS; SKQCSQATPAIYCSS; KQCSQATPAIYCSST; QCSQATPAIYCSSTA; CSQATPAIYCSSTAF; SQATPAIYCSSTAFP; RVSTLFLAKTVSTAC; FLLSAKIIAFAKCFS; NSKYIPNNKNTSSHF; SKYIPNNKNTSSHFV; KYIPNNKNTSSHFVS; YIPNNKNTSSHFVST; IPNNKNTSSHFVSTA; PNNKNTSSHFVSTAY; NNKNTSSHFVSTAYS; NKNTSSHFVSTAYSV; KNTSSHFVSTAYSVI; NTSSHFVSTAYSVIN; TSSHFVSTAYSVINF; SSHFVSTAYSVINFQ; SHFVSTAYSVINFQD; HFVSTAYSVINFQDT; FVSTAYSVINFQDTC; VSTAYSVINFQDTCF; STAYSVINFQDTCFV; TAYSVINFQDTCFVS; AYSVINFQDTCFVSS; YSVINFQDTCFVSSG; SVINFQDTCFVSSGS; VINFQDTCFVSSGSS; INFQDTCFVSSGSSG; NFQDTCFVSSGSSGL; FQDTCFVSSGSSGLK; QDTCFVSSGSSGLKS; DTCFVSSGSSGLKSC; TCFVSSGSSGLKSCS; CFVSSGSSGLKSCSF; FVSSGSSGLKSCSFK; VSSGSSGLKSCSFKP; SSGSSGLKSCSFKPP; MLSSIVWYGSLVKAL; LSSIVWYGSLVKALY; SSIVWYGSLVKALYS; SIVWYGSLVKALYSK; IVWYGSLVKALYSKY; VWYGSLVKALYSKYS; WYGSLVKALYSKYSL; YGSLVKALYSKYSLL; GSLVKALYSKYSLLT; SLVKALYSKYSLLTP; LVKALYSKYSLLTPL; VKALYSKYSLLTPLQ; KALYSKYSLLTPLQI; ALYSKYSLLTPLQIK; LYSKYSLLTPLQIKK; YSKYSLLTPLQIKKL; SKYSLLTPLQIKKLK; KYSLLTPLQIKKLKV; YSLLTPLQIKKLKVH; SLLTPLQIKKLKVHS; LLTPLQIKKLKVHSF; QKLLIAETLCLCGVK; KLLIAETLCLCGVKK; LLIAETLCLCGVKKN; LIAETLCLCGVKKNI; IAETLCLCGVKKNII; AETLCLCGVKKNIIL; ETLCLCGVKKNIILC; TLCLCGVKKNIILCP; LCLCGVKKNIILCPA; CLCGVKKNIILCPAH; LCGVKKNIILCPAHM; CGVKKNIILCPAHMC; GVKKNIILCPAHMCL; VKKNIILCPAHMCLL; KKNIILCPAHMCLLI; KNIILCPAHMCLLIK; NIILCPAHMCLLIKV; IILCPAHMCLLIKVT; ILCPAHMCLLIKVTE; LCPAHMCLLIKVTEY; CPAHMCLLIKVTEYF; PAHMCLLIKVTEYFS; AHMCLLIKVTEYFSI; HMCLLIKVTEYFSIS; MCLLIKVTEYFSISF; CLLIKVTEYFSISFL; LLIKVTEYFSISFLY; LIKVTEYFSISFLYR; IKVTEYFSISFLYRI; AFSLVVYTAKQARVL; FSLVVYTAKQARVLL; SLVVYTAKQARVLLL; LVVYTAKQARVLLLN; VVYTAKQARVLLLNT; VYTAKQARVLLLNTA; LRNWCRSEGKSLGSS; RNWCRSEGKSLGSST; NWCRSEGKSLGSSTF; WCRSEGKSLGSSTFL; CRSEGKSLGSSTFLF; RSEGKSLGSSTFLFF; SEGKSLGSSTFLFFL; EGKSLGSSTFLFFLG; GKSLGSSTFLFFLGG; KSLGSSTFLFFLGGV; SLGSSTFLFFLGGVE; LGSSTFLFFLGGVEC; ESAVASSSLANISSW; SAVASSSLANISSWQ; AVASSSLANISSWQN; VASSSLANISSWQNK; ASSSLANISSWQNKS; SSSLANISSWQNKSS; SSLANISSWQNKSSS; SLANISSWQNKSSSH; LANISSWQNKSSSHF; ANISSWQNKSSSHFS; NISSWQNKSSSHFSL; ISSWQNKSSSHFSLK; SSWQNKSSSHFSLKE; SWQNKSSSHFSLKEL; WQNKSSSHFSLKELH; QNKSSSHFSLKELHQ; NKSSSHFSLKELHQD; KSSSHFSLKELHQDS; SSSHFSLKELHQDSH; SSHFSLKELHQDSHS; SHFSLKELHQDSHSS; HFSLKELHQDSHSSV; FSLKELHQDSHSSVP; VGTYKKNNYLGPFNI; GTYKKNNYLGPFNIL; TYKKNNYLGPFNILL; YKKNNYLGPFNILLF; KKNNYLGPFNILLFI; REFLQLFGPTIAEFL; EFLQLFGPTIAEFLQ; FLQLFGPTIAEFLQL; LQLFGPTIAEFLQLG; QLFGPTIAEFLQLGL; LFGPTIAEFLQLGLS; FGPTIAEFLQLGLSQ; GPTIAEFLQLGLSQT; PTIAEFLQLGLSQTT; TIAEFLQLGLSQTTV; SSQCSSNLSKPRALF; SQCSSNLSKPRALFL; QCSSNLSKPRALFLK; CSSNLSKPRALFLKI; SSNLSKPRALFLKIF; SNLSKPRALFLKIFY; NLSKPRALFLKIFYL; LSKPRALFLKIFYLN; SKPRALFLKIFYLNA; KPRALFLKIFYLNAL; PRALFLKIFYLNALI; ADIACKGSAQKAFWN; DIACKGSAQKAFWNK; AIPCSTGYLGKEENQ; IPCSTGYLGKEENQH; PCSTGYLGKEENQHK; CSTGYLGKEENQHKP; STGYLGKEENQHKPL; TGYLGKEENQHKPLS; GYLGKEENQHKPLSY; YLGKEENQHKPLSYS; LGKEENQHKPLSYSR; GKEENQHKPLSYSRF; KEENQHKPLSYSRFQ; EENQHKPLSYSRFQN; ENQHKPLSYSRFQNQ; NQHKPLSYSRFQNQA; QHKPLSYSRFQNQAD; HKPLSYSRFQNQADE; KPLSYSRFQNQADEL; PLSYSRFQNQADELP; LSYSRFQNQADELPL; SYSRFQNQADELPLH; YSRFQNQADELPLHP; SRFQNQADELPLHPA; RFQNQADELPLHPAP; FQNQADELPLHPAPF; QNQADELPLHPAPFF; NQADELPLHPAPFFY; QADELPLHPAPFFYT; ADELPLHPAPFFYTK; DELPLHPAPFFYTKY; ELPLHPAPFFYTKYS; LPLHPAPFFYTKYSF; PLHPAPFFYTKYSFS; LHPAPFFYTKYSFSS; HPAPFFYTKYSFSSF; PAPFFYTKYSFSSFY; APFFYTKYSFSSFYP; PFFYTKYSFSSFYPR; FFYTKYSFSSFYPRR; FYTKYSFSSFYPRRP; YTKYSFSSFYPRRPL; TKYSFSSFYPRRPLC; KYSFSSFYPRRPLCQ; YSFSSFYPRRPLCQG; SFSSFYPRRPLCQGE; FSSFYPRRPLCQGEI; SSFYPRRPLCQGEIP; SFYPRRPLCQGEIPY; FYPRRPLCQGEIPYT; YPRRPLCQGEIPYTS; PRRPLCQGEIPYTSL; RRPLCQGEIPYTSLN; RPLCQGEIPYTSLNK; PLCQGEIPYTSLNKL; LCQGEIPYTSLNKLF; CQGEIPYTSLNKLFS; QGEIPYTSLNKLFSL; GEIPYTSLNKLFSLR; EIPYTSLNKLFSLRE; IPYTSLNKLFSLRED; PYTSLNKLFSLREDF; YTSLNKLFSLREDFP; TSLNKLFSLREDFPR; SLNKLFSLREDFPRQ; LNKLFSLREDFPRQL; NKLFSLREDFPRQLF; KLFSLREDFPRQLFQ; LFSLREDFPRQLFQG; FSLREDFPRQLFQGL; SLREDFPRQLFQGLK; LREDFPRQLFQGLKG; REDFPRQLFQGLKGP 16 mers: GFPQIVLLGLRKSLHT; FPQIVLLGLRKSLHTL; PQIVLLGLRKSLHTLT; QIVLLGLRKSLHTLTT; EKGWRQRRPRPLIYYK; KGWRQRRPRPLIYYKK; GWRQRRPRPLIYYKKK; WRQRRPRPLIYYKKKG; RQRRPRPLIYYKKKGH; QRRPRPLIYYKKKGHR; RRPRPLIYYKKKGHRE; RPRPLIYYKKKGHREE; PRPLIYYKKKGHREEL; RPLIYYKKKGHREELL; PLIYYKKKGHREELLT; LIYYKKKGHREELLTH; IYYKKKGHREELLTHG; YYKKKGHREELLTHGM; YKKKGHREELLTHGMQ; KKKGHREELLTHGMQP; KKGHREELLTHGMQPN; KGHREELLTHGMQPNH; GHREELLTHGMQPNHD; HREELLTHGMQPNHDL; REELLTHGMQPNHDLR; EELLTHGMQPNHDLRK; ELLTHGMQPNHDLRKE; LLTHGMQPNHDLRKES; LTHGMQPNHDLRKESA; LTGECSQTMTSGRKVH; TGECSQTMTSGRKVHD; GECSQTMTSGRKVHDS; ECSQTMTSGRKVHDSQ; CSQTMTSGRKVHDSQG; SQTMTSGRKVHDSQGG; QTMTSGRKVHDSQGGA; TMTSGRKVHDSQGGAA; MTSGRKVHDSQGGAAY; TSGRKVHDSQGGAAYP; SGRKVHDSQGGAAYPW; GRKVHDSQGGAAYPWN; RKVHDSQGGAAYPWNA; KVHDSQGGAAYPWNAA; VHDSQGGAAYPWNAAK; HDSQGGAAYPWNAAKP; PQEGKCMTDMFCEPRN; QEGKCMTDMFCEPRNL; EGKCMTDMFCEPRNLG; GKCMTDMFCEPRNLGL; KCMTDMFCEPRNLGLV; CMTDMFCEPRNLGLVP; MTDMFCEPRNLGLVPS; TGQRPWFCASCHDKLQ; KLVKPGLEQKKELRGF; LVKPGLEQKKELRGFL; VKPGLEQKKELRGFLF; KPGLEQKKELRGFLFL; PGLEQKKELRGFLFLF; VIPFFLYFQVHGCCSS; IPFFLYFQVHGCCSST; PFFLYFQVHGCCSSTF; FFLYFQVHGCCSSTFG; FLYFQVHGCCSSTFGG; LYFQVHGCCSSTFGGP; YFQVHGCCSSTFGGPS; FQVHGCCSSTFGGPSC; QVHGCCSSTFGGPSCQ; VHGCCSSTFGGPSCQC; HGCCSSTFGGPSCQCI; NCCWGGCCCYRSSNCI; CCWGGCCCYRSSNCIP; CWGGCCCYRSSNCIPC; WGGCCCYRSSNCIPCY; GGCCCYRSSNCIPCYC; GCCCYRSSNCIPCYCR; CCCYRSSNCIPCYCRG; CCYRSSNCIPCYCRGH; CYRSSNCIPCYCRGHN; YRSSNCIPCYCRGHNK; RSSNCIPCYCRGHNKY; SSNCIPCYCRGHNKYL; SNCIPCYCRGHNKYLR; NCIPCYCRGHNKYLRG; CIPCYCRGHNKYLRGY; IPCYCRGHNKYLRGYS; PCYCRGHNKYLRGYSC; CYCRGHNKYLRGYSCY; YCRGHNKYLRGYSCYR; CRGHNKYLRGYSCYRP; RGHNKYLRGYSCYRPN; GHNKYLRGYSCYRPNS; HNKYLRGYSCYRPNSS; NKYLRGYSCYRPNSSN; KYLRGYSCYRPNSSNI; YLRGYSCYRPNSSNIC; LRGYSCYRPNSSNICC; RGYSCYRPNSSNICCN; GYSCYRPNSSNICCNC; YSCYRPNSSNICCNCW; SCYRPNSSNICCNCWC; CYRPNSSNICCNCWCS; YRPNSSNICCNCWCSW; RPNSSNICCNCWCSWG; PNSSNICCNCWCSWGY; NSSNICCNCWCSWGYC; SSNICCNCWCSWGYCW; SNICCNCWCSWGYCWV; NICCNCWCSWGYCWVC; ICCNCWCSWGYCWVCC; CCNCWCSWGYCWVCCF; CNCWCSWGYCWVCCFN; NCWCSWGYCWVCCFNS; CWCSWGYCWVCCFNSN; WCSWGYCWVCCFNSNC; LGSQSFHCRPLSAIRH; GSQSFHCRPLSAIRHG; SQSFHCRPLSAIRHGF; QSFHCRPLSAIRHGFG; SFHCRPLSAIRHGFGI; FHCRPLSAIRHGFGIV; ALGSFFVCYYFPGFVA; LGSFFVCYYFPGFVAC; GSFFVCYYFPGFVACY; YTFYNLTGIAEKNRKI; TFYNLTGIAEKNRKIF; IFGGNYLDNCKCPYKL; FGGNYLDNCKCPYKLL; QYRRSYTKNGLKKSTK; YRRSYTKNGLKKSTKC; RRSYTKNGLKKSTKCT; RSYTKNGLKKSTKCTF; SYTKNGLKKSTKCTFR; YTKNGLKKSTKCTFRR; TKNGLKKSTKCTFRRV; KNGLKKSTKCTFRRVY; NGLKKSTKCTFRRVYR; GLKKSTKCTFRRVYRK; LKKSTKCTFRRVYRKN; KKSTKCTFRRVYRKNY; KSTKCTFRRVYRKNYC; STKCTFRRVYRKNYCP; TKCTFRRVYRKNYCPR; KCTFRRVYRKNYCPRR; CTFRRVYRKNYCPRRC; SKNCSSMDVAFTSRPV; KNCSSMDVAFTSRPVR; NCSSMDVAFTSRPVRD; CSSMDVAFTSRPVRDC; SSMDVAFTSRPVRDCN; SMDVAFTSRPVRDCNT; MDVAFTSRPVRDCNTC; DVAFTSRPVRDCNTCS; RWPQPKEKESVQGQLP; WPQPKEKESVQGQLPK; PQPKEKESVQGQLPKS; QPKEKESVQGQLPKSQ; PKEKESVQGQLPKSQR; KEKESVQGQLPKSQRN; EKESVQGQLPKSQRNP; KESVQGQLPKSQRNPC; ESVQGQLPKSQRNPCK; SVQGQLPKSQRNPCKC; VQGQLPKSQRNPCKCQ; QGQLPKSQRNPCKCQN; GQLPKSQRNPCKCQNY; VLKMTLAVIAQREKCF; LKMTLAVIAQREKCFP; KMTLAVIAQREKCFPV; MTLAVIAQREKCFPVT; TLAVIAQREKCFPVTA; LAVIAQREKCFPVTAQ; AVIAQREKCFPVTAQQ; VIAQREKCFPVTAQQE; IAQREKCFPVTAQQEF; AQREKCFPVTAQQEFP; QREKCFPVTAQQEFPS; REKCFPVTAQQEFPSP; EKCFPVTAQQEFPSPI; LACLTFMQGHKKCMSM; ACLTFMQGHKKCMSMV; CLTFMQGHKKCMSMVE; LTFMQGHKKCMSMVEE; TFMQGHKKCMSMVEEN; FMQGHKKCMSMVEENL; MQGHKKCMSMVEENLF; QGHKKCMSMVEENLFK; GHKKCMSMVEENLFKA; HKKCMSMVEENLFKAV; KKCMSMVEENLFKAVI; KCMSMVEENLFKAVIS; CMSMVEENLFKAVIST; MSMVEENLFKAVISTS; SMVEENLFKAVISTSL; MVEENLFKAVISTSLL; ILTIRPIWTKTMLIQL; LTIRPIWTKTMLIQLS; TIRPIWTKTMLIQLSA; IRPIWTKTMLIQLSAG; RPIWTKTMLIQLSAGY; PIWTKTMLIQLSAGYL; IWTKTMLIQLSAGYLI; WTKTMLIQLSAGYLIP; TKTMLIQLSAGYLIPV; KTMLIQLSAGYLIPVE; TMLIQLSAGYLIPVEM; MLIQLSAGYLIPVEMK; LIQLSAGYLIPVEMKM; IQLSAGYLIPVEMKML; QLSAGYLIPVEMKMLG; LSAGYLIPVEMKMLGI; SAGYLIPVEMKMLGIL; AGYLIPVEMKMLGILG; GYLIPVEMKMLGILGL; YLIPVEMKMLGILGLS; LIPVEMKMLGILGLSQ; IPVEMKMLGILGLSQE; PVEMKMLGILGLSQEG; VEMKMLGILGLSQEGK; EMKMLGILGLSQEGKM; MKMLGILGLSQEGKMF; KMLGILGLSQEGKMFP; MLGILGLSQEGKMFPQ; LGILGLSQEGKMFPQY; GILGLSQEGKMFPQYF; ILGLSQEGKMFPQYFM; MNRVWGLFVKLIACMF; NRVWGLFVKLIACMFQ; RVWGLFVKLIACMFQL; VWGLFVKLIACMFQLL; WGLFVKLIACMFQLLI; GLFVKLIACMFQLLIF; LFVKLIACMFQLLIFV; FVKLIACMFQLLIFVA; VKLIACMFQLLIFVAC; KLIACMFQLLIFVACL; LIACMFQLLIFVACLL; IACMFQLLIFVACLLT; ACMFQLLIFVACLLTA; CMFQLLIFVACLLTAL; MFQLLIFVACLLTALE; FQLLIFVACLLTALEH; QLLIFVACLLTALEHN; LLIFVACLLTALEHNS; LIFVACLLTALEHNSG; IFVACLLTALEHNSGE; FVACLLTALEHNSGEA; VACLLTALEHNSGEAL; ACLLTALEHNSGEALQ; CLLTALEHNSGEALQD; LLTALEHNSGEALQDI; LTALEHNSGEALQDIL; TALEHNSGEALQDILR; ALEHNSGEALQDILRS; LEHNSGEALQDILRSA; TGEPREWMGSLCMVWN; GEPREWMGSLCMVWNP; EPREWMGSLCMVWNPR; KRLGCLMAQKDFQGTQ; RLGCLMAQKDFQGTQI; DILTNRDNCKPKCFKQ; ILTNRDNCKPKCFKQV; LTNRDNCKPKCFKQVL; TNRDNCKPKCFKQVLL; NRDNCKPKCFKQVLLL; RDNCKPKCFKQVLLLY; DNCKPKCFKQVLLLYI; NCKPKCFKQVLLLYIY; CKPKCFKQVLLLYIYI; MLLLYKPLLSLCYFGG; LLLYKPLLSLCYFGGG; LLYKPLLSLCYFGGGV; LYKPLLSLCYFGGGVL; YKPLLSLCYFGGGVLG; KPLLSLCYFGGGVLGL; PLLSLCYFGGGVLGLL; LLSLCYFGGGVLGLLK; LSLCYFGGGVLGLLKH; LWGSDLWESSAGAEVS; WGSDLWESSAGAEVSE; GSDLWESSAGAEVSET; SDLWESSAGAEVSETW; DLWESSAGAEVSETWE; LWESSAGAEVSETWEE; WESSAGAEVSETWEEH; ESSAGAEVSETWEEHC; SSAGAEVSETWEEHCD; SAGAEVSETWEEHCDW; AGAEVSETWEEHCDWD; GAEVSETWEEHCDWDS; AEVSETWEEHCDWDSV; EVSETWEEHCDWDSVL; VSETWEEHCDWDSVLD; SETWEEHCDWDSVLDP; ETWEEHCDWDSVLDPC; TWEEHCDWDSVLDPCP; WEEHCDWDSVLDPCPE; EEHCDWDSVLDPCPES; EHCDWDSVLDPCPESS; HCDWDSVLDPCPESSV; CDWDSVLDPCPESSVS; DWDSVLDPCPESSVSE; WDSVLDPCPESSVSES; DSVLDPCPESSVSESS; SVLDPCPESSVSESSS; VLDPCPESSVSESSSL; LDPCPESSVSESSSLV; DPCPESSVSESSSLVI; PCPESSVSESSSLVIS; CPESSVSESSSLVISR; PESSVSESSSLVISRI; ESSVSESSSLVISRIH; SSVSESSSLVISRIHF; SVSESSSLVISRIHFP; VSESSSLVISRIHFPM; SESSSLVISRIHFPMH; ESSSLVISRIHFPMHI; SSSLVISRIHFPMHIL; SSLVISRIHFPMHILY; SLVISRIHFPMHILYF; LVISRIHFPMHILYFI; VISRIHFPMHILYFIL; ISRIHFPMHILYFILE; SRIHFPMHILYFILEK; RIHFPMHILYFILEKV; IHFPMHILYFILEKVY; HFPMHILYFILEKVYI; FPMHILYFILEKVYIL; PMHILYFILEKVYILI; MHILYFILEKVYILIS; HILYFILEKVYILISE; ILYFILEKVYILISES; LYFILEKVYILISESS; YFILEKVYILISESSL; FILEKVYILISESSLS; ILEKVYILISESSLSF; LEKVYILISESSLSFH; EKVYILISESSLSFHS; KVYILISESSLSFHST; VYILISESSLSFHSTI; YILISESSLSFHSTIL; ILISESSLSFHSTILD; LISESSLSFHSTILDC; ISESSLSFHSTILDCI; SESSLSFHSTILDCIS; ESSLSFHSTILDCISV; SSLSFHSTILDCISVA; SLSFHSTILDCISVAK; LSFHSTILDCISVAKS; SFHSTILDCISVAKSA; FHSTILDCISVAKSAT; HSTILDCISVAKSATG; STILDCISVAKSATGL; TILDCISVAKSATGLN; ILDCISVAKSATGLNQ; LDCISVAKSATGLNQI; DCISVAKSATGLNQIS; CISVAKSATGLNQISS; ISVAKSATGLNQISSS; SVAKSATGLNQISSSN; VAKSATGLNQISSSNK; AKSATGLNQISSSNKV; KSATGLNQISSSNKVI; SATGLNQISSSNKVIP; ATGLNQISSSNKVIPL; TGLNQISSSNKVIPLC; GLNQISSSNKVIPLCK; LNQISSSNKVIPLCKI; NQISSSNKVIPLCKIL; QISSSNKVIPLCKILF; ISSSNKVIPLCKILFS; SSSNKVIPLCKILFSS; SSNKVIPLCKILFSSK; SNKVIPLCKILFSSKN; NKVIPLCKILFSSKNS; KVIPLCKILFSSKNSE; VIPLCKILFSSKNSEF; IPLCKILFSSKNSEFC; PLCKILFSSKNSEFCK; LCKILFSSKNSEFCKD; CKILFSSKNSEFCKDF; KILFSSKNSEFCKDFL; ILFSSKNSEFCKDFLK; LFSSKNSEFCKDFLKY; FSSKNSEFCKDFLKYI; SSKNSEFCKDFLKYIL; SKNSEFCKDFLKYILG; KNSEFCKDFLKYILGL; NSEFCKDFLKYILGLK; SEFCKDFLKYILGLKS; EFCKDFLKYILGLKSI; FCKDFLKYILGLKSIC; CKDFLKYILGLKSICL; KDFLKYILGLKSICLT; DFLKYILGLKSICLTN; FLKYILGLKSICLTNL; LKYILGLKSICLTNLA; KYILGLKSICLTNLAC; YILGLKSICLTNLACR; ILGLKSICLTNLACRV; LGLKSICLTNLACRVL; GLKSICLTNLACRVLG; LKSICLTNLACRVLGT; KSICLTNLACRVLGTG; SICLTNLACRVLGTGY; ICLTNLACRVLGTGYS; CLTNLACRVLGTGYSF; LTNLACRVLGTGYSFI; TNLACRVLGTGYSFIV; NLACRVLGTGYSFIVT; LACRVLGTGYSFIVTK; ACRVLGTGYSFIVTKP; CRVLGTGYSFIVTKPG; RVLGTGYSFIVTKPGG; VLGTGYSFIVTKPGGN; LGTGYSFIVTKPGGNI; GTGYSFIVTKPGGNIW; TGYSFIVTKPGGNIWV; GYSFIVTKPGGNIWVL; YSFIVTKPGGNIWVLL; SFIVTKPGGNIWVLLF; FIVTKPGGNIWVLLFK; IVTKPGGNIWVLLFKC; VTKPGGNIWVLLFKCF; TKPGGNIWVLLFKCFF; KPGGNIWVLLFKCFFS; PGGNIWVLLFKCFFSK; GGNIWVLLFKCFFSKF; GNIWVLLFKCFFSKFT; NIWVLLFKCFFSKFTL; IWVLLFKCFFSKFTLT; WVLLFKCFFSKFTLTL; VLLFKCFFSKFTLTLP; LLFKCFFSKFTLTLPS; LFKCFFSKFTLTLPSK; SLKLSKLFIPCPEGKS; LKLSKLFIPCPEGKSF; KLSKLFIPCPEGKSFD; LSKLFIPCPEGKSFDS; SKLFIPCPEGKSFDSA; KLFIPCPEGKSFDSAP; LFIPCPEGKSFDSAPV; FIPCPEGKSFDSAPVP; IPCPEGKSFDSAPVPF; PCPEGKSFDSAPVPFT; CPEGKSFDSAPVPFTS; PEGKSFDSAPVPFTSS; EGKSFDSAPVPFTSSK; GKSFDSAPVPFTSSKT; KSFDSAPVPFTSSKTT; SFDSAPVPFTSSKTTM; FDSAPVPFTSSKTTMY; SIATPSSKVSLSMGRF; IATPSSKVSLSMGRFT; ATPSSKVSLSMGRFTF; TPSSKVSLSMGRFTFK; PSSKVSLSMGRFTFKA; SSKVSLSMGRFTFKAL; SKVSLSMGRFTFKALP; KVSLSMGRFTFKALPP; VSLSMGRFTFKALPPH; SLSMGRFTFKALPPHK; LSMGRFTFKALPPHKS; SMGRFTFKALPPHKSN; MGRFTFKALPPHKSNN; GRFTFKALPPHKSNNP; RFTFKALPPHKSNNPA; FTFKALPPHKSNNPAA; TFKALPPHKSNNPAAS; FKALPPHKSNNPAASV; KALPPHKSNNPAASVV; ALPPHKSNNPAASVVF; LPPHKSNNPAASVVFP; PPHKSNNPAASVVFPL; PHKSNNPAASVVFPLS; HKSNNPAASVVFPLSM; KSNNPAASVVFPLSMG; SNNPAASVVFPLSMGP; NNPAASVVFPLSMGPL; NPAASVVFPLSMGPLN; PAASVVFPLSMGPLNN; AASVVFPLSMGPLNNQ; ASVVFPLSMGPLNNQY; SVVFPLSMGPLNNQYL; VVFPLSMGPLNNQYLL; VFPLSMGPLNNQYLLL; FPLSMGPLNNQYLLLG; PLSMGPLNNQYLLLGT; LSMGPLNNQYLLLGTL; SMGPLNNQYLLLGTLK; MGPLNNQYLLLGTLKT; GPLNNQYLLLGTLKTI; PLNNQYLLLGTLKTIQ; LNNQYLLLGTLKTIQC; NNQYLLLGTLKTIQCK; NQYLLLGTLKTIQCKK; QYLLLGTLKTIQCKKS; YLLLGTLKTIQCKKSN; LLLGTLKTIQCKKSNI; LLGTLKTIQCKKSNIT; LGTLKTIQCKKSNITE; GTLKTIQCKKSNITES; TLKTIQCKKSNITESI; LKTIQCKKSNITESIL; KTIQCKKSNITESILG; TIQCKKSNITESILGS; IQCKKSNITESILGSK; QCKKSNITESILGSKQ; CKKSNITESILGSKQC; KKSNITESILGSKQCS; KSNITESILGSKQCSQ; SNITESILGSKQCSQA; NITESILGSKQCSQAT; ITESILGSKQCSQATP; TESILGSKQCSQATPA; ESILGSKQCSQATPAI; SILGSKQCSQATPAIY; ILGSKQCSQATPAIYC; LGSKQCSQATPAIYCS; GSKQCSQATPAIYCSS; SKQCSQATPAIYCSST; KQCSQATPAIYCSSTA; QCSQATPAIYCSSTAF; CSQATPAIYCSSTAFP; NSKYIPNNKNTSSHFV; SKYIPNNKNTSSHFVS; KYIPNNKNTSSHFVST; YIPNNKNTSSHFVSTA; IPNNKNTSSHFVSTAY; PNNKNTSSHFVSTAYS; NNKNTSSHFVSTAYSV; NKNTSSHFVSTAYSVI; KNTSSHFVSTAYSVIN; NTSSHFVSTAYSVINF; TSSHFVSTAYSVINFQ; SSHFVSTAYSVINFQD; SHFVSTAYSVINFQDT; HFVSTAYSVINFQDTC; FVSTAYSVINFQDTCF; VSTAYSVINFQDTCFV; STAYSVINFQDTCFVS; TAYSVINFQDTCFVSS; AYSVINFQDTCFVSSG; YSVINFQDTCFVSSGS; SVINFQDTCFVSSGSS; VINFQDTCFVSSGSSG; INFQDTCFVSSGSSGL; NFQDTCFVSSGSSGLK; FQDTCFVSSGSSGLKS; QDTCFVSSGSSGLKSC; DTCFVSSGSSGLKSCS; TCFVSSGSSGLKSCSF; CFVSSGSSGLKSCSFK; FVSSGSSGLKSCSFKP; VSSGSSGLKSCSFKPP; MLSSIVWYGSLVKALY; LSSIVWYGSLVKALYS; SSIVWYGSLVKALYSK; SIVWYGSLVKALYSKY; IVWYGSLVKALYSKYS; VWYGSLVKALYSKYSL; WYGSLVKALYSKYSLL; YGSLVKALYSKYSLLT; GSLVKALYSKYSLLTP; SLVKALYSKYSLLTPL; LVKALYSKYSLLTPLQ; VKALYSKYSLLTPLQI; KALYSKYSLLTPLQIK; ALYSKYSLLTPLQIKK; LYSKYSLLTPLQIKKL; YSKYSLLTPLQIKKLK; SKYSLLTPLQIKKLKV; KYSLLTPLQIKKLKVH; YSLLTPLQIKKLKVHS; SLLTPLQIKKLKVHSF; QKLLIAETLCLCGVKK; KLLIAETLCLCGVKKN; LLIAETLCLCGVKKNI; LIAETLCLCGVKKNII; IAETLCLCGVKKNIIL; AETLCLCGVKKNIILC; ETLCLCGVKKNIILCP; TLCLCGVKKNIILCPA; LCLCGVKKNIILCPAH; CLCGVKKNIILCPAHM; LCGVKKNIILCPAHMC; CGVKKNIILCPAHMCL; GVKKNIILCPAHMCLL; VKKNIILCPAHMCLLI; KKNIILCPAHMCLLIK; KNIILCPAHMCLLIKV; NIILCPAHMCLLIKVT; IILCPAHMCLLIKVTE; ILCPAHMCLLIKVTEY; LCPAHMCLLIKVTEYF; CPAHMCLLIKVTEYFS; PAHMCLLIKVTEYFSI; AHMCLLIKVTEYFSIS; HMCLLIKVTEYFSISF; MCLLIKVTEYFSISFL; CLLIKVTEYFSISFLY; LLIKVTEYFSISFLYR; LIKVTEYFSISFLYRI; AFSLVVYTAKQARVLL; FSLVVYTAKQARVLLL; SLVVYTAKQARVLLLN; LVVYTAKQARVLLLNT; VVYTAKQARVLLLNTA; LRNWCRSEGKSLGSST; RNWCRSEGKSLGSSTF; NWCRSEGKSLGSSTFL; WCRSEGKSLGSSTFLF; CRSEGKSLGSSTFLFF; RSEGKSLGSSTFLFFL; SEGKSLGSSTFLFFLG; EGKSLGSSTFLFFLGG; GKSLGSSTFLFFLGGV; KSLGSSTFLFFLGGVE; SLGSSTFLFFLGGVEC; ESAVASSSLANISSWQ; SAVASSSLANISSWQN; AVASSSLANISSWQNK; VASSSLANISSWQNKS; ASSSLANISSWQNKSS; SSSLANISSWQNKSSS; SSLANISSWQNKSSSH; SLANISSWQNKSSSHF; LANISSWQNKSSSHFS; ANISSWQNKSSSHFSL; NISSWQNKSSSHFSLK; ISSWQNKSSSHFSLKE; SSWQNKSSSHFSLKEL; SWQNKSSSHFSLKELH; WQNKSSSHFSLKELHQ; QNKSSSHFSLKELHQD; NKSSSHFSLKELHQDS; KSSSHFSLKELHQDSH; SSSHFSLKELHQDSHS; SSHFSLKELHQDSHSS; SHFSLKELHQDSHSSV; HFSLKELHQDSHSSVP; VGTYKKNNYLGPFNIL; GTYKKNNYLGPFNILL; TYKKNNYLGPFNILLF; YKKNNYLGPFNILLFI; REFLQLFGPTIAEFLQ; EFLQLFGPTIAEFLQL; FLQLFGPTIAEFLQLG; LQLFGPTIAEFLQLGL; QLFGPTIAEFLQLGLS; LFGPTIAEFLQLGLSQ; FGPTIAEFLQLGLSQT; GPTIAEFLQLGLSQTT; PTIAEFLQLGLSQTTV; SSQCSSNLSKPRALFL; SQCSSNLSKPRALFLK; QCSSNLSKPRALFLKI; CSSNLSKPRALFLKIF; SSNLSKPRALFLKIFY; SNLSKPRALFLKIFYL; NLSKPRALFLKIFYLN; LSKPRALFLKIFYLNA; SKPRALFLKIFYLNAL; KPRALFLKIFYLNALI; ADIACKGSAQKAFWNK; AIPCSTGYLGKEENQH; IPCSTGYLGKEENQHK; PCSTGYLGKEENQHKP; CSTGYLGKEENQHKPL; STGYLGKEENQHKPLS; TGYLGKEENQHKPLSY; GYLGKEENQHKPLSYS; YLGKEENQHKPLSYSR; LGKEENQHKPLSYSRF; GKEENQHKPLSYSRFQ; KEENQHKPLSYSRFQN; EENQHKPLSYSRFQNQ; ENQHKPLSYSRFQNQA; NQHKPLSYSRFQNQAD; QHKPLSYSRFQNQADE; HKPLSYSRFQNQADEL; KPLSYSRFQNQADELP; PLSYSRFQNQADELPL; LSYSRFQNQADELPLH; SYSRFQNQADELPLHP; YSRFQNQADELPLHPA; SRFQNQADELPLHPAP; RFQNQADELPLHPAPF; FQNQADELPLHPAPFF; QNQADELPLHPAPFFY; NQADELPLHPAPFFYT; QADELPLHPAPFFYTK; ADELPLHPAPFFYTKY; DELPLHPAPFFYTKYS; ELPLHPAPFFYTKYSF; LPLHPAPFFYTKYSFS; PLHPAPFFYTKYSFSS; LHPAPFFYTKYSFSSF; HPAPFFYTKYSFSSFY; PAPFFYTKYSFSSFYP; APFFYTKYSFSSFYPR; PFFYTKYSFSSFYPRR; FFYTKYSFSSFYPRRP; FYTKYSFSSFYPRRPL; YTKYSFSSFYPRRPLC; TKYSFSSFYPRRPLCQ; KYSFSSFYPRRPLCQG; YSFSSFYPRRPLCQGE; SFSSFYPRRPLCQGEI; FSSFYPRRPLCQGEIP; SSFYPRRPLCQGEIPY; SFYPRRPLCQGEIPYT; FYPRRPLCQGEIPYTS; YPRRPLCQGEIPYTSL; PRRPLCQGEIPYTSLN; RRPLCQGEIPYTSLNK; RPLCQGEIPYTSLNKL; PLCQGEIPYTSLNKLF; LCQGEIPYTSLNKLFS; CQGEIPYTSLNKLFSL; QGEIPYTSLNKLFSLR; GEIPYTSLNKLFSLRE; EIPYTSLNKLFSLRED; IPYTSLNKLFSLREDF; PYTSLNKLFSLREDFP; YTSLNKLFSLREDFPR; TSLNKLFSLREDFPRQ; SLNKLFSLREDFPRQL; LNKLFSLREDFPRQLF; NKLFSLREDFPRQLFQ; KLFSLREDFPRQLFQG; LFSLREDFPRQLFQGL; FSLREDFPRQLFQGLK; SLREDFPRQLFQGLKG; LREDFPRQLFQGLKGP BK virus, reading frame 3 13 mers: ASEKASTPLLLER; SEKASTPLLLERK; EKASTPLLLERKG; KASTPLLLERKGG; ASTPLLLERKGGG; STPLLLERKGGGR; TPLLLERKGGGRG; PLLLERKGGGRGG; LLLERKGGGRGGL; LLERKGGGRGGLG; LERKGGGRGGLGL; ERKGGGRGGLGLL; RKGGGRGGLGLLY; KGGGRGGLGLLYI; GGGRGGLGLLYII; GGRGGLGLLYIIK; GRGGLGLLYIIKK; RGGLGLLYIIKKK; GGLGLLYIIKKKA; GLGLLYIIKKKAT; LGLLYIIKKKATG; GLLYIIKKKATGR; LLYIIKKKATGRS; LYIIKKKATGRSC; YIIKKKATGRSCL; IIKKKATGRSCLP; IKKKATGRSCLPM; KKKATGRSCLPME; KKATGRSCLPMEC; KATGRSCLPMECS; ATGRSCLPMECSQ; TGRSCLPMECSQT; GRSCLPMECSQTM; RSCLPMECSQTMT; SCLPMECSQTMTS; CLPMECSQTMTSG; LPMECSQTMTSGR; PMECSQTMTSGRK; MECSQTMTSGRKV; ECSQTMTSGRKVH; CSQTMTSGRKVHD; SQTMTSGRKVHDS; QTMTSGRKVHDSQ; TMTSGRKVHDSQG; MTSGRKVHDSQGN; TSGRKVHDSQGNA; SGRKVHDSQGNAA; GRKVHDSQGNAAK; RKVHDSQGNAAKP; PQEGKCMTHREEL; QEGKCMTHREELL; EGKCMTHREELLT; GKCMTHREELLTH; KCMTHREELLTHG; CMTHREELLTHGM; MTHREELLTHGMQ; THREELLTHGMQP; HREELLTHGMQPN; REELLTHGMQPNH; EELLTHGMQPNHD; ELLTHGMQPNHDL; LLTHGMQPNHDLR; LTHGMQPNHDLRK; THGMQPNHDLRKE; HGMQPNHDLRKES; GMQPNHDLRKESA; QTCFASLGILALS; TCFASLGILALSP; CFASLGILALSPV; FASLGILALSPVK; ASLGILALSPVKL; SLGILALSPVKLD; LGILALSPVKLDK; GILALSPVKLDKG; ILALSPVKLDKGH; LALSPVKLDKGHG; ALSPVKLDKGHGS; LSPVKLDKGHGSA; SPVKLDKGHGSAP; PVKLDKGHGSAPA; VKLDKGHGSAPAV; KLDKGHGSAPAVT; LDKGHGSAPAVTT; DKGHGSAPAVTTS; KGHGSAPAVTTSF; GHGSAPAVTTSFS; HGSAPAVTTSFSE; GSAPAVTTSFSES; SAPAVTTSFSESW; NLDWNKKKSSEDF; LDWNKKKSSEDFY; DWNKKKSSEDFYF; WNKKKSSEDFYFY; NKKKSSEDFYFYF; KKKSSEDFYFYFR; KKSSEDFYFYFRA; KSSEDFYFYFRAF; SSEDFYFYFRAFA; SEDFYFYFRAFAG; EDFYFYFRAFAGI; DFYFYFRAFAGIL; RQCRREKQKYHCF; QCRREKQKYHCFT; CRREKQKYHCFTC; RREKQKYHCFTCC; REKQKYHCFTCCK; EKQKYHCFTCCKR; KQKYHCFTCCKRL; QKYHCFTCCKRLC; KYHCFTCCKRLCK; YHCFTCCKRLCKR; HCFTCCKRLCKRL; CFTCCKRLCKRLL; FTCCKRLCKRLLG; TCCKRLCKRLLGK; SLFFCISRFMGAA; LFFCISRFMGAAL; FFCISRFMGAALA; FCISRFMGAALAL; CISRFMGAALALL; ISRFMGAALALLG; SRFMGAALALLGD; RFMGAALALLGDL; FMGAALALLGDLV; MGAALALLGDLVA; GAALALLGDLVAS; AALALLGDLVASV; ALALLGDLVASVS; LALLGDLVASVSE; ALLGDLVASVSEA; LLGDLVASVSEAA; LGDLVASVSEAAA; GDLVASVSEAAAA; DLVASVSEAAAAT; LVASVSEAAAATG; VASVSEAAAATGF; ASVSEAAAATGFS; SVSEAAAATGFSV; VSEAAAATGFSVA; SEAAAATGFSVAE; EAAAATGFSVAEI; AAAATGFSVAEIA; AAATGFSVAEIAA; AATGFSVAEIAAG; ATGFSVAEIAAGE; TGFSVAEIAAGEA; GFSVAEIAAGEAA; FSVAEIAAGEAAA; SVAEIAAGEAAAA; VAEIAAGEAAAAI; AEIAAGEAAAAIE; EIAAGEAAAAIEV; IAAGEAAAAIEVQ; AAGEAAAAIEVQI; AGEAAAAIEVQIA; GEAAAAIEVQIAS; EAAAAIEVQIASL; AAAAIEVQIASLA; AAAIEVQIASLAT; AAIEVQIASLATV; AIEVQIASLATVE; IEVQIASLATVEG; EVQIASLATVEGI; VQIASLATVEGIT; QIASLATVEGITS; IASLATVEGITST; ASLATVEGITSTS; SLATVEGITSTSE; LATVEGITSTSEA; ATVEGITSTSEAI; TVEGITSTSEAIA; VEGITSTSEAIAA; EGITSTSEAIAAI; GITSTSEAIAAIG; ITSTSEAIAAIGL; TSTSEAIAAIGLT; STSEAIAAIGLTP; TSEAIAAIGLTPQ; SEAIAAIGLTPQT; EAIAAIGLTPQTY; AIAAIGLTPQTYA; IAAIGLTPQTYAV; AAIGLTPQTYAVI; AIGLTPQTYAVIA; IGLTPQTYAVIAG; GLTPQTYAVIAGA; LTPQTYAVIAGAP; TPQTYAVIAGAPG; PQTYAVIAGAPGA; QTYAVIAGAPGAI; TYAVIAGAPGAIA; YAVIAGAPGAIAG; AVIAGAPGAIAGF; VIAGAPGAIAGFA; IAGAPGAIAGFAA; AGAPGAIAGFAAL; GAPGAIAGFAALI; APGAIAGFAALIQ; PGAIAGFAALIQT; GAIAGFAALIQTV; AIAGFAALIQTVS; IAGFAALIQTVSG; AGFAALIQTVSGI; GFAALIQTVSGIS; FAALIQTVSGISS; AALIQTVSGISSL; ALIQTVSGISSLA; LIQTVSGISSLAQ; IQTVSGISSLAQV; QTVSGISSLAQVG; TVSGISSLAQVGY; VSGISSLAQVGYK; SGISSLAQVGYKF; GISSLAQVGYKFF; ISSLAQVGYKFFD; SSLAQVGYKFFDD; SLAQVGYKFFDDW; LAQVGYKFFDDWD; AQVGYKFFDDWDH; QVGYKFFDDWDHK; VGYKFFDDWDHKV; GYKFFDDWDHKVS; YKFFDDWDHKVST; KFFDDWDHKVSTV; FFDDWDHKVSTVG; FDDWDHKVSTVGL; DDWDHKVSTVGLY; DWDHKVSTVGLYQ; WDHKVSTVGLYQQ; DHKVSTVGLYQQS; HKVSTVGLYQQSG; KVSTVGLYQQSGM; VSTVGLYQQSGMA; STVGLYQQSGMAL; TVGLYQQSGMALE; VGLYQQSGMALEL; GLYQQSGMALELF; LYQQSGMALELFN; YQQSGMALELFNP; QQSGMALELFNPD; QSGMALELFNPDE; SGMALELFNPDEY; GMALELFNPDEYY; MALELFNPDEYYD; ALELFNPDEYYDI; LELFNPDEYYDIL; ELFNPDEYYDILF; LFNPDEYYDILFP; FNPDEYYDILFPG; NPDEYYDILFPGV; PDEYYDILFPGVN; DEYYDILFPGVNT; EYYDILFPGVNTF; YYDILFPGVNTFV; YDILFPGVNTFVN; DILFPGVNTFVNN; ILFPGVNTFVNNI; LFPGVNTFVNNIQ; FPGVNTFVNNIQY; PGVNTFVNNIQYL; GVNTFVNNIQYLD; VNTFVNNIQYLDP; NTFVNNIQYLDPR; TFVNNIQYLDPRH; FVNNIQYLDPRHW; VNNIQYLDPRHWG; NNIQYLDPRHWGP; NIQYLDPRHWGPS; IQYLDPRHWGPSL; QYLDPRHWGPSLF; YLDPRHWGPSLFA; LDPRHWGPSLFAT; DPRHWGPSLFATI; PRHWGPSLFATIS; RHWGPSLFATISQ; HWGPSLFATISQA; WGPSLFATISQAL; GPSLFATISQALW; PSLFATISQALWH; SLFATISQALWHV; LFATISQALWHVI; FATISQALWHVIR; ATISQALWHVIRD; TISQALWHVIRDD; ISQALWHVIRDDI; SQALWHVIRDDIP; QALWHVIRDDIPS; ALWHVIRDDIPSI; LWHVIRDDIPSIT; WHVIRDDIPSITS; HVIRDDIPSITSQ; VIRDDIPSITSQE; IRDDIPSITSQEL; RDDIPSITSQELQ; DDIPSITSQELQR; DIPSITSQELQRR; IPSITSQELQRRT; PSITSQELQRRTE; SITSQELQRRTER; ITSQELQRRTERF; TSQELQRRTERFF; SQELQRRTERFFR; QELQRRTERFFRD; ELQRRTERFFRDS; LQRRTERFFRDSL; QRRTERFFRDSLA; RRTERFFRDSLAR; RTERFFRDSLARF; TERFFRDSLARFL; ERFFRDSLARFLE; RFFRDSLARFLEE; FFRDSLARFLEET; FRDSLARFLEETT; RDSLARFLEETTW; DSLARFLEETTWT; SLARFLEETTWTI; LARFLEETTWTIV; ARFLEETTWTIVN; RFLEETTWTIVNA; FLEETTWTIVNAP; LEETTWTIVNAPI; EETTWTIVNAPIN; ETTWTIVNAPINF; TTWTIVNAPINFY; TWTIVNAPINFYN; WTIVNAPINFYNY; TIVNAPINFYNYI; IVNAPINFYNYIQ; VNAPINFYNYIQQ; NAPINFYNYIQQY; APINFYNYIQQYY; PINFYNYIQQYYS; INFYNYIQQYYSD; NFYNYIQQYYSDL; FYNYIQQYYSDLS; YNYIQQYYSDLSP; NYIQQYYSDLSPI; YIQQYYSDLSPIR; IQQYYSDLSPIRP; QQYYSDLSPIRPS; QYYSDLSPIRPSM; YYSDLSPIRPSMV; YSDLSPIRPSMVR; SDLSPIRPSMVRQ; DLSPIRPSMVRQV; LSPIRPSMVRQVA; SPIRPSMVRQVAE; PIRPSMVRQVAER; IRPSMVRQVAERE; RPSMVRQVAEREG; PSMVRQVAEREGT; SMVRQVAEREGTR; MVRQVAEREGTRV; VRQVAEREGTRVH; RQVAEREGTRVHF; QVAEREGTRVHFG; VAEREGTRVHFGH; AEREGTRVHFGHT; EREGTRVHFGHTY; REGTRVHFGHTYS; EGTRVHFGHTYSI; GTRVHFGHTYSID; TRVHFGHTYSIDD; RVHFGHTYSIDDA; VHFGHTYSIDDAD; HFGHTYSIDDADS; FGHTYSIDDADSI; GHTYSIDDADSIE; HTYSIDDADSIEE; TYSIDDADSIEEV; YSIDDADSIEEVT; SIDDADSIEEVTQ; IDDADSIEEVTQR; DDADSIEEVTQRM; DADSIEEVTQRMD; ADSIEEVTQRMDL; DSIEEVTQRMDLR; SIEEVTQRMDLRN; IEEVTQRMDLRNQ; EEVTQRMDLRNQQ; EVTQRMDLRNQQS; VTQRMDLRNQQSV; TQRMDLRNQQSVH; QRMDLRNQQSVHS; RMDLRNQQSVHSG; MDLRNQQSVHSGE; DLRNQQSVHSGEF; LRNQQSVHSGEFI; RNQQSVHSGEFIE; NQQSVHSGEFIEK; QQSVHSGEFIEKT; QSVHSGEFIEKTI; SVHSGEFIEKTIA; VHSGEFIEKTIAP; HSGEFIEKTIAPG; SGEFIEKTIAPGG; GEFIEKTIAPGGA; EFIEKTIAPGGAN; FIEKTIAPGGANQ; IEKTIAPGGANQR; EKTIAPGGANQRT; KTIAPGGANQRTA; TIAPGGANQRTAP; IAPGGANQRTAPQ; APGGANQRTAPQW; PGGANQRTAPQWM; GGANQRTAPQWML; GANQRTAPQWMLP; ANQRTAPQWMLPL; NQRTAPQWMLPLL; QRTAPQWMLPLLL; RTAPQWMLPLLLG; TAPQWMLPLLLGL; APQWMLPLLLGLY; PQWMLPLLLGLYG; QWMLPLLLGLYGT; WMLPLLLGLYGTV; MLPLLLGLYGTVT; LPLLLGLYGTVTP; PLLLGLYGTVTPA; LLLGLYGTVTPAL; LLGLYGTVTPALE; LGLYGTVTPALEA; GLYGTVTPALEAY; LYGTVTPALEAYE; YGTVTPALEAYED; GTVTPALEAYEDG; TVTPALEAYEDGP; VTPALEAYEDGPN; TPALEAYEDGPNQ; PALEAYEDGPNQK; ALEAYEDGPNQKK; LEAYEDGPNQKKR; EAYEDGPNQKKRR; AYEDGPNQKKRRV; YEDGPNQKKRRVS; EDGPNQKKRRVSR; DGPNQKKRRVSRG; GPNQKKRRVSRGS; PNQKKRRVSRGSS; NQKKRRVSRGSSQ; QKKRRVSRGSSQK; KKRRVSRGSSQKA; KRRVSRGSSQKAK; RRVSRGSSQKAKG; RVSRGSSQKAKGT; VSRGSSQKAKGTR; SRGSSQKAKGTRA; RGSSQKAKGTRAS; GSSQKAKGTRASA; SSQKAKGTRASAK; SQKAKGTRASAKT; QKAKGTRASAKTT; KAKGTRASAKTTN; AKGTRASAKTTNK; KGTRASAKTTNKR; GTRASAKTTNKRR; TRASAKTTNKRRS; RASAKTTNKRRSR; ASAKTTNKRRSRS; SAKTTNKRRSRSS; AKTTNKRRSRSSR; KTTNKRRSRSSRS; NWGRCYYRGRMLP; WGRCYYRGRMLPK; GRCYYRGRMLPKP; RCYYRGRMLPKPR; CYYRGRMLPKPRN; YYRGRMLPKPRNG; YRGRMLPKPRNGG; RGRMLPKPRNGGS; GRMLPKPRNGGSR; PREKNASLLQHSK; REKNASLLQHSKN; EKNASLLQHSKNS; KNASLLQHSKNSP; NASLLQHSKNSPP; ASLLQHSKNSPPQ; SLLQHSKNSPPQF; LLQHSKNSPPQFK; GPNLWKSTDVGGC; PNLWKSTDVGGCN; NLWKSTDVGGCNC; LWKSTDVGGCNCT; WKSTDVGGCNCTN; KSTDVGGCNCTNR; STDVGGCNCTNRG; TDVGGCNCTNRGY; DVGGCNCTNRGYW; VGGCNCTNRGYWN; GGCNCTNRGYWNN; FPLLCCRWRTLGN; PLLCCRWRTLGNA; LLCCRWRTLGNAG; LCCRWRTLGNAGS; CCRWRTLGNAGSA; CRWRTLGNAGSAN; RWRTLGNAGSANE; WRTLGNAGSANEL; RTLGNAGSANELQ; TLGNAGSANELQV; LGNAGSANELQVK; GNAGSANELQVKV; NAGSANELQVKVP; VFWDFHRRGKCSP; FWDFHRRGKCSPS; WDFHRRGKCSPST; DFHRRGKCSPSTS; FHRRGKCSPSTSC; HRRGKCSPSTSCD; RRGKCSPSTSCDQ; RGKCSPSTSCDQH; GKCSPSTSCDQHS; KCSPSTSCDQHSY; CSPSTSCDQHSYH; SPSTSCDQHSYHS; PSTSCDQHSYHSV; STSCDQHSYHSVA; TSCDQHSYHSVAR; QLWNTTVERPCKI; LWNTTVERPCKIF; DPPEKKICKESLP; PPEKKICKESLPN; PEKKICKESLPNF; EKKICKESLPNFL; KKICKESLPNFLF; KICKESLPNFLFA; ICKESLPNFLFAK; PYKQENPESGWAA; YKQENPESGWAAY; KQENPESGWAAYV; QENPESGWAAYVW; ENPESGWAAYVWY; NPESGWAAYVWYG; PESGWAAYVWYGI; ESGWAAYVWYGIP; SGWAAYVWYGIPG; GWAAYVWYGIPGR; WAAYVWYGIPGRR; AAYVWYGIPGRRG; WHRKTSRGPRYDK; HRKTSRGPRYDKI; RKTSRGPRYDKIY; QTGTIANQNALNR; TGTIANQNALNRC; GTIANQNALNRCF; TIANQNALNRCFY; IANQNALNRCFYC; ANQNALNRCFYCT; NQNALNRCFYCTY; QNALNRCFYCTYT; NALNRCFYCTYTF; ALNRCFYCTYTFN; LNRCFYCTYTFNK; NRCFYCTYTFNKC; RCFYCTYTFNKCC; CFYCTYTFNKCCF; FYCTYTFNKCCFC; YCTYTFNKCCFCI; CTYTFNKCCFCIS; TYTFNKCCFCISH; YTFNKCCFCISHF; NTESLYTNATLDY; TESLYTNATLDYG; ESLYTNATLDYGG; SLYTNATLDYGGL; LYTNATLDYGGLT; YTNATLDYGGLTF; TNATLDYGGLTFG; NATLDYGGLTFGN; ATLDYGGLTFGNL; TLDYGGLTFGNLQ; LDYGGLTFGNLQQ; DYGGLTFGNLQQG; YGGLTFGNLQQGL; GGLTFGNLQQGLK; GLTFGNLQQGLKY; LTFGNLQQGLKYL; TFGNLQQGLKYLR; FGNLQQGLKYLRL; GNLQQGLKYLRLG; NLQQGLKYLRLGK; LQQGLKYLRLGKS; QQGLKYLRLGKSI; QGLKYLRLGKSIV; GLKYLRLGKSIVI; LKYLRLGKSIVIG; KYLRLGKSIVIGI; YLRLGKSIVIGIQ; LRLGKSIVIGIQC; RLGKSIVIGIQCL; LGKSIVIGIQCLI; GKSIVIGIQCLIH; KSIVIGIQCLIHV; SIVIGIQCLIHVQ; IVIGIQCLIHVQS; VIGIQCLIHVQSL; IGIQCLIHVQSLQ; GIQCLIHVQSLQF; IQCLIHVQSLQFL; QCLIHVQSLQFLN; CLIHVQSLQFLNP; LIHVQSLQFLNPL; IHVQSLQFLNPLL; HVQSLQFLNPLLL; YQEYISPCIYYIS; QEYISPCIYYISS; EYISPCIYYISSL; YISPCIYYISSLK; ISPCIYYISSLKK; SPCIYYISSLKKY; PCIYYISSLKKYT; CIYYISSLKKYTY; IYYISSLKKYTYL; YYISSLKKYTYLS; YISSLKKYTYLSQ; ISSLKKYTYLSQN; SSLKKYTYLSQNP; SLKKYTYLSQNPA; LKKYTYLSQNPAF; KKYTYLSQNPAFP; KYTYLSQNPAFPS; YTYLSQNPAFPSI; TYLSQNPAFPSIQ; YLSQNPAFPSIQQ; LSQNPAFPSIQQF; TKLAVATRSFHFV; KLAVATRSFHFVK; LAVATRSFHFVKF; AVATRSFHFVKFF; VATRSFHFVKFFF; ATRSFHFVKFFFQ; TRSFHFVKFFFQV; RSFHFVKFFFQVR; SFHFVKFFFQVRT; FHFVKFFFQVRTL; HFVKFFFQVRTLS; FVKFFFQVRTLSF; VKFFFQVRTLSFV; KFFFQVRTLSFVR; FFFQVRTLSFVRI; FFQVRTLSFVRIF; FQVRTLSFVRIFL; QVRTLSFVRIFLN; VRTLSFVRIFLNI; RTLSFVRIFLNIF; TLSFVRIFLNIFW; LSFVRIFLNIFWA; PSLVEIFGFFCLN; SLVEIFGFFCLNV; LVEIFGFFCLNVS; VEIFGFFCLNVSF; EIFGFFCLNVSFL; IFGFFCLNVSFLN; FGFFCLNVSFLNL; GFFCLNVSFLNLP; HFHLNNLSNCLNC; FHLNNLSNCLNCL; HLNNLSNCLNCLF; LNNLSNCLNCLFH; NNLSNCLNCLFHV; NLSNCLNCLFHVL; LSNCLNCLFHVLK; SNCLNCLFHVLKA; NCLNCLFHVLKAN; CLNCLFHVLKANP; LNCLFHVLKANPL; NCLFHVLKANPLI; CLFHVLKANPLIQ; LFHVLKANPLIQL; FHVLKANPLIQLL; HVLKANPLIQLLS; VLKANPLIQLLSL; LKANPLIQLLSLL; KANPLIQLLSLLH; ANPLIQLLSLLHL; NPLIQLLSLLHLQ; PLIQLLSLLHLQK; LIQLLSLLHLQKQ; IQLLSLLHLQKQP; QLLSLLHLQKQPC; LLSLLHLQKQPCT; LSLLHLQKQPCTD; SLLHLQKQPCTDL; LHLAQRLAFPWVG; HLAQRLAFPWVGL; LAQRLAFPWVGLH; AQRLAFPWVGLHL; QRLAFPWVGLHLR; RLAFPWVGLHLRL; LAFPWVGLHLRLY; AFPWVGLHLRLYH; FPWVGLHLRLYHH; PWVGLHLRLYHHT; WVGLHLRLYHHTN; VGLHLRLYHHTNL; GLHLRLYHHTNLI; LHLRLYHHTNLIT; HLRLYHHTNLITL; LRLYHHTNLITLQ; RLYHHTNLITLQL; LYHHTNLITLQLV; YHHTNLITLQLVL; HHTNLITLQLVLF; HTNLITLQLVLFF; TNLITLQLVLFFH; NLITLQLVLFFHY; LITLQLVLFFHYQ; ITLQLVLFFHYQW; TLQLVLFFHYQWD; LQLVLFFHYQWDL; KQYSAKNQILQNP; QYSAKNQILQNPF; VANSAAKQHLPYI; ANSAAKQHLPYIV; NSAAKQHLPYIVL; SAAKQHLPYIVLV; AAKQHLPYIVLVQ; AKQHLPYIVLVQH; KQHLPYIVLVQHF; QHLPYIVLVQHFH; HLPYIVLVQHFHE; LPYIVLVQHFHEL; PYIVLVQHFHELQ; YIVLVQHFHELQI; IVLVQHFHELQIL; VLVQHFHELQILN; LVQHFHELQILNP; VQHFHELQILNPF; QHFHELQILNPFY; HFHELQILNPFYL; FHELQILNPFYLI; HELQILNPFYLIY; ELQILNPFYLIYD; IFLLAFLPWSYEG; FLLAFLPWSYEGY; LLAFLPWSYEGYL; LAFLPWSYEGYLL; AFLPWSYEGYLLF; FLPWSYEGYLLFF; LKLYLLLADKYFF; KLYLLLADKYFFD; LYLLLADKYFFDF; YLLLADKYFFDFY; LLLADKYFFDFYF; LLADKYFFDFYFL; LADKYFFDFYFLQ; ADKYFFDFYFLQK; SDKAGLFSDTFYT; DKAGLFSDTFYTP; KAGLFSDTFYTPL; AGLFSDTFYTPLH; GLFSDTFYTPLHC; LFSDTFYTPLHCI; FSDTFYTPLHCIE; SDTFYTPLHCIEI; DTFYTPLHCIEIL; TFYTPLHCIEILN; FYTPLHCIEILNT; YTPLHCIEILNTY; TPLHCIEILNTYL; PLHCIEILNTYLI; LHCIEILNTYLII; HCIEILNTYLIIK; CIEILNTYLIIKT; IEILNTYLIIKTH; EILNTYLIIKTHP; ILNTYLIIKTHPH; LNTYLIIKTHPHT; NTYLIIKTHPHTL; TYLIIKTHPHTLS; YLIIKTHPHTLSL; LIIKTHPHTLSLL; IIKTHPHTLSLLH; IKTHPHTLSLLHT; KTHPHTLSLLHTQ; LISKTPALFLQAL; ISKTPALFLQALL; SKTPALFLQALLG; NHAPLSPLECFLL; LQKLYVYVELKRI; GLLPFFFFWVVLS; LLPFFFFWVVLSV; LPFFFFWVVLSVE; PFFFFWVVLSVEN; FFFFWVVLSVENL; FFFWVVLSVENLL; FFWVVLSVENLLL; FWVVLSVENLLLL; WVVLSVENLLLLL; VVLSVENLLLLLH; VLSVENLLLLLHH; LSVENLLLLLHHW; SVENLLLLLHHWQ; VENLLLLLHHWQT; ENLLLLLHHWQTY; NLLLLLHHWQTYL; LLLLLHHWQTYLH; LLLLHHWQTYLHG; LLLHHWQTYLHGK; LLHHWQTYLHGKI; LHHWQTYLHGKIN; HHWQTYLHGKINL; HWQTYLHGKINLH; WQTYLHGKINLHP; QTYLHGKINLHPI; TYLHGKINLHPIF; YLHGKINLHPIFH; RNSTRTPTLLFHR; NSTRTPTLLFHRL; STRTPTLLFHRLA; TRTPTLLFHRLAP; RTPTLLFHRLAPI; TPTLLFHRLAPIK; PTLLFHRLAPIKK; TLLFHRLAPIKKI; LLFHRLAPIKKII; LFHRLAPIKKIIT; GLLIFYYLSKYKL; LLIFYYLSKYKLV; LIFYYLSKYKLVT; IFYYLSKYKLVTL; FYYLSKYKLVTLK; YYLSKYKLVTLKL; ISEGSFSNYLDPP; SEGSFSNYLDPPL; EGSFSNYLDPPLQ; GSFSNYLDPPLQS; SFSNYLDPPLQSF; FSNYLDPPLQSFF; SNYLDPPLQSFFS; AKPLCEAVNAVAI; KPLCEAVNAVAIY; PLCEAVNAVAIYP; LCEAVNAVAIYPN; CEAVNAVAIYPNQ; EAVNAVAIYPNQG; AVNAVAIYPNQGL; VNAVAIYPNQGLF; NAVAIYPNQGLFS; HARAVHRRLFGTN; ARAVHRRLFGTNR; RAVHRRLFGTNRP; AVHRRLFGTNRPF; VHRRLFGTNRPFL; HRRLFGTNRPFLA; RRLFGTNRPFLAV; RLFGTNRPFLAVQ; LFGTNRPFLAVQG; FGTNRPFLAVQGI; GTNRPFLAVQGIW; TNRPFLAVQGIWA; NRPFLAVQGIWAK; RPFLAVQGIWAKR; PFLAVQGIWAKRK; FLAVQGIWAKRKI; LAVQGIWAKRKIS; AVQGIWAKRKIST; VQGIWAKRKISTN; QGIWAKRKISTNL; ATPGSKIRLMSYL; TPGSKIRLMSYLY; PGSKIRLMSYLYI; GSKIRLMSYLYIL; SKIRLMSYLYILL; KIRLMSYLYILLH; IRLMSYLYILLHF; RLMSYLYILLHFF; LMSYLYILLHFFI; MSYLYILLHFFIQ; SYLYILLHFFIQS; YLYILLHFFIQSI; LYILLHFFIQSIH; YILLHFFIQSIHS; ILLHFFIQSIHSL; LLHFFIQSIHSLH; LHFFIQSIHSLHF; HFFIQSIHSLHFI; FFIQSIHSLHFIL; FIQSIHSLHFILV; IQSIHSLHFILVA; QSIHSLHFILVAP; SIHSLHFILVAPF; IHSLHFILVAPFV; HSLHFILVAPFVR; SLHFILVAPFVRV; LHFILVAPFVRVK; HFILVAPFVRVKF; FILVAPFVRVKFL; ILVAPFVRVKFLT 14 mers: ASEKASTPLLLERK; SEKASTPLLLERKG; EKASTPLLLERKGG; KASTPLLLERKGGG; ASTPLLLERKGGGR; STPLLLERKGGGRG; TPLLLERKGGGRGG; PLLLERKGGGRGGL; LLLERKGGGRGGLG; LLERKGGGRGGLGL; LERKGGGRGGLGLL; ERKGGGRGGLGLLY; RKGGGRGGLGLLYI; KGGGRGGLGLLYII; GGGRGGLGLLYIIK; GGRGGLGLLYIIKK; GRGGLGLLYIIKKK; RGGLGLLYIIKKKA; GGLGLLYIIKKKAT; GLGLLYIIKKKATG; LGLLYIIKKKATGR; GLLYIIKKKATGRS; LLYIIKKKATGRSC; LYIIKKKATGRSCL; YIIKKKATGRSCLP; IIKKKATGRSCLPM; IKKKATGRSCLPME; KKKATGRSCLPMEC; KKATGRSCLPMECS; KATGRSCLPMECSQ; ATGRSCLPMECSQT; TGRSCLPMECSQTM; GRSCLPMECSQTMT; RSCLPMECSQTMTS; SCLPMECSQTMTSG; CLPMECSQTMTSGR; LPMECSQTMTSGRK; PMECSQTMTSGRKV; MECSQTMTSGRKVH; ECSQTMTSGRKVHD; CSQTMTSGRKVHDS; SQTMTSGRKVHDSQ; QTMTSGRKVHDSQG; TMTSGRKVHDSQGN; MTSGRKVHDSQGNA; TSGRKVHDSQGNAA; SGRKVHDSQGNAAK; GRKVHDSQGNAAKP; PQEGKCMTHREELL; QEGKCMTHREELLT; EGKCMTHREELLTH; GKCMTHREELLTHG; KCMTHREELLTHGM; CMTHREELLTHGMQ; MTHREELLTHGMQP; THREELLTHGMQPN; HREELLTHGMQPNH; REELLTHGMQPNHD; EELLTHGMQPNHDL; ELLTHGMQPNHDLR; LLTHGMQPNHDLRK; LTHGMQPNHDLRKE; THGMQPNHDLRKES; HGMQPNHDLRKESA; QTCFASLGILALSP; TCFASLGILALSPV; CFASLGILALSPVK; FASLGILALSPVKL; ASLGILALSPVKLD; SLGILALSPVKLDK; LGILALSPVKLDKG; GILALSPVKLDKGH; ILALSPVKLDKGHG; LALSPVKLDKGHGS; ALSPVKLDKGHGSA; LSPVKLDKGHGSAP; SPVKLDKGHGSAPA; PVKLDKGHGSAPAV; VKLDKGHGSAPAVT; KLDKGHGSAPAVTT; LDKGHGSAPAVTTS; DKGHGSAPAVTTSF; KGHGSAPAVTTSFS; GHGSAPAVTTSFSE; HGSAPAVTTSFSES; GSAPAVTTSFSESW; NLDWNKKKSSEDFY; LDWNKKKSSEDFYF; DWNKKKSSEDFYFY; WNKKKSSEDFYFYF; NKKKSSEDFYFYFR; KKKSSEDFYFYFRA; KKSSEDFYFYFRAF; KSSEDFYFYFRAFA; SSEDFYFYFRAFAG; SEDFYFYFRAFAGI; EDFYFYFRAFAGIL; RQCRREKQKYHCFT; QCRREKQKYHCFTC; CRREKQKYHCFTCC; RREKQKYHCFTCCK; REKQKYHCFTCCKR; EKQKYHCFTCCKRL; KQKYHCFTCCKRLC; QKYHCFTCCKRLCK; KYHCFTCCKRLCKR; YHCFTCCKRLCKRL; HCFTCCKRLCKRLL; CFTCCKRLCKRLLG; FTCCKRLCKRLLGK; SLFFCISRFMGAAL; LFFCISRFMGAALA; FFCISRFMGAALAL; FCISRFMGAALALL; CISRFMGAALALLG; ISRFMGAALALLGD; SRFMGAALALLGDL; RFMGAALALLGDLV; FMGAALALLGDLVA; MGAALALLGDLVAS; GAALALLGDLVASV; AALALLGDLVASVS; ALALLGDLVASVSE; LALLGDLVASVSEA; ALLGDLVASVSEAA; LLGDLVASVSEAAA; LGDLVASVSEAAAA; GDLVASVSEAAAAT; DLVASVSEAAAATG; LVASVSEAAAATGF; VASVSEAAAATGFS; ASVSEAAAATGFSV; SVSEAAAATGFSVA; VSEAAAATGFSVAE; SEAAAATGFSVAEI; EAAAATGFSVAEIA; AAAATGFSVAEIAA; AAATGFSVAEIAAG; AATGFSVAEIAAGE; ATGFSVAEIAAGEA; TGFSVAEIAAGEAA; GFSVAEIAAGEAAA; FSVAEIAAGEAAAA; SVAEIAAGEAAAAI; VAEIAAGEAAAAIE; AEIAAGEAAAAIEV; EIAAGEAAAAIEVQ; IAAGEAAAAIEVQI; AAGEAAAAIEVQIA; AGEAAAAIEVQIAS; GEAAAAIEVQIASL; EAAAAIEVQIASLA; AAAAIEVQIASLAT; AAAIEVQIASLATV; AAIEVQIASLATVE; AIEVQIASLATVEG; IEVQIASLATVEGI; EVQIASLATVEGIT; VQIASLATVEGITS; QIASLATVEGITST; IASLATVEGITSTS; ASLATVEGITSTSE; SLATVEGITSTSEA; LATVEGITSTSEAI; ATVEGITSTSEAIA; TVEGITSTSEAIAA; VEGITSTSEAIAAI; EGITSTSEAIAAIG; GITSTSEAIAAIGL; ITSTSEAIAAIGLT; TSTSEAIAAIGLTP; STSEAIAAIGLTPQ; TSEAIAAIGLTPQT; SEAIAAIGLTPQTY; EAIAAIGLTPQTYA; AIAAIGLTPQTYAV; IAAIGLTPQTYAVI; AAIGLTPQTYAVIA; AIGLTPQTYAVIAG; IGLTPQTYAVIAGA; GLTPQTYAVIAGAP; LTPQTYAVIAGAPG; TPQTYAVIAGAPGA; PQTYAVIAGAPGAI; QTYAVIAGAPGAIA; TYAVIAGAPGAIAG; YAVIAGAPGAIAGF; AVIAGAPGAIAGFA; VIAGAPGAIAGFAA; IAGAPGAIAGFAAL; AGAPGAIAGFAALI; GAPGAIAGFAALIQ; APGAIAGFAALIQT; PGAIAGFAALIQTV; GAIAGFAALIQTVS; AIAGFAALIQTVSG; IAGFAALIQTVSGI; AGFAALIQTVSGIS; GFAALIQTVSGISS; FAALIQTVSGISSL; AALIQTVSGISSLA; ALIQTVSGISSLAQ; LIQTVSGISSLAQV; IQTVSGISSLAQVG; QTVSGISSLAQVGY; TVSGISSLAQVGYK; VSGISSLAQVGYKF; SGISSLAQVGYKFF; GISSLAQVGYKFFD; ISSLAQVGYKFFDD; SSLAQVGYKFFDDW; SLAQVGYKFFDDWD; LAQVGYKFFDDWDH; AQVGYKFFDDWDHK; QVGYKFFDDWDHKV; VGYKFFDDWDHKVS; GYKFFDDWDHKVST; YKFFDDWDHKVSTV; KFFDDWDHKVSTVG; FFDDWDHKVSTVGL; FDDWDHKVSTVGLY; DDWDHKVSTVGLYQ; DWDHKVSTVGLYQQ; WDHKVSTVGLYQQS; DHKVSTVGLYQQSG; HKVSTVGLYQQSGM; KVSTVGLYQQSGMA; VSTVGLYQQSGMAL; STVGLYQQSGMALE; TVGLYQQSGMALEL; VGLYQQSGMALELF; GLYQQSGMALELFN; LYQQSGMALELFNP; YQQSGMALELFNPD; QQSGMALELFNPDE; QSGMALELFNPDEY; SGMALELFNPDEYY; GMALELFNPDEYYD; MALELFNPDEYYDI; ALELFNPDEYYDIL; LELFNPDEYYDILF; ELFNPDEYYDILFP; LFNPDEYYDILFPG; FNPDEYYDILFPGV; NPDEYYDILFPGVN; PDEYYDILFPGVNT; DEYYDILFPGVNTF; EYYDILFPGVNTFV; YYDILFPGVNTFVN; YDILFPGVNTFVNN; DILFPGVNTFVNNI; ILFPGVNTFVNNIQ; LFPGVNTFVNNIQY; FPGVNTFVNNIQYL; PGVNTFVNNIQYLD; GVNTFVNNIQYLDP; VNTFVNNIQYLDPR; NTFVNNIQYLDPRH; TFVNNIQYLDPRHW; FVNNIQYLDPRHWG; VNNIQYLDPRHWGP; NNIQYLDPRHWGPS; NIQYLDPRHWGPSL; IQYLDPRHWGPSLF; QYLDPRHWGPSLFA; YLDPRHWGPSLFAT; LDPRHWGPSLFATI; DPRHWGPSLFATIS; PRHWGPSLFATISQ; RHWGPSLFATISQA; HWGPSLFATISQAL; WGPSLFATISQALW; GPSLFATISQALWH; PSLFATISQALWHV; SLFATISQALWHVI; LFATISQALWHVIR; FATISQALWHVIRD; ATISQALWHVIRDD; TISQALWHVIRDDI; ISQALWHVIRDDIP; SQALWHVIRDDIPS; QALWHVIRDDIPSI; ALWHVIRDDIPSIT; LWHVIRDDIPSITS; WHVIRDDIPSITSQ; HVIRDDIPSITSQE; VIRDDIPSITSQEL; IRDDIPSITSQELQ; RDDIPSITSQELQR; DDIPSITSQELQRR; DIPSITSQELQRRT; IPSITSQELQRRTE; PSITSQELQRRTER; SITSQELQRRTERF; ITSQELQRRTERFF; TSQELQRRTERFFR; SQELQRRTERFFRD; QELQRRTERFFRDS; ELQRRTERFFRDSL; LQRRTERFFRDSLA; QRRTERFFRDSLAR; RRTERFFRDSLARF; RTERFFRDSLARFL; TERFFRDSLARFLE; ERFFRDSLARFLEE; RFFRDSLARFLEET; FFRDSLARFLEETT; FRDSLARFLEETTW; RDSLARFLEETTWT; DSLARFLEETTWTI; SLARFLEETTWTIV; LARFLEETTWTIVN; ARFLEETTWTIVNA; RFLEETTWTIVNAP; FLEETTWTIVNAPI; LEETTWTIVNAPIN; EETTWTIVNAPINF; ETTWTIVNAPINFY; TTWTIVNAPINFYN; TWTIVNAPINFYNY; WTIVNAPINFYNYI; TIVNAPINFYNYIQ; IVNAPINFYNYIQQ; VNAPINFYNYIQQY; NAPINFYNYIQQYY; APINFYNYIQQYYS; PINFYNYIQQYYSD; INFYNYIQQYYSDL; NFYNYIQQYYSDLS; FYNYIQQYYSDLSP; YNYIQQYYSDLSPI; NYIQQYYSDLSPIR; YIQQYYSDLSPIRP; IQQYYSDLSPIRPS; QQYYSDLSPIRPSM; QYYSDLSPIRPSMV; YYSDLSPIRPSMVR; YSDLSPIRPSMVRQ; SDLSPIRPSMVRQV; DLSPIRPSMVRQVA; LSPIRPSMVRQVAE; SPIRPSMVRQVAER; PIRPSMVRQVAERE; IRPSMVRQVAEREG; RPSMVRQVAEREGT; PSMVRQVAEREGTR; SMVRQVAEREGTRV; MVRQVAEREGTRVH; VRQVAEREGTRVHF; RQVAEREGTRVHFG; QVAEREGTRVHFGH; VAEREGTRVHFGHT; AEREGTRVHFGHTY; EREGTRVHFGHTYS; REGTRVHFGHTYSI; EGTRVHFGHTYSID; GTRVHFGHTYSIDD; TRVHFGHTYSIDDA; RVHFGHTYSIDDAD; VHFGHTYSIDDADS; HFGHTYSIDDADSI; FGHTYSIDDADSIE; GHTYSIDDADSIEE; HTYSIDDADSIEEV; TYSIDDADSIEEVT; YSIDDADSIEEVTQ; SIDDADSIEEVTQR; IDDADSIEEVTQRM; DDADSIEEVTQRMD; DADSIEEVTQRMDL; ADSIEEVTQRMDLR; DSIEEVTQRMDLRN; SIEEVTQRMDLRNQ; IEEVTQRMDLRNQQ; EEVTQRMDLRNQQS; EVTQRMDLRNQQSV; VTQRMDLRNQQSVH; TQRMDLRNQQSVHS; QRMDLRNQQSVHSG; RMDLRNQQSVHSGE; MDLRNQQSVHSGEF; DLRNQQSVHSGEFI; LRNQQSVHSGEFIE; RNQQSVHSGEFIEK; NQQSVHSGEFIEKT; QQSVHSGEFIEKTI; QSVHSGEFIEKTIA; SVHSGEFIEKTIAP; VHSGEFIEKTIAPG; HSGEFIEKTIAPGG; SGEFIEKTIAPGGA; GEFIEKTIAPGGAN; EFIEKTIAPGGANQ; FIEKTIAPGGANQR; IEKTIAPGGANQRT; EKTIAPGGANQRTA; KTIAPGGANQRTAP; TIAPGGANQRTAPQ; IAPGGANQRTAPQW; APGGANQRTAPQWM; PGGANQRTAPQWML; GGANQRTAPQWMLP; GANQRTAPQWMLPL; ANQRTAPQWMLPLL; NQRTAPQWMLPLLL; QRTAPQWMLPLLLG; RTAPQWMLPLLLGL; TAPQWMLPLLLGLY; APQWMLPLLLGLYG; PQWMLPLLLGLYGT; QWMLPLLLGLYGTV; WMLPLLLGLYGTVT; MLPLLLGLYGTVTP; LPLLLGLYGTVTPA; PLLLGLYGTVTPAL; LLLGLYGTVTPALE; LLGLYGTVTPALEA; LGLYGTVTPALEAY; GLYGTVTPALEAYE; LYGTVTPALEAYED; YGTVTPALEAYEDG; GTVTPALEAYEDGP; TVTPALEAYEDGPN; VTPALEAYEDGPNQ; TPALEAYEDGPNQK; PALEAYEDGPNQKK; ALEAYEDGPNQKKR; LEAYEDGPNQKKRR; EAYEDGPNQKKRRV; AYEDGPNQKKRRVS; YEDGPNQKKRRVSR; EDGPNQKKRRVSRG; DGPNQKKRRVSRGS; GPNQKKRRVSRGSS; PNQKKRRVSRGSSQ; NQKKRRVSRGSSQK; QKKRRVSRGSSQKA; KKRRVSRGSSQKAK; KRRVSRGSSQKAKG; RRVSRGSSQKAKGT; RVSRGSSQKAKGTR; VSRGSSQKAKGTRA; SRGSSQKAKGTRAS; RGSSQKAKGTRASA; GSSQKAKGTRASAK; SSQKAKGTRASAKT; SQKAKGTRASAKTT; QKAKGTRASAKTTN; KAKGTRASAKTTNK; AKGTRASAKTTNKR; KGTRASAKTTNKRR; GTRASAKTTNKRRS; TRASAKTTNKRRSR; RASAKTTNKRRSRS; ASAKTTNKRRSRSS; SAKTTNKRRSRSSR; AKTTNKRRSRSSRS; NWGRCYYRGRMLPK; WGRCYYRGRMLPKP; GRCYYRGRMLPKPR; RCYYRGRMLPKPRN; CYYRGRMLPKPRNG; YYRGRMLPKPRNGG; YRGRMLPKPRNGGS; RGRMLPKPRNGGSR; PREKNASLLQHSKN; REKNASLLQHSKNS; EKNASLLQHSKNSP; KNASLLQHSKNSPP; NASLLQHSKNSPPQ; ASLLQHSKNSPPQF; SLLQHSKNSPPQFK; GPNLWKSTDVGGCN; PNLWKSTDVGGCNC; NLWKSTDVGGCNCT; LWKSTDVGGCNCTN; WKSTDVGGCNCTNR; KSTDVGGCNCTNRG; STDVGGCNCTNRGY; TDVGGCNCTNRGYW; DVGGCNCTNRGYWN; VGGCNCTNRGYWNN; FPLLCCRWRTLGNA; PLLCCRWRTLGNAG; LLCCRWRTLGNAGS; LCCRWRTLGNAGSA; CCRWRTLGNAGSAN; CRWRTLGNAGSANE; RWRTLGNAGSANEL; WRTLGNAGSANELQ; RTLGNAGSANELQV; TLGNAGSANELQVK; LGNAGSANELQVKV; GNAGSANELQVKVP; VFWDFHRRGKCSPS; FWDFHRRGKCSPST; WDFHRRGKCSPSTS; DFHRRGKCSPSTSC; FHRRGKCSPSTSCD; HRRGKCSPSTSCDQ; RRGKCSPSTSCDQH; RGKCSPSTSCDQHS; GKCSPSTSCDQHSY; KCSPSTSCDQHSYH; CSPSTSCDQHSYHS; SPSTSCDQHSYHSV; PSTSCDQHSYHSVA; STSCDQHSYHSVAR; QLWNTTVERPCKIF; DPPEKKICKESLPN; PPEKKICKESLPNF; PEKKICKESLPNFL; EKKICKESLPNFLF; KKICKESLPNFLFA; KICKESLPNFLFAK; PYKQENPESGWAAY; YKQENPESGWAAYV; KQENPESGWAAYVW; QENPESGWAAYVWY; ENPESGWAAYVWYG; NPESGWAAYVWYGI; PESGWAAYVWYGIP; ESGWAAYVWYGIPG; SGWAAYVWYGIPGR; GWAAYVWYGIPGRR; WAAYVWYGIPGRRG; WHRKTSRGPRYDKI; HRKTSRGPRYDKIY; QTGTIANQNALNRC; TGTIANQNALNRCF; GTIANQNALNRCFY; TIANQNALNRCFYC; IANQNALNRCFYCT; ANQNALNRCFYCTY; NQNALNRCFYCTYT; QNALNRCFYCTYTF; NALNRCFYCTYTFN; ALNRCFYCTYTFNK; LNRCFYCTYTFNKC; NRCFYCTYTFNKCC; RCFYCTYTFNKCCF; CFYCTYTFNKCCFC; FYCTYTFNKCCFCI; YCTYTFNKCCFCIS; CTYTFNKCCFCISH; TYTFNKCCFCISHF; NTESLYTNATLDYG; TESLYTNATLDYGG; ESLYTNATLDYGGL; SLYTNATLDYGGLT; LYTNATLDYGGLTF; YTNATLDYGGLTFG; TNATLDYGGLTFGN; NATLDYGGLTFGNL; ATLDYGGLTFGNLQ; TLDYGGLTFGNLQQ; LDYGGLTFGNLQQG; DYGGLTFGNLQQGL; YGGLTFGNLQQGLK; GGLTFGNLQQGLKY; GLTFGNLQQGLKYL; LTFGNLQQGLKYLR; TFGNLQQGLKYLRL; FGNLQQGLKYLRLG; GNLQQGLKYLRLGK; NLQQGLKYLRLGKS; LQQGLKYLRLGKSI; QQGLKYLRLGKSIV; QGLKYLRLGKSIVI; GLKYLRLGKSIVIG; LKYLRLGKSIVIGI; KYLRLGKSIVIGIQ; YLRLGKSIVIGIQC; LRLGKSIVIGIQCL; RLGKSIVIGIQCLI; LGKSIVIGIQCLIH; GKSIVIGIQCLIHV; KSIVIGIQCLIHVQ; SIVIGIQCLIHVQS; IVIGIQCLIHVQSL; VIGIQCLIHVQSLQ; IGIQCLIHVQSLQF; GIQCLIHVQSLQFL; IQCLIHVQSLQFLN; QCLIHVQSLQFLNP; CLIHVQSLQFLNPL; LIHVQSLQFLNPLL; IHVQSLQFLNPLLL; YQEYISPCIYYISS; QEYISPCIYYISSL; EYISPCIYYISSLK; YISPCIYYISSLKK; ISPCIYYISSLKKY; SPCIYYISSLKKYT; PCIYYISSLKKYTY; CIYYISSLKKYTYL; IYYISSLKKYTYLS; YYISSLKKYTYLSQ; YISSLKKYTYLSQN; ISSLKKYTYLSQNP; SSLKKYTYLSQNPA; SLKKYTYLSQNPAF; LKKYTYLSQNPAFP; KKYTYLSQNPAFPS; KYTYLSQNPAFPSI; YTYLSQNPAFPSIQ; TYLSQNPAFPSIQQ; YLSQNPAFPSIQQF; TKLAVATRSFHFVK; KLAVATRSFHFVKF; LAVATRSFHFVKFF; AVATRSFHFVKFFF; VATRSFHFVKFFFQ; ATRSFHFVKFFFQV; TRSFHFVKFFFQVR; RSFHFVKFFFQVRT; SFHFVKFFFQVRTL; FHFVKFFFQVRTLS; HFVKFFFQVRTLSF; FVKFFFQVRTLSFV; VKFFFQVRTLSFVR; KFFFQVRTLSFVRI; FFFQVRTLSFVRIF; FFQVRTLSFVRIFL; FQVRTLSFVRIFLN; QVRTLSFVRIFLNI; VRTLSFVRIFLNIF; RTLSFVRIFLNIFW; TLSFVRIFLNIFWA; PSLVEIFGFFCLNV; SLVEIFGFFCLNVS; LVEIFGFFCLNVSF; VEIFGFFCLNVSFL; EIFGFFCLNVSFLN; IFGFFCLNVSFLNL; FGFFCLNVSFLNLP; HFHLNNLSNCLNCL; FHLNNLSNCLNCLF; HLNNLSNCLNCLFH; LNNLSNCLNCLFHV; NNLSNCLNCLFHVL; NLSNCLNCLFHVLK; LSNCLNCLFHVLKA; SNCLNCLFHVLKAN; NCLNCLFHVLKANP; CLNCLFHVLKANPL; LNCLFHVLKANPLI; NCLFHVLKANPLIQ; CLFHVLKANPLIQL; LFHVLKANPLIQLL; FHVLKANPLIQLLS; HVLKANPLIQLLSL; VLKANPLIQLLSLL; LKANPLIQLLSLLH; KANPLIQLLSLLHL; ANPLIQLLSLLHLQ; NPLIQLLSLLHLQK; PLIQLLSLLHLQKQ; LIQLLSLLHLQKQP; IQLLSLLHLQKQPC; QLLSLLHLQKQPCT; LLSLLHLQKQPCTD; LSLLHLQKQPCTDL; LHLAQRLAFPWVGL; HLAQRLAFPWVGLH; LAQRLAFPWVGLHL; AQRLAFPWVGLHLR; QRLAFPWVGLHLRL; RLAFPWVGLHLRLY; LAFPWVGLHLRLYH; AFPWVGLHLRLYHH; FPWVGLHLRLYHHT; PWVGLHLRLYHHTN; WVGLHLRLYHHTNL; VGLHLRLYHHTNLI; GLHLRLYHHTNLIT; LHLRLYHHTNLITL; HLRLYHHTNLITLQ; LRLYHHTNLITLQL; RLYHHTNLITLQLV; LYHHTNLITLQLVL; YHHTNLITLQLVLF; HHTNLITLQLVLFF; HTNLITLQLVLFFH; TNLITLQLVLFFHY; NLITLQLVLFFHYQ; LITLQLVLFFHYQW; ITLQLVLFFHYQWD; TLQLVLFFHYQWDL; KQYSAKNQILQNPF; VANSAAKQHLPYIV; ANSAAKQHLPYIVL; NSAAKQHLPYIVLV; SAAKQHLPYIVLVQ; AAKQHLPYIVLVQH; AKQHLPYIVLVQHF; KQHLPYIVLVQHFH; QHLPYIVLVQHFHE; HLPYIVLVQHFHEL; LPYIVLVQHFHELQ; PYIVLVQHFHELQI; YIVLVQHFHELQIL; IVLVQHFHELQILN; VLVQHFHELQILNP; LVQHFHELQILNPF; VQHFHELQILNPFY; QHFHELQILNPFYL; HFHELQILNPFYLI; FHELQILNPFYLIY; HELQILNPFYLIYD; IFLLAFLPWSYEGY; FLLAFLPWSYEGYL; LLAFLPWSYEGYLL; LAFLPWSYEGYLLF; AFLPWSYEGYLLFF; LKLYLLLADKYFFD; KLYLLLADKYFFDF; LYLLLADKYFFDFY; YLLLADKYFFDFYF; LLLADKYFFDFYFL; LLADKYFFDFYFLQ; LADKYFFDFYFLQK; SDKAGLFSDTFYTP; DKAGLFSDTFYTPL; KAGLFSDTFYTPLH; AGLFSDTFYTPLHC; GLFSDTFYTPLHCI; LFSDTFYTPLHCIE; FSDTFYTPLHCIEI; SDTFYTPLHCIEIL; DTFYTPLHCIEILN; TFYTPLHCIEILNT; FYTPLHCIEILNTY; YTPLHCIEILNTYL; TPLHCIEILNTYLI; PLHCIEILNTYLII; LHCIEILNTYLIIK; HCIEILNTYLIIKT; CIEILNTYLIIKTH; IEILNTYLIIKTHP; EILNTYLIIKTHPH; ILNTYLIIKTHPHT; LNTYLIIKTHPHTL; NTYLIIKTHPHTLS; TYLIIKTHPHTLSL; YLIIKTHPHTLSLL; LIIKTHPHTLSLLH; IIKTHPHTLSLLHT; IKTHPHTLSLLHTQ; LISKTPALFLQALL; ISKTPALFLQALLG; GLLPFFFFWVVLSV; LLPFFFFWVVLSVE; LPFFFFWVVLSVEN; PFFFFWVVLSVENL; FFFFWVVLSVENLL; FFFWVVLSVENLLL; FFWVVLSVENLLLL; FWVVLSVENLLLLL; WVVLSVENLLLLLH; VVLSVENLLLLLHH; VLSVENLLLLLHHW; LSVENLLLLLHHWQ; SVENLLLLLHHWQT; VENLLLLLHHWQTY; ENLLLLLHHWQTYL; NLLLLLHHWQTYLH; LLLLLHHWQTYLHG; LLLLHHWQTYLHGK; LLLHHWQTYLHGKI; LLHHWQTYLHGKIN; LHHWQTYLHGKINL; HHWQTYLHGKINLH; HWQTYLHGKINLHP; WQTYLHGKINLHPI; QTYLHGKINLHPIF; TYLHGKINLHPIFH; RNSTRTPTLLFHRL; NSTRTPTLLFHRLA; STRTPTLLFHRLAP; TRTPTLLFHRLAPI; RTPTLLFHRLAPIK; TPTLLFHRLAPIKK; PTLLFHRLAPIKKI; TLLFHRLAPIKKII; LLFHRLAPIKKIIT; GLLIFYYLSKYKLV; LLIFYYLSKYKLVT; LIFYYLSKYKLVTL; IFYYLSKYKLVTLK; FYYLSKYKLVTLKL; ISEGSFSNYLDPPL; SEGSFSNYLDPPLQ; EGSFSNYLDPPLQS; GSFSNYLDPPLQSF; SFSNYLDPPLQSFF; FSNYLDPPLQSFFS; AKPLCEAVNAVAIY; KPLCEAVNAVAIYP; PLCEAVNAVAIYPN; LCEAVNAVAIYPNQ; CEAVNAVAIYPNQG; EAVNAVAIYPNQGL; AVNAVAIYPNQGLF; VNAVAIYPNQGLFS; HARAVHRRLFGTNR; ARAVHRRLFGTNRP; RAVHRRLFGTNRPF; AVHRRLFGTNRPFL; VHRRLFGTNRPFLA; HRRLFGTNRPFLAV; RRLFGTNRPFLAVQ; RLFGTNRPFLAVQG; LFGTNRPFLAVQGI; FGTNRPFLAVQGIW; GTNRPFLAVQGIWA; TNRPFLAVQGIWAK; NRPFLAVQGIWAKR; RPFLAVQGIWAKRK; PFLAVQGIWAKRKI; FLAVQGIWAKRKIS; LAVQGIWAKRKIST; AVQGIWAKRKISTN; VQGIWAKRKISTNL; ATPGSKIRLMSYLY; TPGSKIRLMSYLYI; PGSKIRLMSYLYIL; GSKIRLMSYLYILL; SKIRLMSYLYILLH; KIRLMSYLYILLHF; IRLMSYLYILLHFF; RLMSYLYILLHFFI; LMSYLYILLHFFIQ; MSYLYILLHFFIQS; SYLYILLHFFIQSI; YLYILLHFFIQSIH; LYILLHFFIQSIHS; YILLHFFIQSIHSL; ILLHFFIQSIHSLH; LLHFFIQSIHSLHF; LHFFIQSIHSLHFI; HFFIQSIHSLHFIL; FFIQSIHSLHFILV; FIQSIHSLHFILVA; IQSIHSLHFILVAP; QSIHSLHFILVAPF; SIHSLHFILVAPFV; IHSLHFILVAPFVR; HSLHFILVAPFVRV; SLHFILVAPFVRVK; LHFILVAPFVRVKF; HFILVAPFVRVKFL; FILVAPFVRVKFLT 15 mers: ASEKASTPLLLERKG; SEKASTPLLLERKGG; EKASTPLLLERKGGG; KASTPLLLERKGGGR; ASTPLLLERKGGGRG; STPLLLERKGGGRGG; TPLLLERKGGGRGGL; PLLLERKGGGRGGLG; LLLERKGGGRGGLGL; LLERKGGGRGGLGLL; LERKGGGRGGLGLLY; ERKGGGRGGLGLLYI; RKGGGRGGLGLLYII; KGGGRGGLGLLYIIK; GGGRGGLGLLYIIKK; GGRGGLGLLYIIKKK; GRGGLGLLYIIKKKA; RGGLGLLYIIKKKAT; GGLGLLYIIKKKATG; GLGLLYIIKKKATGR; LGLLYIIKKKATGRS; GLLYIIKKKATGRSC; LLYIIKKKATGRSCL; LYIIKKKATGRSCLP; YIIKKKATGRSCLPM; IIKKKATGRSCLPME; IKKKATGRSCLPMEC; KKKATGRSCLPMECS; KKATGRSCLPMECSQ; KATGRSCLPMECSQT; ATGRSCLPMECSQTM; TGRSCLPMECSQTMT; GRSCLPMECSQTMTS; RSCLPMECSQTMTSG; SCLPMECSQTMTSGR; CLPMECSQTMTSGRK; LPMECSQTMTSGRKV; PMECSQTMTSGRKVH; MECSQTMTSGRKVHD; ECSQTMTSGRKVHDS; CSQTMTSGRKVHDSQ; SQTMTSGRKVHDSQG; QTMTSGRKVHDSQGN; TMTSGRKVHDSQGNA; MTSGRKVHDSQGNAA; TSGRKVHDSQGNAAK; SGRKVHDSQGNAAKP; PQEGKCMTHREELLT; QEGKCMTHREELLTH; EGKCMTHREELLTHG; GKCMTHREELLTHGM; KCMTHREELLTHGMQ; CMTHREELLTHGMQP; MTHREELLTHGMQPN; THREELLTHGMQPNH; HREELLTHGMQPNHD; REELLTHGMQPNHDL; EELLTHGMQPNHDLR; ELLTHGMQPNHDLRK; LLTHGMQPNHDLRKE; LTHGMQPNHDLRKES; THGMQPNHDLRKESA; QTCFASLGILALSPV; TCFASLGILALSPVK; CFASLGILALSPVKL; FASLGILALSPVKLD; ASLGILALSPVKLDK; SLGILALSPVKLDKG; LGILALSPVKLDKGH; GILALSPVKLDKGHG; ILALSPVKLDKGHGS; LALSPVKLDKGHGSA; ALSPVKLDKGHGSAP; LSPVKLDKGHGSAPA; SPVKLDKGHGSAPAV; PVKLDKGHGSAPAVT; VKLDKGHGSAPAVTT; KLDKGHGSAPAVTTS; LDKGHGSAPAVTTSF; DKGHGSAPAVTTSFS; KGHGSAPAVTTSFSE; GHGSAPAVTTSFSES; HGSAPAVTTSFSESW; NLDWNKKKSSEDFYF; LDWNKKKSSEDFYFY; DWNKKKSSEDFYFYF; WNKKKSSEDFYFYFR; NKKKSSEDFYFYFRA; KKKSSEDFYFYFRAF; KKSSEDFYFYFRAFA; KSSEDFYFYFRAFAG; SSEDFYFYFRAFAGI; SEDFYFYFRAFAGIL; RQCRREKQKYHCFTC; QCRREKQKYHCFTCC; CRREKQKYHCFTCCK; RREKQKYHCFTCCKR; REKQKYHCFTCCKRL; EKQKYHCFTCCKRLC; KQKYHCFTCCKRLCK; QKYHCFTCCKRLCKR; KYHCFTCCKRLCKRL; YHCFTCCKRLCKRLL; HCFTCCKRLCKRLLG; CFTCCKRLCKRLLGK; SLFFCISRFMGAALA; LFFCISRFMGAALAL; FFCISRFMGAALALL; FCISRFMGAALALLG; CISRFMGAALALLGD; ISRFMGAALALLGDL; SRFMGAALALLGDLV; RFMGAALALLGDLVA; FMGAALALLGDLVAS; MGAALALLGDLVASV; GAALALLGDLVASVS; AALALLGDLVASVSE; ALALLGDLVASVSEA; LALLGDLVASVSEAA; ALLGDLVASVSEAAA; LLGDLVASVSEAAAA; LGDLVASVSEAAAAT; GDLVASVSEAAAATG; DLVASVSEAAAATGF; LVASVSEAAAATGFS; VASVSEAAAATGFSV; ASVSEAAAATGFSVA; SVSEAAAATGFSVAE; VSEAAAATGFSVAEI; SEAAAATGFSVAEIA; EAAAATGFSVAEIAA; AAAATGFSVAEIAAG; AAATGFSVAEIAAGE; AATGFSVAEIAAGEA; ATGFSVAEIAAGEAA; TGFSVAEIAAGEAAA; GFSVAEIAAGEAAAA; FSVAEIAAGEAAAAI; SVAEIAAGEAAAAIE; VAEIAAGEAAAAIEV; AEIAAGEAAAAIEVQ; EIAAGEAAAAIEVQI; IAAGEAAAAIEVQIA; AAGEAAAAIEVQIAS; AGEAAAAIEVQIASL; GEAAAAIEVQIASLA; EAAAAIEVQIASLAT; AAAAIEVQIASLATV; AAAIEVQIASLATVE; AAIEVQIASLATVEG; AIEVQIASLATVEGI; IEVQIASLATVEGIT; EVQIASLATVEGITS; VQIASLATVEGITST; QIASLATVEGITSTS; IASLATVEGITSTSE; ASLATVEGITSTSEA; SLATVEGITSTSEAI; LATVEGITSTSEAIA; ATVEGITSTSEAIAA; TVEGITSTSEAIAAI; VEGITSTSEAIAAIG; EGITSTSEAIAAIGL; GITSTSEAIAAIGLT; ITSTSEAIAAIGLTP; TSTSEAIAAIGLTPQ; STSEAIAAIGLTPQT; TSEAIAAIGLTPQTY; SEAIAAIGLTPQTYA; EAIAAIGLTPQTYAV; AIAAIGLTPQTYAVI; IAAIGLTPQTYAVIA; AAIGLTPQTYAVIAG; AIGLTPQTYAVIAGA; IGLTPQTYAVIAGAP; GLTPQTYAVIAGAPG; LTPQTYAVIAGAPGA; TPQTYAVIAGAPGAI; PQTYAVIAGAPGAIA; QTYAVIAGAPGAIAG; TYAVIAGAPGAIAGF; YAVIAGAPGAIAGFA; AVIAGAPGAIAGFAA; VIAGAPGAIAGFAAL; IAGAPGAIAGFAALI; AGAPGAIAGFAALIQ; GAPGAIAGFAALIQT; APGAIAGFAALIQTV; PGAIAGFAALIQTVS; GAIAGFAALIQTVSG; AIAGFAALIQTVSGI; IAGFAALIQTVSGIS; AGFAALIQTVSGISS; GFAALIQTVSGISSL; FAALIQTVSGISSLA; AALIQTVSGISSLAQ; ALIQTVSGISSLAQV; LIQTVSGISSLAQVG; IQTVSGISSLAQVGY; QTVSGISSLAQVGYK; TVSGISSLAQVGYKF; VSGISSLAQVGYKFF; SGISSLAQVGYKFFD; GISSLAQVGYKFFDD; ISSLAQVGYKFFDDW; SSLAQVGYKFFDDWD; SLAQVGYKFFDDWDH; LAQVGYKFFDDWDHK; AQVGYKFFDDWDHKV; QVGYKFFDDWDHKVS; VGYKFFDDWDHKVST; GYKFFDDWDHKVSTV; YKFFDDWDHKVSTVG; KFFDDWDHKVSTVGL; FFDDWDHKVSTVGLY; FDDWDHKVSTVGLYQ; DDWDHKVSTVGLYQQ; DWDHKVSTVGLYQQS; WDHKVSTVGLYQQSG; DHKVSTVGLYQQSGM; HKVSTVGLYQQSGMA; KVSTVGLYQQSGMAL; VSTVGLYQQSGMALE; STVGLYQQSGMALEL; TVGLYQQSGMALELF; VGLYQQSGMALELFN; GLYQQSGMALELFNP; LYQQSGMALELFNPD; YQQSGMALELFNPDE; QQSGMALELFNPDEY; QSGMALELFNPDEYY; SGMALELFNPDEYYD; GMALELFNPDEYYDI; MALELFNPDEYYDIL; ALELFNPDEYYDILF; LELFNPDEYYDILFP; ELFNPDEYYDILFPG; LFNPDEYYDILFPGV; FNPDEYYDILFPGVN; NPDEYYDILFPGVNT; PDEYYDILFPGVNTF; DEYYDILFPGVNTFV; EYYDILFPGVNTFVN; YYDILFPGVNTFVNN; YDILFPGVNTFVNNI; DILFPGVNTFVNNIQ; ILFPGVNTFVNNIQY; LFPGVNTFVNNIQYL; FPGVNTFVNNIQYLD; PGVNTFVNNIQYLDP; GVNTFVNNIQYLDPR; VNTFVNNIQYLDPRH; NTFVNNIQYLDPRHW; TFVNNIQYLDPRHWG; FVNNIQYLDPRHWGP; VNNIQYLDPRHWGPS; NNIQYLDPRHWGPSL; NIQYLDPRHWGPSLF; IQYLDPRHWGPSLFA; QYLDPRHWGPSLFAT; YLDPRHWGPSLFATI; LDPRHWGPSLFATIS; DPRHWGPSLFATISQ; PRHWGPSLFATISQA; RHWGPSLFATISQAL; HWGPSLFATISQALW; WGPSLFATISQALWH; GPSLFATISQALWHV; PSLFATISQALWHVI; SLFATISQALWHVIR; LFATISQALWHVIRD; FATISQALWHVIRDD; ATISQALWHVIRDDI; TISQALWHVIRDDIP; ISQALWHVIRDDIPS; SQALWHVIRDDIPSI; QALWHVIRDDIPSIT; ALWHVIRDDIPSITS; LWHVIRDDIPSITSQ; WHVIRDDIPSITSQE; HVIRDDIPSITSQEL; VIRDDIPSITSQELQ; IRDDIPSITSQELQR; RDDIPSITSQELQRR; DDIPSITSQELQRRT; DIPSITSQELQRRTE; IPSITSQELQRRTER; PSITSQELQRRTERF; SITSQELQRRTERFF; ITSQELQRRTERFFR; TSQELQRRTERFFRD; SQELQRRTERFFRDS; QELQRRTERFFRDSL; ELQRRTERFFRDSLA; LQRRTERFFRDSLAR; QRRTERFFRDSLARF; RRTERFFRDSLARFL; RTERFFRDSLARFLE; TERFFRDSLARFLEE; ERFFRDSLARFLEET; RFFRDSLARFLEETT; FFRDSLARFLEETTW; FRDSLARFLEETTWT; RDSLARFLEETTWTI; DSLARFLEETTWTIV; SLARFLEETTWTIVN; LARFLEETTWTIVNA; ARFLEETTWTIVNAP; RFLEETTWTIVNAPI; FLEETTWTIVNAPIN; LEETTWTIVNAPINF; EETTWTIVNAPINFY; ETTWTIVNAPINFYN; TTWTIVNAPINFYNY; TWTIVNAPINFYNYI; WTIVNAPINFYNYIQ; TIVNAPINFYNYIQQ; IVNAPINFYNYIQQY; VNAPINFYNYIQQYY; NAPINFYNYIQQYYS; APINFYNYIQQYYSD; PINFYNYIQQYYSDL; INFYNYIQQYYSDLS; NFYNYIQQYYSDLSP; FYNYIQQYYSDLSPI; YNYIQQYYSDLSPIR; NYIQQYYSDLSPIRP; YIQQYYSDLSPIRPS; IQQYYSDLSPIRPSM; QQYYSDLSPIRPSMV; QYYSDLSPIRPSMVR; YYSDLSPIRPSMVRQ; YSDLSPIRPSMVRQV; SDLSPIRPSMVRQVA; DLSPIRPSMVRQVAE; LSPIRPSMVRQVAER; SPIRPSMVRQVAERE; PIRPSMVRQVAEREG; IRPSMVRQVAEREGT; RPSMVRQVAEREGTR; PSMVRQVAEREGTRV; SMVRQVAEREGTRVH; MVRQVAEREGTRVHF; VRQVAEREGTRVHFG; RQVAEREGTRVHFGH; QVAEREGTRVHFGHT; VAEREGTRVHFGHTY; AEREGTRVHFGHTYS; EREGTRVHFGHTYSI; REGTRVHFGHTYSID; EGTRVHFGHTYSIDD; GTRVHFGHTYSIDDA; TRVHFGHTYSIDDAD; RVHFGHTYSIDDADS; VHFGHTYSIDDADSI; HFGHTYSIDDADSIE; FGHTYSIDDADSIEE; GHTYSIDDADSIEEV; HTYSIDDADSIEEVT; TYSIDDADSIEEVTQ; YSIDDADSIEEVTQR; SIDDADSIEEVTQRM; IDDADSIEEVTQRMD; DDADSIEEVTQRMDL; DADSIEEVTQRMDLR; ADSIEEVTQRMDLRN; DSIEEVTQRMDLRNQ; SIEEVTQRMDLRNQQ; IEEVTQRMDLRNQQS; EEVTQRMDLRNQQSV; EVTQRMDLRNQQSVH; VTQRMDLRNQQSVHS; TQRMDLRNQQSVHSG; QRMDLRNQQSVHSGE; RMDLRNQQSVHSGEF; MDLRNQQSVHSGEFI; DLRNQQSVHSGEFIE; LRNQQSVHSGEFIEK; RNQQSVHSGEFIEKT; NQQSVHSGEFIEKTI; QQSVHSGEFIEKTIA; QSVHSGEFIEKTIAP; SVHSGEFIEKTIAPG; VHSGEFIEKTIAPGG; HSGEFIEKTIAPGGA; SGEFIEKTIAPGGAN; GEFIEKTIAPGGANQ; EFIEKTIAPGGANQR; FIEKTIAPGGANQRT; IEKTIAPGGANQRTA; EKTIAPGGANQRTAP; KTIAPGGANQRTAPQ; TIAPGGANQRTAPQW; IAPGGANQRTAPQWM; APGGANQRTAPQWML; PGGANQRTAPQWMLP; GGANQRTAPQWMLPL; GANQRTAPQWMLPLL; ANQRTAPQWMLPLLL; NQRTAPQWMLPLLLG; QRTAPQWMLPLLLGL; RTAPQWMLPLLLGLY; TAPQWMLPLLLGLYG; APQWMLPLLLGLYGT; PQWMLPLLLGLYGTV; QWMLPLLLGLYGTVT; WMLPLLLGLYGTVTP; MLPLLLGLYGTVTPA; LPLLLGLYGTVTPAL; PLLLGLYGTVTPALE; LLLGLYGTVTPALEA; LLGLYGTVTPALEAY; LGLYGTVTPALEAYE; GLYGTVTPALEAYED; LYGTVTPALEAYEDG; YGTVTPALEAYEDGP; GTVTPALEAYEDGPN; TVTPALEAYEDGPNQ; VTPALEAYEDGPNQK; TPALEAYEDGPNQKK; PALEAYEDGPNQKKR; ALEAYEDGPNQKKRR; LEAYEDGPNQKKRRV; EAYEDGPNQKKRRVS; AYEDGPNQKKRRVSR; YEDGPNQKKRRVSRG; EDGPNQKKRRVSRGS; DGPNQKKRRVSRGSS; GPNQKKRRVSRGSSQ; PNQKKRRVSRGSSQK; NQKKRRVSRGSSQKA; QKKRRVSRGSSQKAK; KKRRVSRGSSQKAKG; KRRVSRGSSQKAKGT; RRVSRGSSQKAKGTR; RVSRGSSQKAKGTRA; VSRGSSQKAKGTRAS; SRGSSQKAKGTRASA; RGSSQKAKGTRASAK; GSSQKAKGTRASAKT; SSQKAKGTRASAKTT; SQKAKGTRASAKTTN; QKAKGTRASAKTTNK; KAKGTRASAKTTNKR; AKGTRASAKTTNKRR; KGTRASAKTTNKRRS; GTRASAKTTNKRRSR; TRASAKTTNKRRSRS; RASAKTTNKRRSRSS; ASAKTTNKRRSRSSR; SAKTTNKRRSRSSRS; NWGRCYYRGRMLPKP; WGRCYYRGRMLPKPR; GRCYYRGRMLPKPRN; RCYYRGRMLPKPRNG; CYYRGRMLPKPRNGG; YYRGRMLPKPRNGGS; YRGRMLPKPRNGGSR; PREKNASLLQHSKNS; REKNASLLQHSKNSP; EKNASLLQHSKNSPP; KNASLLQHSKNSPPQ; NASLLQHSKNSPPQF; ASLLQHSKNSPPQFK; GPNLWKSTDVGGCNC; PNLWKSTDVGGCNCT; NLWKSTDVGGCNCTN; LWKSTDVGGCNCTNR; WKSTDVGGCNCTNRG; KSTDVGGCNCTNRGY; STDVGGCNCTNRGYW; TDVGGCNCTNRGYWN; DVGGCNCTNRGYWNN; FPLLCCRWRTLGNAG; PLLCCRWRTLGNAGS; LLCCRWRTLGNAGSA; LCCRWRTLGNAGSAN; CCRWRTLGNAGSANE; CRWRTLGNAGSANEL; RWRTLGNAGSANELQ; WRTLGNAGSANELQV; RTLGNAGSANELQVK; TLGNAGSANELQVKV; LGNAGSANELQVKVP; VFWDFHRRGKCSPST; FWDFHRRGKCSPSTS; WDFHRRGKCSPSTSC; DFHRRGKCSPSTSCD; FHRRGKCSPSTSCDQ; HRRGKCSPSTSCDQH; RRGKCSPSTSCDQHS; RGKCSPSTSCDQHSY; GKCSPSTSCDQHSYH; KCSPSTSCDQHSYHS; CSPSTSCDQHSYHSV; SPSTSCDQHSYHSVA; PSTSCDQHSYHSVAR; DPPEKKICKESLPNF; PPEKKICKESLPNFL; PEKKICKESLPNFLF; EKKICKESLPNFLFA; KKICKESLPNFLFAK; PYKQENPESGWAAYV; YKQENPESGWAAYVW; KQENPESGWAAYVWY; QENPESGWAAYVWYG; ENPESGWAAYVWYGI; NPESGWAAYVWYGIP; PESGWAAYVWYGIPG; ESGWAAYVWYGIPGR; SGWAAYVWYGIPGRR; GWAAYVWYGIPGRRG; WHRKTSRGPRYDKIY; QTGTIANQNALNRCF; TGTIANQNALNRCFY; GTIANQNALNRCFYC; TIANQNALNRCFYCT; IANQNALNRCFYCTY; ANQNALNRCFYCTYT; NQNALNRCFYCTYTF; QNALNRCFYCTYTFN; NALNRCFYCTYTFNK; ALNRCFYCTYTFNKC; LNRCFYCTYTFNKCC; NRCFYCTYTFNKCCF; RCFYCTYTFNKCCFC; CFYCTYTFNKCCFCI; FYCTYTFNKCCFCIS; YCTYTFNKCCFCISH; CTYTFNKCCFCISHF; NTESLYTNATLDYGG; TESLYTNATLDYGGL; ESLYTNATLDYGGLT; SLYTNATLDYGGLTF; LYTNATLDYGGLTFG; YTNATLDYGGLTFGN; TNATLDYGGLTFGNL; NATLDYGGLTFGNLQ; ATLDYGGLTFGNLQQ; TLDYGGLTFGNLQQG; LDYGGLTFGNLQQGL; DYGGLTFGNLQQGLK; YGGLTFGNLQQGLKY; GGLTFGNLQQGLKYL; GLTFGNLQQGLKYLR; LTFGNLQQGLKYLRL; TFGNLQQGLKYLRLG; FGNLQQGLKYLRLGK; GNLQQGLKYLRLGKS; NLQQGLKYLRLGKSI; LQQGLKYLRLGKSIV; QQGLKYLRLGKSIVI; QGLKYLRLGKSIVIG; GLKYLRLGKSIVIGI; LKYLRLGKSIVIGIQ; KYLRLGKSIVIGIQC; YLRLGKSIVIGIQCL; LRLGKSIVIGIQCLI; RLGKSIVIGIQCLIH; LGKSIVIGIQCLIHV; GKSIVIGIQCLIHVQ; KSIVIGIQCLIHVQS; SIVIGIQCLIHVQSL; IVIGIQCLIHVQSLQ; VIGIQCLIHVQSLQF; IGIQCLIHVQSLQFL; GIQCLIHVQSLQFLN; IQCLIHVQSLQFLNP; QCLIHVQSLQFLNPL; CLIHVQSLQFLNPLL; LIHVQSLQFLNPLLL; YQEYISPCIYYISSL; QEYISPCIYYISSLK; EYISPCIYYISSLKK; YISPCIYYISSLKKY; ISPCIYYISSLKKYT; SPCIYYISSLKKYTY; PCIYYISSLKKYTYL; CIYYISSLKKYTYLS; IYYISSLKKYTYLSQ; YYISSLKKYTYLSQN; YISSLKKYTYLSQNP; ISSLKKYTYLSQNPA; SSLKKYTYLSQNPAF; SLKKYTYLSQNPAFP; LKKYTYLSQNPAFPS; KKYTYLSQNPAFPSI; KYTYLSQNPAFPSIQ; YTYLSQNPAFPSIQQ; TYLSQNPAFPSIQQF; TKLAVATRSFHFVKF; KLAVATRSFHFVKFF; LAVATRSFHFVKFFF; AVATRSFHFVKFFFQ; VATRSFHFVKFFFQV; ATRSFHFVKFFFQVR; TRSFHFVKFFFQVRT; RSFHFVKFFFQVRTL; SFHFVKFFFQVRTLS; FHFVKFFFQVRTLSF; HFVKFFFQVRTLSFV; FVKFFFQVRTLSFVR; VKFFFQVRTLSFVRI; KFFFQVRTLSFVRIF; FFFQVRTLSFVRIFL; FFQVRTLSFVRIFLN; FQVRTLSFVRIFLNI; QVRTLSFVRIFLNIF; VRTLSFVRIFLNIFW; RTLSFVRIFLNIFWA; PSLVEIFGFFCLNVS; SLVEIFGFFCLNVSF; LVEIFGFFCLNVSFL; VEIFGFFCLNVSFLN; EIFGFFCLNVSFLNL; IFGFFCLNVSFLNLP; HFHLNNLSNCLNCLF; FHLNNLSNCLNCLFH; HLNNLSNCLNCLFHV; LNNLSNCLNCLFHVL; NNLSNCLNCLFHVLK; NLSNCLNCLFHVLKA; LSNCLNCLFHVLKAN; SNCLNCLFHVLKANP; NCLNCLFHVLKANPL; CLNCLFHVLKANPLI; LNCLFHVLKANPLIQ; NCLFHVLKANPLIQL; CLFHVLKANPLIQLL; LFHVLKANPLIQLLS; FHVLKANPLIQLLSL; HVLKANPLIQLLSLL; VLKANPLIQLLSLLH; LKANPLIQLLSLLHL; KANPLIQLLSLLHLQ; ANPLIQLLSLLHLQK; NPLIQLLSLLHLQKQ; PLIQLLSLLHLQKQP; LIQLLSLLHLQKQPC; IQLLSLLHLQKQPCT; QLLSLLHLQKQPCTD; LLSLLHLQKQPCTDL; LHLAQRLAFPWVGLH; HLAQRLAFPWVGLHL; LAQRLAFPWVGLHLR; AQRLAFPWVGLHLRL; QRLAFPWVGLHLRLY; RLAFPWVGLHLRLYH; LAFPWVGLHLRLYHH; AFPWVGLHLRLYHHT; FPWVGLHLRLYHHTN; PWVGLHLRLYHHTNL; WVGLHLRLYHHTNLI; VGLHLRLYHHTNLIT; GLHLRLYHHTNLITL; LHLRLYHHTNLITLQ; HLRLYHHTNLITLQL; LRLYHHTNLITLQLV; RLYHHTNLITLQLVL; LYHHTNLITLQLVLF; YHHTNLITLQLVLFF; HHTNLITLQLVLFFH; HTNLITLQLVLFFHY; TNLITLQLVLFFHYQ; NLITLQLVLFFHYQW; LITLQLVLFFHYQWD; ITLQLVLFFHYQWDL; VANSAAKQHLPYIVL; ANSAAKQHLPYIVLV; NSAAKQHLPYIVLVQ; SAAKQHLPYIVLVQH; AAKQHLPYIVLVQHF; AKQHLPYIVLVQHFH; KQHLPYIVLVQHFHE; QHLPYIVLVQHFHEL; HLPYIVLVQHFHELQ; LPYIVLVQHFHELQI; PYIVLVQHFHELQIL; YIVLVQHFHELQILN; IVLVQHFHELQILNP; VLVQHFHELQILNPF; LVQHFHELQILNPFY; VQHFHELQILNPFYL; QHFHELQILNPFYLI; HFHELQILNPFYLIY; FHELQILNPFYLIYD; IFLLAFLPWSYEGYL; FLLAFLPWSYEGYLL; LLAFLPWSYEGYLLF; LAFLPWSYEGYLLFF; LKLYLLLADKYFFDF; KLYLLLADKYFFDFY; LYLLLADKYFFDFYF; YLLLADKYFFDFYFL; LLLADKYFFDFYFLQ; LLADKYFFDFYFLQK; SDKAGLFSDTFYTPL; DKAGLFSDTFYTPLH; KAGLFSDTFYTPLHC; AGLFSDTFYTPLHCI; GLFSDTFYTPLHCIE; LFSDTFYTPLHCIEI; FSDTFYTPLHCIEIL; SDTFYTPLHCIEILN; DTFYTPLHCIEILNT; TFYTPLHCIEILNTY; FYTPLHCIEILNTYL; YTPLHCIEILNTYLI; TPLHCIEILNTYLII; PLHCIEILNTYLIIK; LHCIEILNTYLIIKT; HCIEILNTYLIIKTH; CIEILNTYLIIKTHP; IEILNTYLIIKTHPH; EILNTYLIIKTHPHT; ILNTYLIIKTHPHTL; LNTYLIIKTHPHTLS; NTYLIIKTHPHTLSL; TYLIIKTHPHTLSLL; YLIIKTHPHTLSLLH; LIIKTHPHTLSLLHT; IIKTHPHTLSLLHTQ; LISKTPALFLQALLG; GLLPFFFFWVVLSVE; LLPFFFFWVVLSVEN; LPFFFFWVVLSVENL; PFFFFWVVLSVENLL; FFFFWVVLSVENLLL; FFFWVVLSVENLLLL; FFWVVLSVENLLLLL; FWVVLSVENLLLLLH; WVVLSVENLLLLLHH; VVLSVENLLLLLHHW; VLSVENLLLLLHHWQ; LSVENLLLLLHHWQT; SVENLLLLLHHWQTY; VENLLLLLHHWQTYL; ENLLLLLHHWQTYLH; NLLLLLHHWQTYLHG; LLLLLHHWQTYLHGK; LLLLHHWQTYLHGKI; LLLHHWQTYLHGKIN; LLHHWQTYLHGKINL; LHHWQTYLHGKINLH; HHWQTYLHGKINLHP; HWQTYLHGKINLHPI; WQTYLHGKINLHPIF; QTYLHGKINLHPIFH; RNSTRTPTLLFHRLA; NSTRTPTLLFHRLAP; STRTPTLLFHRLAPI; TRTPTLLFHRLAPIK; RTPTLLFHRLAPIKK; TPTLLFHRLAPIKKI; PTLLFHRLAPIKKII; TLLFHRLAPIKKIIT; GLLIFYYLSKYKLVT; LLIFYYLSKYKLVTL; LIFYYLSKYKLVTLK; IFYYLSKYKLVTLKL; ISEGSFSNYLDPPLQ; SEGSFSNYLDPPLQS; EGSFSNYLDPPLQSF; GSFSNYLDPPLQSFF; SFSNYLDPPLQSFFS; AKPLCEAVNAVAIYP; KPLCEAVNAVAIYPN; PLCEAVNAVAIYPNQ; LCEAVNAVAIYPNQG; CEAVNAVAIYPNQGL; EAVNAVAIYPNQGLF; AVNAVAIYPNQGLFS; HARAVHRRLFGTNRP; ARAVHRRLFGTNRPF; RAVHRRLFGTNRPFL; AVHRRLFGTNRPFLA; VHRRLFGTNRPFLAV; HRRLFGTNRPFLAVQ; RRLFGTNRPFLAVQG; RLFGTNRPFLAVQGI; LFGTNRPFLAVQGIW; FGTNRPFLAVQGIWA; GTNRPFLAVQGIWAK; TNRPFLAVQGIWAKR; NRPFLAVQGIWAKRK; RPFLAVQGIWAKRKI; PFLAVQGIWAKRKIS; FLAVQGIWAKRKIST; LAVQGIWAKRKISTN; AVQGIWAKRKISTNL; ATPGSKIRLMSYLYI; TPGSKIRLMSYLYIL; PGSKIRLMSYLYILL; GSKIRLMSYLYILLH; SKIRLMSYLYILLHF; KIRLMSYLYILLHFF; IRLMSYLYILLHFFI; RLMSYLYILLHFFIQ; LMSYLYILLHFFIQS; MSYLYILLHFFIQSI; SYLYILLHFFIQSIH; YLYILLHFFIQSIHS; LYILLHFFIQSIHSL; YILLHFFIQSIHSLH; ILLHFFIQSIHSLHF; LLHFFIQSIHSLHFI; LHFFIQSIHSLHFIL; HFFIQSIHSLHFILV; FFIQSIHSLHFILVA; FIQSIHSLHFILVAP; IQSIHSLHFILVAPF; QSIHSLHFILVAPFV; SIHSLHFILVAPFVR; IHSLHFILVAPFVRV; HSLHFILVAPFVRVK; SLHFILVAPFVRVKF; LHFILVAPFVRVKFL; HFILVAPFVRVKFLT; KVHELHGFFPVKNFI; VHELHGFFPVKNFIH 16 mers: ASEKASTPLLLERKGG; SEKASTPLLLERKGGG; EKASTPLLLERKGGGR; KASTPLLLERKGGGRG; ASTPLLLERKGGGRGG; STPLLLERKGGGRGGL; TPLLLERKGGGRGGLG; PLLLERKGGGRGGLGL; LLLERKGGGRGGLGLL; LLERKGGGRGGLGLLY; LERKGGGRGGLGLLYI; ERKGGGRGGLGLLYII; RKGGGRGGLGLLYIIK; KGGGRGGLGLLYIIKK; GGGRGGLGLLYIIKKK; GGRGGLGLLYIIKKKA; GRGGLGLLYIIKKKAT; RGGLGLLYIIKKKATG; GGLGLLYIIKKKATGR; GLGLLYIIKKKATGRS; LGLLYIIKKKATGRSC; GLLYIIKKKATGRSCL; LLYIIKKKATGRSCLP; LYIIKKKATGRSCLPM; YIIKKKATGRSCLPME; IIKKKATGRSCLPMEC; IKKKATGRSCLPMECS; KKKATGRSCLPMECSQ; KKATGRSCLPMECSQT; KATGRSCLPMECSQTM; ATGRSCLPMECSQTMT; TGRSCLPMECSQTMTS; GRSCLPMECSQTMTSG; RSCLPMECSQTMTSGR; SCLPMECSQTMTSGRK; CLPMECSQTMTSGRKV; LPMECSQTMTSGRKVH; PMECSQTMTSGRKVHD; MECSQTMTSGRKVHDS; ECSQTMTSGRKVHDSQ; CSQTMTSGRKVHDSQG; SQTMTSGRKVHDSQGN; QTMTSGRKVHDSQGNA; TMTSGRKVHDSQGNAA; MTSGRKVHDSQGNAAK; TSGRKVHDSQGNAAKP; PQEGKCMTHREELLTH; QEGKCMTHREELLTHG; EGKCMTHREELLTHGM; GKCMTHREELLTHGMQ; KCMTHREELLTHGMQP; CMTHREELLTHGMQPN; MTHREELLTHGMQPNH; THREELLTHGMQPNHD; HREELLTHGMQPNHDL; REELLTHGMQPNHDLR; EELLTHGMQPNHDLRK; ELLTHGMQPNHDLRKE; LLTHGMQPNHDLRKES; LTHGMQPNHDLRKESA; QTCFASLGILALSPVK; TCFASLGILALSPVKL; CFASLGILALSPVKLD; FASLGILALSPVKLDK; ASLGILALSPVKLDKG; SLGILALSPVKLDKGH; LGILALSPVKLDKGHG; GILALSPVKLDKGHGS; ILALSPVKLDKGHGSA; LALSPVKLDKGHGSAP; ALSPVKLDKGHGSAPA; LSPVKLDKGHGSAPAV; SPVKLDKGHGSAPAVT; PVKLDKGHGSAPAVTT; VKLDKGHGSAPAVTTS; KLDKGHGSAPAVTTSF; LDKGHGSAPAVTTSFS; DKGHGSAPAVTTSFSE; KGHGSAPAVTTSFSES; GHGSAPAVTTSFSESW; NLDWNKKKSSEDFYFY; LDWNKKKSSEDFYFYF; DWNKKKSSEDFYFYFR; WNKKKSSEDFYFYFRA; NKKKSSEDFYFYFRAF; KKKSSEDFYFYFRAFA; KKSSEDFYFYFRAFAG; KSSEDFYFYFRAFAGI; SSEDFYFYFRAFAGIL; RQCRREKQKYHCFTCC; QCRREKQKYHCFTCCK; CRREKQKYHCFTCCKR; RREKQKYHCFTCCKRL; REKQKYHCFTCCKRLC; EKQKYHCFTCCKRLCK; KQKYHCFTCCKRLCKR; QKYHCFTCCKRLCKRL; KYHCFTCCKRLCKRLL; YHCFTCCKRLCKRLLG; HCFTCCKRLCKRLLGK; SLFFCISRFMGAALAL; LFFCISRFMGAALALL; FFCISRFMGAALALLG; FCISRFMGAALALLGD; CISRFMGAALALLGDL; ISRFMGAALALLGDLV; SRFMGAALALLGDLVA; RFMGAALALLGDLVAS; FMGAALALLGDLVASV; MGAALALLGDLVASVS; GAALALLGDLVASVSE; AALALLGDLVASVSEA; ALALLGDLVASVSEAA; LALLGDLVASVSEAAA; ALLGDLVASVSEAAAA; LLGDLVASVSEAAAAT; LGDLVASVSEAAAATG; GDLVASVSEAAAATGF; DLVASVSEAAAATGFS; LVASVSEAAAATGFSV; VASVSEAAAATGFSVA; ASVSEAAAATGFSVAE; SVSEAAAATGFSVAEI; VSEAAAATGFSVAEIA; SEAAAATGFSVAEIAA; EAAAATGFSVAEIAAG; AAAATGFSVAEIAAGE; AAATGFSVAEIAAGEA; AATGFSVAEIAAGEAA; ATGFSVAEIAAGEAAA; TGFSVAEIAAGEAAAA; GFSVAEIAAGEAAAAI; FSVAEIAAGEAAAAIE; SVAEIAAGEAAAAIEV; VAEIAAGEAAAAIEVQ; AEIAAGEAAAAIEVQI; EIAAGEAAAAIEVQIA; IAAGEAAAAIEVQIAS; AAGEAAAAIEVQIASL; AGEAAAAIEVQIASLA; GEAAAAIEVQIASLAT; EAAAAIEVQIASLATV; AAAAIEVQIASLATVE; AAAIEVQIASLATVEG; AAIEVQIASLATVEGI; AIEVQIASLATVEGIT; IEVQIASLATVEGITS; EVQIASLATVEGITST; VQIASLATVEGITSTS; QIASLATVEGITSTSE; IASLATVEGITSTSEA; ASLATVEGITSTSEAI; SLATVEGITSTSEAIA; LATVEGITSTSEAIAA; ATVEGITSTSEAIAAI; TVEGITSTSEAIAAIG; VEGITSTSEAIAAIGL; EGITSTSEAIAAIGLT; GITSTSEAIAAIGLTP; ITSTSEAIAAIGLTPQ; TSTSEAIAAIGLTPQT; STSEAIAAIGLTPQTY; TSEAIAAIGLTPQTYA; SEAIAAIGLTPQTYAV; EAIAAIGLTPQTYAVI; AIAAIGLTPQTYAVIA; IAAIGLTPQTYAVIAG; AAIGLTPQTYAVIAGA; AIGLTPQTYAVIAGAP; IGLTPQTYAVIAGAPG; GLTPQTYAVIAGAPGA; LTPQTYAVIAGAPGAI; TPQTYAVIAGAPGAIA; PQTYAVIAGAPGAIAG; QTYAVIAGAPGAIAGF; TYAVIAGAPGAIAGFA; YAVIAGAPGAIAGFAA; AVIAGAPGAIAGFAAL; VIAGAPGAIAGFAALI; IAGAPGAIAGFAALIQ; AGAPGAIAGFAALIQT; GAPGAIAGFAALIQTV; APGAIAGFAALIQTVS; PGAIAGFAALIQTVSG; GAIAGFAALIQTVSGI; AIAGFAALIQTVSGIS; IAGFAALIQTVSGISS; AGFAALIQTVSGISSL; GFAALIQTVSGISSLA; FAALIQTVSGISSLAQ; AALIQTVSGISSLAQV; ALIQTVSGISSLAQVG; LIQTVSGISSLAQVGY; IQTVSGISSLAQVGYK; QTVSGISSLAQVGYKF; TVSGISSLAQVGYKFF; VSGISSLAQVGYKFFD; SGISSLAQVGYKFFDD; GISSLAQVGYKFFDDW; ISSLAQVGYKFFDDWD; SSLAQVGYKFFDDWDH; SLAQVGYKFFDDWDHK; LAQVGYKFFDDWDHKV; AQVGYKFFDDWDHKVS; QVGYKFFDDWDHKVST; VGYKFFDDWDHKVSTV; GYKFFDDWDHKVSTVG; YKFFDDWDHKVSTVGL; KFFDDWDHKVSTVGLY; FFDDWDHKVSTVGLYQ; FDDWDHKVSTVGLYQQ; DDWDHKVSTVGLYQQS; DWDHKVSTVGLYQQSG; WDHKVSTVGLYQQSGM; DHKVSTVGLYQQSGMA; HKVSTVGLYQQSGMAL; KVSTVGLYQQSGMALE; VSTVGLYQQSGMALEL; STVGLYQQSGMALELF; TVGLYQQSGMALELFN; VGLYQQSGMALELFNP; GLYQQSGMALELFNPD; LYQQSGMALELFNPDE; YQQSGMALELFNPDEY; QQSGMALELFNPDEYY; QSGMALELFNPDEYYD; SGMALELFNPDEYYDI; GMALELFNPDEYYDIL; MALELFNPDEYYDILF; ALELFNPDEYYDILFP; LELFNPDEYYDILFPG; ELFNPDEYYDILFPGV; LFNPDEYYDILFPGVN; FNPDEYYDILFPGVNT; NPDEYYDILFPGVNTF; PDEYYDILFPGVNTFV; DEYYDILFPGVNTFVN; EYYDILFPGVNTFVNN; YYDILFPGVNTFVNNI; YDILFPGVNTFVNNIQ; DILFPGVNTFVNNIQY; ILFPGVNTFVNNIQYL; LFPGVNTFVNNIQYLD; FPGVNTFVNNIQYLDP; PGVNTFVNNIQYLDPR; GVNTFVNNIQYLDPRH; VNTFVNNIQYLDPRHW; NTFVNNIQYLDPRHWG; TFVNNIQYLDPRHWGP; FVNNIQYLDPRHWGPS; VNNIQYLDPRHWGPSL; NNIQYLDPRHWGPSLF; NIQYLDPRHWGPSLFA; IQYLDPRHWGPSLFAT; QYLDPRHWGPSLFATI; YLDPRHWGPSLFATIS; LDPRHWGPSLFATISQ; DPRHWGPSLFATISQA; PRHWGPSLFATISQAL; RHWGPSLFATISQALW; HWGPSLFATISQALWH; WGPSLFATISQALWHV; GPSLFATISQALWHVI; PSLFATISQALWHVIR; SLFATISQALWHVIRD; LFATISQALWHVIRDD; FATISQALWHVIRDDI; ATISQALWHVIRDDIP; TISQALWHVIRDDIPS; ISQALWHVIRDDIPSI; SQALWHVIRDDIPSIT; QALWHVIRDDIPSITS; ALWHVIRDDIPSITSQ; LWHVIRDDIPSITSQE; WHVIRDDIPSITSQEL; HVIRDDIPSITSQELQ; VIRDDIPSITSQELQR; IRDDIPSITSQELQRR; RDDIPSITSQELQRRT; DDIPSITSQELQRRTE; DIPSITSQELQRRTER; IPSITSQELQRRTERF; PSITSQELQRRTERFF; SITSQELQRRTERFFR; ITSQELQRRTERFFRD; TSQELQRRTERFFRDS; SQELQRRTERFFRDSL; QELQRRTERFFRDSLA; ELQRRTERFFRDSLAR; LQRRTERFFRDSLARF; QRRTERFFRDSLARFL; RRTERFFRDSLARFLE; RTERFFRDSLARFLEE; TERFFRDSLARFLEET; ERFFRDSLARFLEETT; RFFRDSLARFLEETTW; FFRDSLARFLEETTWT; FRDSLARFLEETTWTI; RDSLARFLEETTWTIV; DSLARFLEETTWTIVN; SLARFLEETTWTIVNA; LARFLEETTWTIVNAP; ARFLEETTWTIVNAPI; RFLEETTWTIVNAPIN; FLEETTWTIVNAPINF; LEETTWTIVNAPINFY; EETTWTIVNAPINFYN; ETTWTIVNAPINFYNY; TTWTIVNAPINFYNYI; TWTIVNAPINFYNYIQ; WTIVNAPINFYNYIQQ; TIVNAPINFYNYIQQY; IVNAPINFYNYIQQYY; VNAPINFYNYIQQYYS; NAPINFYNYIQQYYSD; APINFYNYIQQYYSDL; PINFYNYIQQYYSDLS; INFYNYIQQYYSDLSP; NFYNYIQQYYSDLSPI; FYNYIQQYYSDLSPIR; YNYIQQYYSDLSPIRP; NYIQQYYSDLSPIRPS; YIQQYYSDLSPIRPSM; IQQYYSDLSPIRPSMV; QQYYSDLSPIRPSMVR; QYYSDLSPIRPSMVRQ; YYSDLSPIRPSMVRQV; YSDLSPIRPSMVRQVA; SDLSPIRPSMVRQVAE; DLSPIRPSMVRQVAER; LSPIRPSMVRQVAERE; SPIRPSMVRQVAEREG; PIRPSMVRQVAEREGT; IRPSMVRQVAEREGTR; RPSMVRQVAEREGTRV; PSMVRQVAEREGTRVH; SMVRQVAEREGTRVHF; MVRQVAEREGTRVHFG; VRQVAEREGTRVHFGH; RQVAEREGTRVHFGHT; QVAEREGTRVHFGHTY; VAEREGTRVHFGHTYS; AEREGTRVHFGHTYSI; EREGTRVHFGHTYSID; REGTRVHFGHTYSIDD; EGTRVHFGHTYSIDDA; GTRVHFGHTYSIDDAD; TRVHFGHTYSIDDADS; RVHFGHTYSIDDADSI; VHFGHTYSIDDADSIE; HFGHTYSIDDADSIEE; FGHTYSIDDADSIEEV; GHTYSIDDADSIEEVT; HTYSIDDADSIEEVTQ; TYSIDDADSIEEVTQR; YSIDDADSIEEVTQRM; SIDDADSIEEVTQRMD; IDDADSIEEVTQRMDL; DDADSIEEVTQRMDLR; DADSIEEVTQRMDLRN; ADSIEEVTQRMDLRNQ; DSIEEVTQRMDLRNQQ; SIEEVTQRMDLRNQQS; IEEVTQRMDLRNQQSV; EEVTQRMDLRNQQSVH; EVTQRMDLRNQQSVHS; VTQRMDLRNQQSVHSG; TQRMDLRNQQSVHSGE; QRMDLRNQQSVHSGEF; RMDLRNQQSVHSGEFI; MDLRNQQSVHSGEFIE; DLRNQQSVHSGEFIEK; LRNQQSVHSGEFIEKT; RNQQSVHSGEFIEKTI; NQQSVHSGEFIEKTIA; QQSVHSGEFIEKTIAP; QSVHSGEFIEKTIAPG; SVHSGEFIEKTIAPGG; VHSGEFIEKTIAPGGA; HSGEFIEKTIAPGGAN; SGEFIEKTIAPGGANQ; GEFIEKTIAPGGANQR; EFIEKTIAPGGANQRT; FIEKTIAPGGANQRTA; IEKTIAPGGANQRTAP; EKTIAPGGANQRTAPQ; KTIAPGGANQRTAPQW; TIAPGGANQRTAPQWM; IAPGGANQRTAPQWML; APGGANQRTAPQWMLP; PGGANQRTAPQWMLPL; GGANQRTAPQWMLPLL; GANQRTAPQWMLPLLL; ANQRTAPQWMLPLLLG; NQRTAPQWMLPLLLGL; QRTAPQWMLPLLLGLY; RTAPQWMLPLLLGLYG; TAPQWMLPLLLGLYGT; APQWMLPLLLGLYGTV; PQWMLPLLLGLYGTVT; QWMLPLLLGLYGTVTP; WMLPLLLGLYGTVTPA; MLPLLLGLYGTVTPAL; LPLLLGLYGTVTPALE; PLLLGLYGTVTPALEA; LLLGLYGTVTPALEAY; LLGLYGTVTPALEAYE; LGLYGTVTPALEAYED; GLYGTVTPALEAYEDG; LYGTVTPALEAYEDGP; YGTVTPALEAYEDGPN; GTVTPALEAYEDGPNQ; TVTPALEAYEDGPNQK; VTPALEAYEDGPNQKK; TPALEAYEDGPNQKKR; PALEAYEDGPNQKKRR; ALEAYEDGPNQKKRRV; LEAYEDGPNQKKRRVS; EAYEDGPNQKKRRVSR; AYEDGPNQKKRRVSRG; YEDGPNQKKRRVSRGS; EDGPNQKKRRVSRGSS; DGPNQKKRRVSRGSSQ; GPNQKKRRVSRGSSQK; PNQKKRRVSRGSSQKA; NQKKRRVSRGSSQKAK; QKKRRVSRGSSQKAKG; KKRRVSRGSSQKAKGT; KRRVSRGSSQKAKGTR; RRVSRGSSQKAKGTRA; RVSRGSSQKAKGTRAS; VSRGSSQKAKGTRASA; SRGSSQKAKGTRASAK; RGSSQKAKGTRASAKT; GSSQKAKGTRASAKTT; SSQKAKGTRASAKTTN; SQKAKGTRASAKTTNK; QKAKGTRASAKTTNKR; KAKGTRASAKTTNKRR; AKGTRASAKTTNKRRS; KGTRASAKTTNKRRSR; GTRASAKTTNKRRSRS; TRASAKTTNKRRSRSS; RASAKTTNKRRSRSSR; ASAKTTNKRRSRSSRS; NWGRCYYRGRMLPKPR; WGRCYYRGRMLPKPRN; GRCYYRGRMLPKPRNG; RCYYRGRMLPKPRNGG; CYYRGRMLPKPRNGGS; YYRGRMLPKPRNGGSR; PREKNASLLQHSKNSP; REKNASLLQHSKNSPP; EKNASLLQHSKNSPPQ; KNASLLQHSKNSPPQF; NASLLQHSKNSPPQFK; GPNLWKSTDVGGCNCT; PNLWKSTDVGGCNCTN; NLWKSTDVGGCNCTNR; LWKSTDVGGCNCTNRG; WKSTDVGGCNCTNRGY; KSTDVGGCNCTNRGYW; STDVGGCNCTNRGYWN; TDVGGCNCTNRGYWNN; FPLLCCRWRTLGNAGS; PLLCCRWRTLGNAGSA; LLCCRWRTLGNAGSAN; LCCRWRTLGNAGSANE; CCRWRTLGNAGSANEL; CRWRTLGNAGSANELQ; RWRTLGNAGSANELQV; WRTLGNAGSANELQVK; RTLGNAGSANELQVKV; TLGNAGSANELQVKVP; VFWDFHRRGKCSPSTS; FWDFHRRGKCSPSTSC; WDFHRRGKCSPSTSCD; DFHRRGKCSPSTSCDQ; FHRRGKCSPSTSCDQH; HRRGKCSPSTSCDQHS; RRGKCSPSTSCDQHSY; RGKCSPSTSCDQHSYH; GKCSPSTSCDQHSYHS; KCSPSTSCDQHSYHSV; CSPSTSCDQHSYHSVA; SPSTSCDQHSYHSVAR; DPPEKKICKESLPNFL; PPEKKICKESLPNFLF; PEKKICKESLPNFLFA; EKKICKESLPNFLFAK; PYKQENPESGWAAYVW; YKQENPESGWAAYVWY; KQENPESGWAAYVWYG; QENPESGWAAYVWYGI; ENPESGWAAYVWYGIP; NPESGWAAYVWYGIPG; PESGWAAYVWYGIPGR; ESGWAAYVWYGIPGRR; SGWAAYVWYGIPGRRG; QTGTIANQNALNRCFY; TGTIANQNALNRCFYC; GTIANQNALNRCFYCT; TIANQNALNRCFYCTY; IANQNALNRCFYCTYT; ANQNALNRCFYCTYTF; NQNALNRCFYCTYTFN; QNALNRCFYCTYTFNK; NALNRCFYCTYTFNKC; ALNRCFYCTYTFNKCC; LNRCFYCTYTFNKCCF; NRCFYCTYTFNKCCFC; RCFYCTYTFNKCCFCI; CFYCTYTFNKCCFCIS; FYCTYTFNKCCFCISH; YCTYTFNKCCFCISHF; NTESLYTNATLDYGGL; TESLYTNATLDYGGLT; ESLYTNATLDYGGLTF; SLYTNATLDYGGLTFG; LYTNATLDYGGLTFGN; YTNATLDYGGLTFGNL; TNATLDYGGLTFGNLQ; NATLDYGGLTFGNLQQ; ATLDYGGLTFGNLQQG; TLDYGGLTFGNLQQGL; LDYGGLTFGNLQQGLK; DYGGLTFGNLQQGLKY; YGGLTFGNLQQGLKYL; GGLTFGNLQQGLKYLR; GLTFGNLQQGLKYLRL; LTFGNLQQGLKYLRLG; TFGNLQQGLKYLRLGK; FGNLQQGLKYLRLGKS; GNLQQGLKYLRLGKSI; NLQQGLKYLRLGKSIV; LQQGLKYLRLGKSIVI; QQGLKYLRLGKSIVIG; QGLKYLRLGKSIVIGI; GLKYLRLGKSIVIGIQ; LKYLRLGKSIVIGIQC; KYLRLGKSIVIGIQCL; YLRLGKSIVIGIQCLI; LRLGKSIVIGIQCLIH; RLGKSIVIGIQCLIHV; LGKSIVIGIQCLIHVQ; GKSIVIGIQCLIHVQS; KSIVIGIQCLIHVQSL; SIVIGIQCLIHVQSLQ; IVIGIQCLIHVQSLQF; VIGIQCLIHVQSLQFL; IGIQCLIHVQSLQFLN; GIQCLIHVQSLQFLNP; IQCLIHVQSLQFLNPL; QCLIHVQSLQFLNPLL; CLIHVQSLQFLNPLLL; YQEYISPCIYYISSLK; QEYISPCIYYISSLKK; EYISPCIYYISSLKKY; YISPCIYYISSLKKYT; ISPCIYYISSLKKYTY; SPCIYYISSLKKYTYL; PCIYYISSLKKYTYLS; CIYYISSLKKYTYLSQ; IYYISSLKKYTYLSQN; YYISSLKKYTYLSQNP; YISSLKKYTYLSQNPA; ISSLKKYTYLSQNPAF; SSLKKYTYLSQNPAFP; SLKKYTYLSQNPAFPS; LKKYTYLSQNPAFPSI; KKYTYLSQNPAFPSIQ; KYTYLSQNPAFPSIQQ; YTYLSQNPAFPSIQQF; TKLAVATRSFHFVKFF; KLAVATRSFHFVKFFF; LAVATRSFHFVKFFFQ; AVATRSFHFVKFFFQV; VATRSFHFVKFFFQVR; ATRSFHFVKFFFQVRT; TRSFHFVKFFFQVRTL; RSFHFVKFFFQVRTLS; SFHFVKFFFQVRTLSF; FHFVKFFFQVRTLSFV; HFVKFFFQVRTLSFVR; FVKFFFQVRTLSFVRI; VKFFFQVRTLSFVRIF; KFFFQVRTLSFVRIFL; FFFQVRTLSFVRIFLN; FFQVRTLSFVRIFLNI; FQVRTLSFVRIFLNIF; QVRTLSFVRIFLNIFW; VRTLSFVRIFLNIFWA; PSLVEIFGFFCLNVSF; SLVEIFGFFCLNVSFL; LVEIFGFFCLNVSFLN; VEIFGFFCLNVSFLNL; EIFGFFCLNVSFLNLP; HFHLNNLSNCLNCLFH; FHLNNLSNCLNCLFHV; HLNNLSNCLNCLFHVL; LNNLSNCLNCLFHVLK; NNLSNCLNCLFHVLKA; NLSNCLNCLFHVLKAN; LSNCLNCLFHVLKANP; SNCLNCLFHVLKANPL; NCLNCLFHVLKANPLI; CLNCLFHVLKANPLIQ; LNCLFHVLKANPLIQL; NCLFHVLKANPLIQLL; CLFHVLKANPLIQLLS; LFHVLKANPLIQLLSL; FHVLKANPLIQLLSLL; HVLKANPLIQLLSLLH; VLKANPLIQLLSLLHL; LKANPLIQLLSLLHLQ; KANPLIQLLSLLHLQK; ANPLIQLLSLLHLQKQ; NPLIQLLSLLHLQKQP; PLIQLLSLLHLQKQPC; LIQLLSLLHLQKQPCT; IQLLSLLHLQKQPCTD; QLLSLLHLQKQPCTDL; LHLAQRLAFPWVGLHL; HLAQRLAFPWVGLHLR; LAQRLAFPWVGLHLRL; AQRLAFPWVGLHLRLY; QRLAFPWVGLHLRLYH; RLAFPWVGLHLRLYHH; LAFPWVGLHLRLYHHT; AFPWVGLHLRLYHHTN; FPWVGLHLRLYHHTNL; PWVGLHLRLYHHTNLI; WVGLHLRLYHHTNLIT; VGLHLRLYHHTNLITL; GLHLRLYHHTNLITLQ; LHLRLYHHTNLITLQL; HLRLYHHTNLITLQLV; LRLYHHTNLITLQLVL; RLYHHTNLITLQLVLF; LYHHTNLITLQLVLFF; YHHTNLITLQLVLFFH; HHTNLITLQLVLFFHY; HTNLITLQLVLFFHYQ; TNLITLQLVLFFHYQW; NLITLQLVLFFHYQWD; LITLQLVLFFHYQWDL; VANSAAKQHLPYIVLV; ANSAAKQHLPYIVLVQ; NSAAKQHLPYIVLVQH; SAAKQHLPYIVLVQHF; AAKQHLPYIVLVQHFH; AKQHLPYIVLVQHFHE; KQHLPYIVLVQHFHEL; QHLPYIVLVQHFHELQ; HLPYIVLVQHFHELQI; LPYIVLVQHFHELQIL; PYIVLVQHFHELQILN; YIVLVQHFHELQILNP; IVLVQHFHELQILNPF; VLVQHFHELQILNPFY; LVQHFHELQILNPFYL; VQHFHELQILNPFYLI; QHFHELQILNPFYLIY; HFHELQILNPFYLIYD; IFLLAFLPWSYEGYLL; FLLAFLPWSYEGYLLF; LLAFLPWSYEGYLLFF; LKLYLLLADKYFFDFY; KLYLLLADKYFFDFYF; LYLLLADKYFFDFYFL; YLLLADKYFFDFYFLQ; LLLADKYFFDFYFLQK; SDKAGLFSDTFYTPLH; DKAGLFSDTFYTPLHC; KAGLFSDTFYTPLHCI; AGLFSDTFYTPLHCIE; GLFSDTFYTPLHCIEI; LFSDTFYTPLHCIEIL; FSDTFYTPLHCIEILN; SDTFYTPLHCIEILNT; DTFYTPLHCIEILNTY; TFYTPLHCIEILNTYL; FYTPLHCIEILNTYLI; YTPLHCIEILNTYLII; TPLHCIEILNTYLIIK; PLHCIEILNTYLIIKT; LHCIEILNTYLIIKTH; HCIEILNTYLIIKTHP; CIEILNTYLIIKTHPH; IEILNTYLIIKTHPHT; EILNTYLIIKTHPHTL; ILNTYLIIKTHPHTLS; LNTYLIIKTHPHTLSL; NTYLIIKTHPHTLSLL; TYLIIKTHPHTLSLLH; YLIIKTHPHTLSLLHT; LIIKTHPHTLSLLHTQ; GLLPFFFFWVVLSVEN; LLPFFFFWVVLSVENL; LPFFFFWVVLSVENLL; PFFFFWVVLSVENLLL; FFFFWVVLSVENLLLL; FFFWVVLSVENLLLLL; FFWVVLSVENLLLLLH; FWVVLSVENLLLLLHH; WVVLSVENLLLLLHHW; VVLSVENLLLLLHHWQ; VLSVENLLLLLHHWQT; LSVENLLLLLHHWQTY; SVENLLLLLHHWQTYL; VENLLLLLHHWQTYLH; ENLLLLLHHWQTYLHG; NLLLLLHHWQTYLHGK; LLLLLHHWQTYLHGKI; LLLLHHWQTYLHGKIN; LLLHHWQTYLHGKINL; LLHHWQTYLHGKINLH; LHHWQTYLHGKINLHP; HHWQTYLHGKINLHPI; HWQTYLHGKINLHPIF; WQTYLHGKINLHPIFH; RNSTRTPTLLFHRLAP; NSTRTPTLLFHRLAPI; STRTPTLLFHRLAPIK; TRTPTLLFHRLAPIKK; RTPTLLFHRLAPIKKI; TPTLLFHRLAPIKKII; PTLLFHRLAPIKKIIT; GLLIFYYLSKYKLVTL; LLIFYYLSKYKLVTLK; LIFYYLSKYKLVTLKL; ISEGSFSNYLDPPLQS; SEGSFSNYLDPPLQSF; EGSFSNYLDPPLQSFF; GSFSNYLDPPLQSFFS; AKPLCEAVNAVAIYPN; KPLCEAVNAVAIYPNQ; PLCEAVNAVAIYPNQG; LCEAVNAVAIYPNQGL; CEAVNAVAIYPNQGLF; EAVNAVAIYPNQGLFS; HARAVHRRLFGTNRPF; ARAVHRRLFGTNRPFL; RAVHRRLFGTNRPFLA; AVHRRLFGTNRPFLAV; VHRRLFGTNRPFLAVQ; HRRLFGTNRPFLAVQG; RRLFGTNRPFLAVQGI; RLFGTNRPFLAVQGIW; LFGTNRPFLAVQGIWA; FGTNRPFLAVQGIWAK; GTNRPFLAVQGIWAKR; TNRPFLAVQGIWAKRK; NRPFLAVQGIWAKRKI; RPFLAVQGIWAKRKIS; PFLAVQGIWAKRKIST; FLAVQGIWAKRKISTN; LAVQGIWAKRKISTNL; ATPGSKIRLMSYLYIL; TPGSKIRLMSYLYILL; PGSKIRLMSYLYILLH; GSKIRLMSYLYILLHF; SKIRLMSYLYILLHFF; KIRLMSYLYILLHFFI; IRLMSYLYILLHFFIQ; RLMSYLYILLHFFIQS; LMSYLYILLHFFIQSI; MSYLYILLHFFIQSIH; SYLYILLHFFIQSIHS; YLYILLHFFIQSIHSL; LYILLHFFIQSIHSLH; YILLHFFIQSIHSLHF; ILLHFFIQSIHSLHFI; LLHFFIQSIHSLHFIL; LHFFIQSIHSLHFILV; HFFIQSIHSLHFILVA; FFIQSIHSLHFILVAP; FIQSIHSLHFILVAPF; IQSIHSLHFILVAPFV; QSIHSLHFILVAPFVR; SIHSLHFILVAPFVRV; IHSLHFILVAPFVRVK; HSLHFILVAPFVRVKF; SLHFILVAPFVRVKFL; LHFILVAPFVRVKFLT; HFILVAPFVRVKFLT BK virus reverse reading frame 1 13 mers: MDKVLNREESMEL; DKVLNREESMELM; KVLNREESMELMD; VLNREESMELMDL; LNREESMELMDLL; NREESMELMDLLG; REESMELMDLLGL; EESMELMDLLGLE; ESMELMDLLGLER; SMELMDLLGLERA; MELMDLLGLERAA; ELMDLLGLERAAW; LMDLLGLERAAWG; MDLLGLERAAWGN; DLLGLERAAWGNL; LLGLERAAWGNLP; LGLERAAWGNLPL; GLERAAWGNLPLM; LERAAWGNLPLMR; ERAAWGNLPLMRK; RAAWGNLPLMRKA; AAWGNLPLMRKAY; AWGNLPLMRKAYL; WGNLPLMRKAYLR; GNLPLMRKAYLRK; NLPLMRKAYLRKC; LPLMRKAYLRKCK; PLMRKAYLRKCKE; LMRKAYLRKCKEF; MRKAYLRKCKEFH; RKAYLRKCKEFHP; KAYLRKCKEFHPD; AYLRKCKEFHPDK; YLRKCKEFHPDKG; LRKCKEFHPDKGG; RKCKEFHPDKGGD; KCKEFHPDKGGDE; CKEFHPDKGGDED; KEFHPDKGGDEDK; EFHPDKGGDEDKM; FHPDKGGDEDKMK; HPDKGGDEDKMKR; PDKGGDEDKMKRM; DKGGDEDKMKRMN; KGGDEDKMKRMNT; GGDEDKMKRMNTL; GDEDKMKRMNTLY; DEDKMKRMNTLYK; EDKMKRMNTLYKK; DKMKRMNTLYKKM; KMKRMNTLYKKME; MKRMNTLYKKMEQ; KRMNTLYKKMEQD; RMNTLYKKMEQDV; MNTLYKKMEQDVK; NTLYKKMEQDVKV; TLYKKMEQDVKVA; LYKKMEQDVKVAH; YKKMEQDVKVAHQ; KKMEQDVKVAHQP; KMEQDVKVAHQPD; MEQDVKVAHQPDF; EQDVKVAHQPDFG; QDVKVAHQPDFGT; DVKVAHQPDFGTW; VKVAHQPDFGTWS; KVAHQPDFGTWSS; VAHQPDFGTWSSS; AHQPDFGTWSSSE; HQPDFGTWSSSEV; QPDFGTWSSSEVC; PDFGTWSSSEVCA; DFGTWSSSEVCAD; FGTWSSSEVCADF; GTWSSSEVCADFP; TWSSSEVCADFPL; WSSSEVCADFPLC; SSSEVCADFPLCP; SSEVCADFPLCPD; SEVCADFPLCPDT; EVCADFPLCPDTL; VCADFPLCPDTLY; CADFPLCPDTLYC; ADFPLCPDTLYCK; DFPLCPDTLYCKE; FPLCPDTLYCKEW; PLCPDTLYCKEWP; LCPDTLYCKEWPI; CPDTLYCKEWPIC; PDTLYCKEWPICS; DTLYCKEWPICSK; TLYCKEWPICSKK; LYCKEWPICSKKP; YCKEWPICSKKPS; CKEWPICSKKPSV; KEWPICSKKPSVH; EWPICSKKPSVHC; WPICSKKPSVHCP; PICSKKPSVHCPC; ICSKKPSVHCPCM; CSKKPSVHCPCML; SKKPSVHCPCMLC; KKPSVHCPCMLCQ; KPSVHCPCMLCQL; PSVHCPCMLCQLR; SVHCPCMLCQLRL; VHCPCMLCQLRLR; HCPCMLCQLRLRH; CPCMLCQLRLRHL; PCMLCQLRLRHLN; CMLCQLRLRHLNR; MLCQLRLRHLNRK; LCQLRLRHLNRKF; CQLRLRHLNRKFL; QLRLRHLNRKFLR; LRLRHLNRKFLRK; RLRHLNRKFLRKE; LRHLNRKFLRKEP; RHLNRKFLRKEPL; HLNRKFLRKEPLV; LNRKFLRKEPLVW; NRKFLRKEPLVWI; RKFLRKEPLVWID; KFLRKEPLVWIDC; FLRKEPLVWIDCY; LRKEPLVWIDCYC; RKEPLVWIDCYCI; KEPLVWIDCYCID; EPLVWIDCYCIDC; PLVWIDCYCIDCF; LVWIDCYCIDCFT; VWIDCYCIDCFTQ; WIDCYCIDCFTQW; IDCYCIDCFTQWF; DCYCIDCFTQWFG; CYCIDCFTQWFGL; YCIDCFTQWFGLD; CIDCFTQWFGLDL; IDCFTQWFGLDLT; DCFTQWFGLDLTE; CFTQWFGLDLTEE; FTQWFGLDLTEET; TQWFGLDLTEETL; QWFGLDLTEETLQ; WFGLDLTEETLQW; FGLDLTEETLQWW; GLDLTEETLQWWV; LDLTEETLQWWVQ; DLTEETLQWWVQI; LTEETLQWWVQII; TEETLQWWVQIIG; EETLQWWVQIIGE; ETLQWWVQIIGET; TLQWWVQIIGETP; LQWWVQIIGETPF; QWWVQIIGETPFR; WWVQIIGETPFRD; WVQIIGETPFRDL; VQIIGETPFRDLK; QIIGETPFRDLKL; KALSNYFFYRCQP; ALSNYFFYRCQPM; LSNYFFYRCQPME; SNYFFYRCQPMEQ; NYFFYRCQPMEQK; YFFYRCQPMEQKS; FFYRCQPMEQKSG; FYRCQPMEQKSGS; YRCQPMEQKSGSP; RCQPMEQKSGSPG; CQPMEQKSGSPGG; QPMEQKSGSPGGV; PMEQKSGSPGGVP; MEQKSGSPGGVPL; EQKSGSPGGVPLM; QKSGSPGGVPLMK; KSGSPGGVPLMKN; SGSPGGVPLMKNG; GSPGGVPLMKNGM; SPGGVPLMKNGMK; PGGVPLMKNGMKI; GGVPLMKNGMKIY; GVPLMKNGMKIYF; VPLMKNGMKIYFA; PLMKNGMKIYFAM; LMKNGMKIYFAMK; MKNGMKIYFAMKI; KNGMKIYFAMKIC; NGMKIYFAMKICL; GMKIYFAMKICLP; MKIYFAMKICLPV; KIYFAMKICLPVM; IYFAMKICLPVMK; YFAMKICLPVMKK; FAMKICLPVMKKQ; AMKICLPVMKKQQ; MKICLPVMKKQQQ; KICLPVMKKQQQI; ICLPVMKKQQQIL; CLPVMKKQQQILN; LPVMKKQQQILNT; PVMKKQQQILNTQ; VMKKQQQILNTQH; MKKQQQILNTQHH; KKQQQILNTQHHP; KQQQILNTQHHPK; QQQILNTQHHPKK; QQILNTQHHPKKK; QILNTQHHPKKKE; ILNTQHHPKKKER; KTLKTFPLIYTSF; TLKTFPLIYTSFL; LKTFPLIYTSFLV; KTFPLIYTSFLVK; TFPLIYTSFLVKL; FPLIYTSFLVKLY; PLIYTSFLVKLYL; LIYTSFLVKLYLV; IYTSFLVKLYLVI; YTSFLVKLYLVIE; TSFLVKLYLVIEP; SFLVKLYLVIEPL; FLVKLYLVIEPLP; LVKLYLVIEPLPA; VKLYLVIEPLPAL; KLYLVIEPLPALL; LYLVIEPLPALLC; YLVIEPLPALLCI; LVIEPLPALLCIL; VIEPLPALLCILL; IEPLPALLCILLK; EPLPALLCILLKK; PLPALLCILLKKK; LPALLCILLKKKL; PALLCILLKKKLK; ALLCILLKKKLKF; LLCILLKKKLKFC; LCILLKKKLKFCI; CILLKKKLKFCIK; ILLKKKLKFCIKN; LLKKKLKFCIKNL; LKKKLKFCIKNLW; KKKLKFCIKNLWK; KKLKFCIKNLWKN; KLKFCIKNLWKNI; LKFCIKNLWKNIL; LLLVDTCVLGIIL; LLVDTCVLGIILY; LVDTCVLGIILYS; VDTCVLGIILYSF; LHIDIEFLQLIIS; HIDIEFLQLIISV; IDIEFLQLIISVK; DIEFLQLIISVKS; IEFLQLIISVKSC; EFLQLIISVKSCV; FLQLIISVKSCVP; LQLIISVKSCVPL; QLIISVKSCVPLV; LIISVKSCVPLVF; FVRVLIRNTYYIV; VRVLIRNTYYIVP; RSMILAQKSLKKQ; SMILAQKSLKKQS; MILAQKSLKKQSR; ILAQKSLKKQSRC; LAQKSLKKQSRCL; AQKSLKKQSRCLG; QKSLKKQSRCLGN; RSVKSVRKKTSLI; SVKSVRKKTSLIT; VKSVRKKTSLITL; KSVRKKTSLITLS; SVRKKTSLITLSI; VRKKTSLITLSIM; RKKTSLITLSIMK; KKTSLITLSIMKS; KTSLITLSIMKST; TSLITLSIMKSTL; SLITLSIMKSTLQ; LITLSIMKSTLQM; ITLSIMKSTLQML; TLSIMKSTLQMLL; LSIMKSTLQMLLF; SIMKSTLQMLLFL; IMKSTLQMLLFLQ; MKSTLQMLLFLQK; KSTLQMLLFLQKV; STLQMLLFLQKVK; TLQMLLFLQKVKI; LQMLLFLQKVKIK; QMLLFLQKVKIKK; MLLFLQKVKIKKV; LLFLQKVKIKKVF; LFLQKVKIKKVFV; FLQKVKIKKVFVS; LQKVKIKKVFVSK; QKVKIKKVFVSKQ; NNIWQVLLGCTVC; NIWQVLLGCTVCY; IWQVLLGCTVCYL; WQVLLGCTVCYLK; QVLLGCTVCYLKW; VLLGCTVCYLKWI; LLGCTVCYLKWIL; YLIFCTVLFSMYL; LIFCTVLFSMYLK; IFCTVLFSMYLKE; FCTVLFSMYLKED; CTVLFSMYLKEDT; TVLFSMYLKEDTG; VLFSMYLKEDTGY; LFSMYLKEDTGYL; FSMYLKEDTGYLK; SMYLKEDTGYLKV; MYLKEDTGYLKVP; YLKEDTGYLKVPL; LKEDTGYLKVPLI; KEDTGYLKVPLIV; EDTGYLKVPLIVE; DTGYLKVPLIVEK; TGYLKVPLIVEKQ; GYLKVPLIVEKQH; KGQELNQRICLQD; GQELNQRICLQDM; QELNQRICLQDME; TKEPKYFHQAWLQ; MSILSLKPCKLDL; ENPYKTQSSYLKK; NPYKTQSSYLKKE; PYKTQSSYLKKEF; YKTQSSYLKKEFY; KTQSSYLKKEFYK; TQSSYLKKEFYKV; QSSYLKKEFYKVE; LILQLIYNLELLN; ILQLIYNLELLNG; LQLIYNLELLNGR; QLIYNLELLNGRK; LIYNLELLNGRKG; IYNLELLNGRKGW; YNLELLNGRKGWI; NLELLNGRKGWIL; LELLNGRKGWILR; NIIYAWGNVFLIL; IIYAWGNVFLILQ; IYAWGNVFLILQE; YAWGNVFLILQEK; AWGNVFLILQEKR; WGNVFLILQEKRI; GNVFLILQEKRIQ; NVFLILQEKRIQK; VFLILQEKRIQKL; FLILQEKRIQKLK; LILQEKRIQKLKT; ILQEKRIQKLKTL; LQEKRIQKLKTLD; QEKRIQKLKTLDM; EKRIQKLKTLDMD; KRIQKLKTLDMDQ; RIQKLKTLDMDQA; IQKLKTLDMDQAL; QKLKTLDMDQALN; KLKTLDMDQALNP; LKTLDMDQALNPN; KTLDMDQALNPNH; TLDMDQALNPNHN; LDMDQALNPNHNA; DMDQALNPNHNAL; MDQALNPNHNALP; DQALNPNHNALPK; QALNPNHNALPKS; ALNPNHNALPKSQ; LNPNHNALPKSQI; NPNHNALPKSQIL; PNHNALPKSQILQ; NHNALPKSQILQP; HNALPKSQILQPL; NALPKSQILQPLL; ALPKSQILQPLLK; LPKSQILQPLLKI; PKSQILQPLLKIP; KSQILQPLLKIPK; SQILQPLLKIPKG; QILQPLLKIPKGQ; ILQPLLKIPKGQT; LQPLLKIPKGQTP; QPLLKIPKGQTPI; PLLKIPKGQTPIV; LLKIPKGQTPIVK; LKIPKGQTPIVKS; KIPKGQTPIVKSC; IPKGQTPIVKSCI; PKGQTPIVKSCIC; KGQTPIVKSCICV; GQTPIVKSCICVK; QTPIVKSCICVKA; TPIVKSCICVKAF; PIVKSCICVKAFS; IVKSCICVKAFSV; VKSCICVKAFSVL; KSCICVKAFSVLK; SCICVKAFSVLKG; CICVKAFSVLKGL; ICVKAFSVLKGLK; CVKAFSVLKGLKH; VKAFSVLKGLKHH; KAFSVLKGLKHHP; AFSVLKGLKHHPQ; FSVLKGLKHHPQN; SVLKGLKHHPQNN; VLKGLKHHPQNNT; LKGLKHHPQNNTS; KGLKHHPQNNTSL; GLKHHPQNNTSLK; LKHHPQNNTSLKV; KHHPQNNTSLKVA; HHPQNNTSLKVAY; HPQNNTSLKVAYT; PQNNTSLKVAYTK; QNNTSLKVAYTKA; NNTSLKVAYTKAA; NTSLKVAYTKAAF; TSLKVAYTKAAFI; SLKVAYTKAAFIK; LKVAYTKAAFIKC; KVAYTKAAFIKCI; VAYTKAAFIKCIC; AYTKAAFIKCICT; YTKAAFIKCICTI; TKAAFIKCICTIK; KAAFIKCICTIKA; AAFIKCICTIKAP; AFIKCICTIKAPV; SILVCNCPCLSIY; ILVCNCPCLSIYL; LVCNCPCLSIYLI; VCNCPCLSIYLII; CNCPCLSIYLIIS; NCPCLSIYLIISG; CPCLSIYLIISGS; PCLSIYLIISGSP; CLSIYLIISGSPG; LSIYLIISGSPGS; SIYLIISGSPGSL; IYLIISGSPGSLS; YLIISGSPGSLSV; LIISGSPGSLSVP; IISGSPGSLSVPS; ISGSPGSLSVPSN; SGSPGSLSVPSNT; GSPGSLSVPSNTL; SPGSLSVPSNTLT; PGSLSVPSNTLTS; GSLSVPSNTLTSS; SLSVPSNTLTSST; LSVPSNTLTSSTW; SVPSNTLTSSTWD; VPSNTLTSSTWDS; PSNTLTSSTWDSI; SNTLTSSTWDSIP; NTLTSSTWDSIPY; TLTSSTWDSIPYI; LTSSTWDSIPYIG; TSSTWDSIPYIGC; SSTWDSIPYIGCP; STWDSIPYIGCPS; TWDSIPYIGCPST; WDSIPYIGCPSTL; DSIPYIGCPSTLW; SIPYIGCPSTLWV; IPYIGCPSTLWVL; PYIGCPSTLWVLL; YIGCPSTLWVLLF; IGCPSTLWVLLFI; GCPSTLWVLLFIR; CPSTLWVLLFIRS; PSTLWVLLFIRSL; STLWVLLFIRSLS; TLWVLLFIRSLSK; LWVLLFIRSLSKK; WVLLFIRSLSKKE; VLLFIRSLSKKEI; LLFIRSLSKKEIG; GFFTDLFLRRILK; FFTDLFLRRILKY; FTDLFLRRILKYL; TDLFLRRILKYLA; DLFLRRILKYLAR; LFLRRILKYLARP; FLRRILKYLARPL; LRRILKYLARPLH; RRILKYLARPLHC; RILKYLARPLHCC; ILKYLARPLHCCV; LKYLARPLHCCVP; KYLARPLHCCVPE; YLARPLHCCVPEL; LARPLHCCVPELL; ARPLHCCVPELLV; RPLHCCVPELLVN; PLHCCVPELLVNR; LHCCVPELLVNRP; HCCVPELLVNRPQ; CCVPELLVNRPQI; CVPELLVNRPQIS; VPELLVNRPQISA; PELLVNRPQISAA; ELLVNRPQISAAE; LLVNRPQISAAET; LVNRPQISAAETY; VNRPQISAAETYR; NRPQISAAETYRL; RPQISAAETYRLS; PQISAAETYRLSA; QISAAETYRLSAL; ISAAETYRLSALQ; SAAETYRLSALQR; AAETYRLSALQRG; AETYRLSALQRGP; ETYRLSALQRGPT; TYRLSALQRGPTP; YRLSALQRGPTPC; RLSALQRGPTPCS; LSALQRGPTPCSS; SALQRGPTPCSSS; ALQRGPTPCSSSN; LQRGPTPCSSSNT; QRGPTPCSSSNTV; RGPTPCSSSNTVV; GPTPCSSSNTVVA; PTPCSSSNTVVAV; TPCSSSNTVVAVL; PCSSSNTVVAVLV; CSSSNTVVAVLVT; STGGTFSPPVKVP; TGGTFSPPVKVPK; GGTFSPPVKVPKY; GTFSPPVKVPKYL; TFSPPVKVPKYLA; FSPPVKVPKYLAF; SPPVKVPKYLAFS; PPVKVPKYLAFSF; PVKVPKYLAFSFL; VKVPKYLAFSFLL; KVPKYLAFSFLLG; VPKYLAFSFLLGS; PKYLAFSFLLGSG; KYLAFSFLLGSGT; YLAFSFLLGSGTQ; LAFSFLLGSGTQH; AFSFLLGSGTQHS; FSFLLGSGTQHST; SFLLGSGTQHSTG; ALWSVFITWDWAV; LWSVFITWDWAVG; WSVFITWDWAVGF; SVFITWDWAVGFL; VFITWDWAVGFLG; FITWDWAVGFLGV; ITWDWAVGFLGVI; TWDWAVGFLGVIV; WDWAVGFLGVIVP; DWAVGFLGVIVPS; WAVGFLGVIVPSG; AVGFLGVIVPSGY; VGFLGVIVPSGYF; GFLGVIVPSGYFD; FLGVIVPSGYFDL; FISTPCISKGSPP; ISTPCISKGSPPT; STPCISKGSPPTA; TPCISKGSPPTAK; PCISKGSPPTAKK; CISKGSPPTAKKW; ISKGSPPTAKKWK; SKGSPPTAKKWKL; KGSPPTAKKWKLL; GSPPTAKKWKLLP; IGFPPPCSCTFCD; GFPPPCSCTFCDP; FPPPCSCTFCDPA; RLSMLVIPITSVC; LSMLVIPITSVCT; SMLVIPITSVCTV; MLVIPITSVCTVT; LVIPITSVCTVTA; VIPITSVCTVTAS; IPITSVCTVTASH; PITSVCTVTASHI; ITSVCTVTASHIS; TSVCTVTASHISR; SVCTVTASHISRF; VCTVTASHISRFP; CTVTASHISRFPQ; TVTASHISRFPQV; VTASHISRFPQVR; TASHISRFPQVRS; ASHISRFPQVRSS; SHISRFPQVRSSF; HISRFPQVRSSFK; ISRFPQVRSSFKL; SRFPQVRSSFKLG; RFPQVRSSFKLGR; FPQVRSSFKLGRG; PQVRSSFKLGRGI; QVRSSFKLGRGIL; VRSSFKLGRGILA; RSSFKLGRGILAV; SSFKLGRGILAVL; QGSIFLSGLSLLK; GSIFLSGLSLLKS; SIFLSGLSLLKSF; IFLSGLSLLKSFS; FLSGLSLLKSFSA; LSGLSLLKSFSAL; SGLSLLKSFSALS; GLSLLKSFSALSF; LSLLKSFSALSFR; SLLKSFSALSFRL; LLKSFSALSFRLK; LKSFSALSFRLKP; KSFSALSFRLKPL; SFSALSFRLKPLR; FSALSFRLKPLRF; SALSFRLKPLRFS; ALSFRLKPLRFSS; LSFRLKPLRFSSG; SFRLKPLRFSSGS; FRLKPLRFSSGSP; RLKPLRFSSGSPI; LKPLRFSSGSPIS; KPLRFSSGSPISG; PLRFSSGSPISGF; LRFSSGSPISGFR; RFSSGSPISGFRK; FSSGSPISGFRKH; SSGSPISGFRKHS; SGSPISGFRKHST; GSPISGFRKHSTS; SPISGFRKHSTSV; PISGFRKHSTSVI; ISGFRKHSTSVIA; SGFRKHSTSVIAS; GFRKHSTSVIAST; FRKHSTSVIASTP; RKHSTSVIASTPV; KHSTSVIASTPVL; HSTSVIASTPVLT; STSVIASTPVLTS; TSVIASTPVLTSR; SVIASTPVLTSRT; VIASTPVLTSRTS; IASTPVLTSRTST; ASTPVLTSRTSTP; STPVLTSRTSTPP; TPVLTSRTSTPPF; PVLTSRTSTPPFI; VLTSRTSTPPFIS; LTSRTSTPPFISS; TSRTSTPPFISSF; SRTSTPPFISSFG; RTSTPPFISSFGT; TSTPPFISSFGTC; STPPFISSFGTCT; TPPFISSFGTCTG; PPFISSFGTCTGS; PFISSFGTCTGSF; FISSFGTCTGSFG; ISSFGTCTGSFGF; SSFGTCTGSFGFL; SFGTCTGSFGFLG; FGTCTGSFGFLGA; GTCTGSFGFLGAA; TCTGSFGFLGAAP; CTGSFGFLGAAPG; TGSFGFLGAAPGH; GSFGFLGAAPGHS; SFGFLGAAPGHSP; FGFLGAAPGHSPF; GFLGAAPGHSPFL; FLGAAPGHSPFLL; LGAAPGHSPFLLV; GAAPGHSPFLLVG; AAPGHSPFLLVGA; APGHSPFLLVGAI; PGHSPFLLVGAIF; GHSPFLLVGAIFI; HSPFLLVGAIFIC; SPFLLVGAIFICF; PFLLVGAIFICFK; FLLVGAIFICFKS; LLVGAIFICFKSR; LVGAIFICFKSRC; VGAIFICFKSRCY; GAIFICFKSRCYS; AIFICFKSRCYSP; IFICFKSRCYSPV; FICFKSRCYSPVQ; ICFKSRCYSPVQA; RQHPLRSSSLIST; QHPLRSSSLISTS; HPLRSSSLISTSW; PLRSSSLISTSWG; LRSSSLISTSWGN; RSSSLISTSWGNS; SSSLISTSWGNSF; SSLISTSWGNSFF; SLISTSWGNSFFY; LISTSWGNSFFYK; ISTSWGNSFFYKL; STSWGNSFFYKLS; VHSLCNFFYTVSI; HSLCNFFYTVSII; SLCNFFYTVSIIY; LCNFFYTVSIIYT; CNFFYTVSIIYTI; NFFYTVSIIYTIS; FFYTVSIIYTISM; FYTVSIIYTISMA; YTVSIIYTISMAK; TVSIIYTISMAKM; VSIIYTISMAKMY; SIIYTISMAKMYT; IIYTISMAKMYTG; IYTISMAKMYTGT; YTISMAKMYTGTF; TISMAKMYTGTFP; ISMAKMYTGTFPF; SMAKMYTGTFPFS; MAKMYTGTFPFSY; AKMYTGTFPFSYL; KMYTGTFPFSYLS; MYTGTFPFSYLSN; YTGTFPFSYLSNH; GPNRGKIRIILLN; PNRGKIRIILLNI; NRGKIRIILLNII; RGKIRIILLNIII; GKIRIILLNIIIK; KIRIILLNIIIKV; IRIILLNIIIKVY; RIILLNIIIKVYR; IILLNIIIKVYRG; ILLNIIIKVYRGI; LLNIIIKVYRGIY; LNIIIKVYRGIYN; NIIIKVYRGIYNC; IIIKVYRGIYNCP; IIKVYRGIYNCPG; IKVYRGIYNCPGS; KVYRGIYNCPGSF; VYRGIYNCPGSFL; YRGIYNCPGSFLQ; RGIYNCPGSFLQK; GIYNCPGSFLQKS; IYNCPGSFLQKSS; YNCPGSFLQKSSQ; NCPGSFLQKSSQG; CPGSFLQKSSQGV; PGSFLQKSSQGVS; GSFLQKSSQGVSK; SFLQKSSQGVSKK; FLQKSSQGVSKKS; LQKSSQGVSKKSF; QKSSQGVSKKSFC; KSSQGVSKKSFCS; SSQGVSKKSFCSS; SQGVSKKSFCSSL; QGVSKKSFCSSLQ; GVSKKSFCSSLQF; VSKKSFCSSLQFL; GYRRYIIPNNMPQ; YRRYIIPNNMPQS; RRYIIPNNMPQSL; RYIIPNNMPQSLG; YIIPNNMPQSLGN; IIPNNMPQSLGNS; IPNNMPQSLGNSS; PNNMPQSLGNSSK; NNMPQSLGNSSKQ; NMPQSLGNSSKQR; MPQSLGNSSKQRR; PQSLGNSSKQRRT; QSLGNSSKQRRTP; SLGNSSKQRRTPM; LGNSSKQRRTPMP; GNSSKQRRTPMPR; NSSKQRRTPMPRI; SSKQRRTPMPRIK; SKQRRTPMPRIKV; KQRRTPMPRIKVL; QRRTPMPRIKVLN; RRTPMPRIKVLNI; RTPMPRIKVLNII; TPMPRIKVLNIIN; PMPRIKVLNIINK; MPRIKVLNIINKS; PRIKVLNIINKSI; RIKVLNIINKSIY; IKVLNIINKSIYT; KVLNIINKSIYTR; VLNIINKSIYTRK; LNIINKSIYTRKQ; NIINKSIYTRKQN; IINKSIYTRKQNI; INKSIYTRKQNII; NKSIYTRKQNIIV; KSIYTRKQNIIVL; SIYTRKQNIIVLI; IYTRKQNIIVLIW; YTRKQNIIVLIWV; TRKQNIIVLIWVK; RKQNIIVLIWVKQ; KQNIIVLIWVKQF; QNIIVLIWVKQFQ; NIIVLIWVKQFQS; IIVLIWVKQFQSH; IVLIWVKQFQSHA; LLIEAYSGNFVIP; LIEAYSGNFVIPI; IEAYSGNFVIPII; EAYSGNFVIPIIK; AYSGNFVIPIIKE; YSGNFVIPIIKEL; SGNFVIPIIKELI; GNFVIPIIKELIP; NFVIPIIKELIPY; FVIPIIKELIPYL; VIPIIKELIPYLS; SSKPSNSPRSTSN; SKPSNSPRSTSNY; KPSNSPRSTSNYS; PSNSPRSTSNYSI; SNSPRSTSNYSIC; NSPRSTSNYSICL; SPRSTSNYSICLR; PRSTSNYSICLRS; GTCYALYSSKGCN; TCYALYSSKGCNL; CYALYSSKGCNLN; YALYSSKGCNLNF; ALYSSKGCNLNFY; LYSSKGCNLNFYS; YSSKGCNLNFYSS; SSKGCNLNFYSSS; SKGCNLNFYSSSS; KGCNLNFYSSSSL; GCNLNFYSSSSLP; CNLNFYSSSSLPS; NLNFYSSSSLPSS; LNFYSSSSLPSSN; NFYSSSSLPSSNF; FYSSSSLPSSNFS; YSSSSLPSSNFSH; KSCGSSSLRYTGN; SSTHEPGNTKKKG; STHEPGNTKKKGL; THEPGNTKKKGLL; HEPGNTKKKGLLT; ESFTESFTAGKAV; SFTESFTAGKAVV; FTESFTAGKAVVL; TESFTAGKAVVLL; ESFTAGKAVVLLF; SFTAGKAVVLLFF; FTAGKAVVLLFFP; TAGKAVVLLFFPS; AGKAVVLLFFPST; GKAVVLLFFPSTL; KAVVLLFFPSTLS; AVVLLFFPSTLSS; VVLLFFPSTLSSP; VLLFFPSTLSSPL; LLFFPSTLSSPLQ; LFFPSTLSSPLQN; FFPSTLSSPLQNS; FPSTLSSPLQNSS; PSTLSSPLQNSSK; STLSSPLQNSSKS; TLSSPLQNSSKSS; LSSPLQNSSKSSK; SSPLQNSSKSSKI; SPLQNSSKSSKIK; PLQNSSKSSKIKI; LQNSSKSSKIKIK; QNSSKSSKIKIKI; NSSKSSKIKIKIL; ALFFVPVQVLPTF; LFFVPVQVLPTFT; FFVPVQVLPTFTE; FVPVQVLPTFTEA; VPVQVLPTFTEAC; PVQVLPTFTEACR; VQVLPTFTEACRD; QVLPTFTEACRDS; VLPTFTEACRDSW; LPTFTEACRDSWR; PTFTEACRDSWRR; TFTEACRDSWRRT; FTEACRDSWRRTM; TEACRDSWRRTMA; EACRDSWRRTMAF; ACRDSWRRTMAFV; CRDSWRRTMAFVQ; RDSWRRTMAFVQF; DSWRRTMAFVQFN; SWRRTMAFVQFNW; WRRTMAFVQFNWG; RRTMAFVQFNWGQ; RTMAFVQFNWGQG; TMAFVQFNWGQGQ; MAFVQFNWGQGQD; AFVQFNWGQGQDS; ARKTCLSCTFLPE; RKTCLSCTFLPEV; KTCLSCTFLPEVM; TCLSCTFLPEVMV; CLSCTFLPEVMVW; LSCTFLPEVMVWL; SCTFLPEVMVWLH; CTFLPEVMVWLHS; TFLPEVMVWLHSM; FLPEVMVWLHSMG; LPEVMVWLHSMGK; PEVMVWLHSMGKQ; EVMVWLHSMGKQL; VMVWLHSMGKQLL; MVWLHSMGKQLLP; VWLHSMGKQLLPV; WLHSMGKQLLPVS; LHSMGKQLLPVSH; HSMGKQLLPVSHA; SMGKQLLPVSHAL; MGKQLLPVSHALS; GKQLLPVSHALSF; KQLLPVSHALSFL; QLLPVSHALSFLR; LLPVSHALSFLRS; LPVSHALSFLRSW; PVSHALSFLRSWF; VSHALSFLRSWFG; SHALSFLRSWFGC; HALSFLRSWFGCI; ALSFLRSWFGCIP; LSFLRSWFGCIPL; EAEAASASTLSLK; GLAKLFGEIPILL; LAKLFGEIPILLQ; AKLFGEIPILLQF; KLFGEIPILLQFL; LFGEIPILLQFLQ 14 mers: MDKVLNREESMELM; DKVLNREESMELMD; KVLNREESMELMDL; VLNREESMELMDLL; LNREESMELMDLLG; NREESMELMDLLGL; REESMELMDLLGLE; EESMELMDLLGLER; ESMELMDLLGLERA; SMELMDLLGLERAA; MELMDLLGLERAAW; ELMDLLGLERAAWG; LMDLLGLERAAWGN; MDLLGLERAAWGNL; DLLGLERAAWGNLP; LLGLERAAWGNLPL; LGLERAAWGNLPLM; GLERAAWGNLPLMR; LERAAWGNLPLMRK; ERAAWGNLPLMRKA; RAAWGNLPLMRKAY; AAWGNLPLMRKAYL; AWGNLPLMRKAYLR; WGNLPLMRKAYLRK; GNLPLMRKAYLRKC; NLPLMRKAYLRKCK; LPLMRKAYLRKCKE; PLMRKAYLRKCKEF; LMRKAYLRKCKEFH; MRKAYLRKCKEFHP; RKAYLRKCKEFHPD; KAYLRKCKEFHPDK; AYLRKCKEFHPDKG; YLRKCKEFHPDKGG; LRKCKEFHPDKGGD; RKCKEFHPDKGGDE; KCKEFHPDKGGDED; CKEFHPDKGGDEDK; KEFHPDKGGDEDKM; EFHPDKGGDEDKMK; FHPDKGGDEDKMKR; HPDKGGDEDKMKRM; PDKGGDEDKMKRMN; DKGGDEDKMKRMNT; KGGDEDKMKRMNTL; GGDEDKMKRMNTLY; GDEDKMKRMNTLYK; DEDKMKRMNTLYKK; EDKMKRMNTLYKKM; DKMKRMNTLYKKME; KMKRMNTLYKKMEQ; MKRMNTLYKKMEQD; KRMNTLYKKMEQDV; RMNTLYKKMEQDVK; MNTLYKKMEQDVKV; NTLYKKMEQDVKVA; TLYKKMEQDVKVAH; LYKKMEQDVKVAHQ; YKKMEQDVKVAHQP; KKMEQDVKVAHQPD; KMEQDVKVAHQPDF; MEQDVKVAHQPDFG; EQDVKVAHQPDFGT; QDVKVAHQPDFGTW; DVKVAHQPDFGTWS; VKVAHQPDFGTWSS; KVAHQPDFGTWSSS; VAHQPDFGTWSSSE; AHQPDFGTWSSSEV; HQPDFGTWSSSEVC; QPDFGTWSSSEVCA; PDFGTWSSSEVCAD; DFGTWSSSEVCADF; FGTWSSSEVCADFP; GTWSSSEVCADFPL; TWSSSEVCADFPLC; WSSSEVCADFPLCP; SSSEVCADFPLCPD; SSEVCADFPLCPDT; SEVCADFPLCPDTL; EVCADFPLCPDTLY; VCADFPLCPDTLYC; CADFPLCPDTLYCK; ADFPLCPDTLYCKE; DFPLCPDTLYCKEW; FPLCPDTLYCKEWP; PLCPDTLYCKEWPI; LCPDTLYCKEWPIC; CPDTLYCKEWPICS; PDTLYCKEWPICSK; DTLYCKEWPICSKK; TLYCKEWPICSKKP; LYCKEWPICSKKPS; YCKEWPICSKKPSV; CKEWPICSKKPSVH; KEWPICSKKPSVHC; EWPICSKKPSVHCP; WPICSKKPSVHCPC; PICSKKPSVHCPCM; ICSKKPSVHCPCML; CSKKPSVHCPCMLC; SKKPSVHCPCMLCQ; KKPSVHCPCMLCQL; KPSVHCPCMLCQLR; PSVHCPCMLCQLRL; SVHCPCMLCQLRLR; VHCPCMLCQLRLRH; HCPCMLCQLRLRHL; CPCMLCQLRLRHLN; PCMLCQLRLRHLNR; CMLCQLRLRHLNRK; MLCQLRLRHLNRKF; LCQLRLRHLNRKFL; CQLRLRHLNRKFLR; QLRLRHLNRKFLRK; LRLRHLNRKFLRKE; RLRHLNRKFLRKEP; LRHLNRKFLRKEPL; RHLNRKFLRKEPLV; HLNRKFLRKEPLVW; LNRKFLRKEPLVWI; NRKFLRKEPLVWID; RKFLRKEPLVWIDC; KFLRKEPLVWIDCY; FLRKEPLVWIDCYC; LRKEPLVWIDCYCI; RKEPLVWIDCYCID; KEPLVWIDCYCIDC; EPLVWIDCYCIDCF; PLVWIDCYCIDCFT; LVWIDCYCIDCFTQ; VWIDCYCIDCFTQW; WIDCYCIDCFTQWF; IDCYCIDCFTQWFG; DCYCIDCFTQWFGL; CYCIDCFTQWFGLD; YCIDCFTQWFGLDL; CIDCFTQWFGLDLT; IDCFTQWFGLDLTE; DCFTQWFGLDLTEE; CFTQWFGLDLTEET; FTQWFGLDLTEETL; TQWFGLDLTEETLQ; QWFGLDLTEETLQW; WFGLDLTEETLQWW; FGLDLTEETLQWWV; GLDLTEETLQWWVQ; LDLTEETLQWWVQI; DLTEETLQWWVQII; LTEETLQWWVQIIG; TEETLQWWVQIIGE; EETLQWWVQIIGET; ETLQWWVQIIGETP; TLQWWVQIIGETPF; LQWWVQIIGETPFR; QWWVQIIGETPFRD; WWVQIIGETPFRDL; WVQIIGETPFRDLK; VQIIGETPFRDLKL; KALSNYFFYRCQPM; ALSNYFFYRCQPME; LSNYFFYRCQPMEQ; SNYFFYRCQPMEQK; NYFFYRCQPMEQKS; YFFYRCQPMEQKSG; FFYRCQPMEQKSGS; FYRCQPMEQKSGSP; YRCQPMEQKSGSPG; RCQPMEQKSGSPGG; CQPMEQKSGSPGGV; QPMEQKSGSPGGVP; PMEQKSGSPGGVPL; MEQKSGSPGGVPLM; EQKSGSPGGVPLMK; QKSGSPGGVPLMKN; KSGSPGGVPLMKNG; SGSPGGVPLMKNGM; GSPGGVPLMKNGMK; SPGGVPLMKNGMKI; PGGVPLMKNGMKIY; GGVPLMKNGMKIYF; GVPLMKNGMKIYFA; VPLMKNGMKIYFAM; PLMKNGMKIYFAMK; LMKNGMKIYFAMKI; MKNGMKIYFAMKIC; KNGMKIYFAMKICL; NGMKIYFAMKICLP; GMKIYFAMKICLPV; MKIYFAMKICLPVM; KIYFAMKICLPVMK; IYFAMKICLPVMKK; YFAMKICLPVMKKQ; FAMKICLPVMKKQQ; AMKICLPVMKKQQQ; MKICLPVMKKQQQI; KICLPVMKKQQQIL; ICLPVMKKQQQILN; CLPVMKKQQQILNT; LPVMKKQQQILNTQ; PVMKKQQQILNTQH; VMKKQQQILNTQHH; MKKQQQILNTQHHP; KKQQQILNTQHHPK; KQQQILNTQHHPKK; QQQILNTQHHPKKK; QQILNTQHHPKKKE; QILNTQHHPKKKER; KTLKTFPLIYTSFL; TLKTFPLIYTSFLV; LKTFPLIYTSFLVK; KTFPLIYTSFLVKL; TFPLIYTSFLVKLY; FPLIYTSFLVKLYL; PLIYTSFLVKLYLV; LIYTSFLVKLYLVI; IYTSFLVKLYLVIE; YTSFLVKLYLVIEP; TSFLVKLYLVIEPL; SFLVKLYLVIEPLP; FLVKLYLVIEPLPA; LVKLYLVIEPLPAL; VKLYLVIEPLPALL; KLYLVIEPLPALLC; LYLVIEPLPALLCI; YLVIEPLPALLCIL; LVIEPLPALLCILL; VIEPLPALLCILLK; IEPLPALLCILLKK; EPLPALLCILLKKK; PLPALLCILLKKKL; LPALLCILLKKKLK; PALLCILLKKKLKF; ALLCILLKKKLKFC; LLCILLKKKLKFCI; LCILLKKKLKFCIK; CILLKKKLKFCIKN; ILLKKKLKFCIKNL; LLKKKLKFCIKNLW; LKKKLKFCIKNLWK; KKKLKFCIKNLWKN; KKLKFCIKNLWKNI; KLKFCIKNLWKNIL; LLLVDTCVLGIILY; LLVDTCVLGIILYS; LVDTCVLGIILYSF; LHIDIEFLQLIISV; HIDIEFLQLIISVK; IDIEFLQLIISVKS; DIEFLQLIISVKSC; IEFLQLIISVKSCV; EFLQLIISVKSCVP; FLQLIISVKSCVPL; LQLIISVKSCVPLV; QLIISVKSCVPLVF; FVRVLIRNTYYIVP; RSMILAQKSLKKQS; SMILAQKSLKKQSR; MILAQKSLKKQSRC; ILAQKSLKKQSRCL; LAQKSLKKQSRCLG; AQKSLKKQSRCLGN; RSVKSVRKKTSLIT; SVKSVRKKTSLITL; VKSVRKKTSLITLS; KSVRKKTSLITLSI; SVRKKTSLITLSIM; VRKKTSLITLSIMK; RKKTSLITLSIMKS; KKTSLITLSIMKST; KTSLITLSIMKSTL; TSLITLSIMKSTLQ; SLITLSIMKSTLQM; LITLSIMKSTLQML; ITLSIMKSTLQMLL; TLSIMKSTLQMLLF; LSIMKSTLQMLLFL; SIMKSTLQMLLFLQ; IMKSTLQMLLFLQK; MKSTLQMLLFLQKV; KSTLQMLLFLQKVK; STLQMLLFLQKVKI; TLQMLLFLQKVKIK; LQMLLFLQKVKIKK; QMLLFLQKVKIKKV; MLLFLQKVKIKKVF; LLFLQKVKIKKVFV; LFLQKVKIKKVFVS; FLQKVKIKKVFVSK; LQKVKIKKVFVSKQ; NNIWQVLLGCTVCY; NIWQVLLGCTVCYL; IWQVLLGCTVCYLK; WQVLLGCTVCYLKW; QVLLGCTVCYLKWI; VLLGCTVCYLKWIL; YLIFCTVLFSMYLK; LIFCTVLFSMYLKE; IFCTVLFSMYLKED; FCTVLFSMYLKEDT; CTVLFSMYLKEDTG; TVLFSMYLKEDTGY; VLFSMYLKEDTGYL; LFSMYLKEDTGYLK; FSMYLKEDTGYLKV; SMYLKEDTGYLKVP; MYLKEDTGYLKVPL; YLKEDTGYLKVPLI; LKEDTGYLKVPLIV; KEDTGYLKVPLIVE; EDTGYLKVPLIVEK; DTGYLKVPLIVEKQ; TGYLKVPLIVEKQH; KGQELNQRICLQDM; GQELNQRICLQDME; ENPYKTQSSYLKKE; NPYKTQSSYLKKEF; PYKTQSSYLKKEFY; YKTQSSYLKKEFYK; KTQSSYLKKEFYKV; TQSSYLKKEFYKVE; LILQLIYNLELLNG; ILQLIYNLELLNGR; LQLIYNLELLNGRK; QLIYNLELLNGRKG; LIYNLELLNGRKGW; IYNLELLNGRKGWI; YNLELLNGRKGWIL; NLELLNGRKGWILR; NIIYAWGNVFLILQ; IIYAWGNVFLILQE; IYAWGNVFLILQEK; YAWGNVFLILQEKR; AWGNVFLILQEKRI; WGNVFLILQEKRIQ; GNVFLILQEKRIQK; NVFLILQEKRIQKL; VFLILQEKRIQKLK; FLILQEKRIQKLKT; LILQEKRIQKLKTL; ILQEKRIQKLKTLD; LQEKRIQKLKTLDM; QEKRIQKLKTLDMD; EKRIQKLKTLDMDQ; KRIQKLKTLDMDQA; RIQKLKTLDMDQAL; IQKLKTLDMDQALN; QKLKTLDMDQALNP; KLKTLDMDQALNPN; LKTLDMDQALNPNH; KTLDMDQALNPNHN; TLDMDQALNPNHNA; LDMDQALNPNHNAL; DMDQALNPNHNALP; MDQALNPNHNALPK; DQALNPNHNALPKS; QALNPNHNALPKSQ; ALNPNHNALPKSQI; LNPNHNALPKSQIL; NPNHNALPKSQILQ; PNHNALPKSQILQP; NHNALPKSQILQPL; HNALPKSQILQPLL; NALPKSQILQPLLK; ALPKSQILQPLLKI; LPKSQILQPLLKIP; PKSQILQPLLKIPK; KSQILQPLLKIPKG; SQILQPLLKIPKGQ; QILQPLLKIPKGQT; ILQPLLKIPKGQTP; LQPLLKIPKGQTPI; QPLLKIPKGQTPIV; PLLKIPKGQTPIVK; LLKIPKGQTPIVKS; LKIPKGQTPIVKSC; KIPKGQTPIVKSCI; IPKGQTPIVKSCIC; PKGQTPIVKSCICV; KGQTPIVKSCICVK; GQTPIVKSCICVKA; QTPIVKSCICVKAF; TPIVKSCICVKAFS; PIVKSCICVKAFSV; IVKSCICVKAFSVL; VKSCICVKAFSVLK; KSCICVKAFSVLKG; SCICVKAFSVLKGL; CICVKAFSVLKGLK; ICVKAFSVLKGLKH; CVKAFSVLKGLKHH; VKAFSVLKGLKHHP; KAFSVLKGLKHHPQ; AFSVLKGLKHHPQN; FSVLKGLKHHPQNN; SVLKGLKHHPQNNT; VLKGLKHHPQNNTS; LKGLKHHPQNNTSL; KGLKHHPQNNTSLK; GLKHHPQNNTSLKV; LKHHPQNNTSLKVA; KHHPQNNTSLKVAY; HHPQNNTSLKVAYT; HPQNNTSLKVAYTK; PQNNTSLKVAYTKA; QNNTSLKVAYTKAA; NNTSLKVAYTKAAF; NTSLKVAYTKAAFI; TSLKVAYTKAAFIK; SLKVAYTKAAFIKC; LKVAYTKAAFIKCI; KVAYTKAAFIKCIC; VAYTKAAFIKCICT; AYTKAAFIKCICTI; YTKAAFIKCICTIK; TKAAFIKCICTIKA; KAAFIKCICTIKAP; AAFIKCICTIKAPV; SILVCNCPCLSIYL; ILVCNCPCLSIYLI; LVCNCPCLSIYLII; VCNCPCLSIYLIIS; CNCPCLSIYLIISG; NCPCLSIYLIISGS; CPCLSIYLIISGSP; PCLSIYLIISGSPG; CLSIYLIISGSPGS; LSIYLIISGSPGSL; SIYLIISGSPGSLS; IYLIISGSPGSLSV; YLIISGSPGSLSVP; LIISGSPGSLSVPS; IISGSPGSLSVPSN; ISGSPGSLSVPSNT; SGSPGSLSVPSNTL; GSPGSLSVPSNTLT; SPGSLSVPSNTLTS; PGSLSVPSNTLTSS; GSLSVPSNTLTSST; SLSVPSNTLTSSTW; LSVPSNTLTSSTWD; SVPSNTLTSSTWDS; VPSNTLTSSTWDSI; PSNTLTSSTWDSIP; SNTLTSSTWDSIPY; NTLTSSTWDSIPYI; TLTSSTWDSIPYIG; LTSSTWDSIPYIGC; TSSTWDSIPYIGCP; SSTWDSIPYIGCPS; STWDSIPYIGCPST; TWDSIPYIGCPSTL; WDSIPYIGCPSTLW; DSIPYIGCPSTLWV; SIPYIGCPSTLWVL; IPYIGCPSTLWVLL; PYIGCPSTLWVLLF; YIGCPSTLWVLLFI; IGCPSTLWVLLFIR; GCPSTLWVLLFIRS; CPSTLWVLLFIRSL; PSTLWVLLFIRSLS; STLWVLLFIRSLSK; TLWVLLFIRSLSKK; LWVLLFIRSLSKKE; WVLLFIRSLSKKEI; VLLFIRSLSKKEIG; GFFTDLFLRRILKY; FFTDLFLRRILKYL; FTDLFLRRILKYLA; TDLFLRRILKYLAR; DLFLRRILKYLARP; LFLRRILKYLARPL; FLRRILKYLARPLH; LRRILKYLARPLHC; RRILKYLARPLHCC; RILKYLARPLHCCV; ILKYLARPLHCCVP; LKYLARPLHCCVPE; KYLARPLHCCVPEL; YLARPLHCCVPELL; LARPLHCCVPELLV; ARPLHCCVPELLVN; RPLHCCVPELLVNR; PLHCCVPELLVNRP; LHCCVPELLVNRPQ; HCCVPELLVNRPQI; CCVPELLVNRPQIS; CVPELLVNRPQISA; VPELLVNRPQISAA; PELLVNRPQISAAE; ELLVNRPQISAAET; LLVNRPQISAAETY; LVNRPQISAAETYR; VNRPQISAAETYRL; NRPQISAAETYRLS; RPQISAAETYRLSA; PQISAAETYRLSAL; QISAAETYRLSALQ; ISAAETYRLSALQR; SAAETYRLSALQRG; AAETYRLSALQRGP; AETYRLSALQRGPT; ETYRLSALQRGPTP; TYRLSALQRGPTPC; YRLSALQRGPTPCS; RLSALQRGPTPCSS; LSALQRGPTPCSSS; SALQRGPTPCSSSN; ALQRGPTPCSSSNT; LQRGPTPCSSSNTV; QRGPTPCSSSNTVV; RGPTPCSSSNTVVA; GPTPCSSSNTVVAV; PTPCSSSNTVVAVL; TPCSSSNTVVAVLV; PCSSSNTVVAVLVT; STGGTFSPPVKVPK; TGGTFSPPVKVPKY; GGTFSPPVKVPKYL; GTFSPPVKVPKYLA; TFSPPVKVPKYLAF; FSPPVKVPKYLAFS; SPPVKVPKYLAFSF; PPVKVPKYLAFSFL; PVKVPKYLAFSFLL; VKVPKYLAFSFLLG; KVPKYLAFSFLLGS; VPKYLAFSFLLGSG; PKYLAFSFLLGSGT; KYLAFSFLLGSGTQ; YLAFSFLLGSGTQH; LAFSFLLGSGTQHS; AFSFLLGSGTQHST; FSFLLGSGTQHSTG; ALWSVFITWDWAVG; LWSVFITWDWAVGF; WSVFITWDWAVGFL; SVFITWDWAVGFLG; VFITWDWAVGFLGV; FITWDWAVGFLGVI; ITWDWAVGFLGVIV; TWDWAVGFLGVIVP; WDWAVGFLGVIVPS; DWAVGFLGVIVPSG; WAVGFLGVIVPSGY; AVGFLGVIVPSGYF; VGFLGVIVPSGYFD; GFLGVIVPSGYFDL; FISTPCISKGSPPT; ISTPCISKGSPPTA; STPCISKGSPPTAK; TPCISKGSPPTAKK; PCISKGSPPTAKKW; CISKGSPPTAKKWK; ISKGSPPTAKKWKL; SKGSPPTAKKWKLL; KGSPPTAKKWKLLP; IGFPPPCSCTFCDP; GFPPPCSCTFCDPA; RLSMLVIPITSVCT; LSMLVIPITSVCTV; SMLVIPITSVCTVT; MLVIPITSVCTVTA; LVIPITSVCTVTAS; VIPITSVCTVTASH; IPITSVCTVTASHI; PITSVCTVTASHIS; ITSVCTVTASHISR; TSVCTVTASHISRF; SVCTVTASHISRFP; VCTVTASHISRFPQ; CTVTASHISRFPQV; TVTASHISRFPQVR; VTASHISRFPQVRS; TASHISRFPQVRSS; ASHISRFPQVRSSF; SHISRFPQVRSSFK; HISRFPQVRSSFKL; ISRFPQVRSSFKLG; SRFPQVRSSFKLGR; RFPQVRSSFKLGRG; FPQVRSSFKLGRGI; PQVRSSFKLGRGIL; QVRSSFKLGRGILA; VRSSFKLGRGILAV; RSSFKLGRGILAVL; QGSIFLSGLSLLKS; GSIFLSGLSLLKSF; SIFLSGLSLLKSFS; IFLSGLSLLKSFSA; FLSGLSLLKSFSAL; LSGLSLLKSFSALS; SGLSLLKSFSALSF; GLSLLKSFSALSFR; LSLLKSFSALSFRL; SLLKSFSALSFRLK; LLKSFSALSFRLKP; LKSFSALSFRLKPL; KSFSALSFRLKPLR; SFSALSFRLKPLRF; FSALSFRLKPLRFS; SALSFRLKPLRFSS; ALSFRLKPLRFSSG; LSFRLKPLRFSSGS; SFRLKPLRFSSGSP; FRLKPLRFSSGSPI; RLKPLRFSSGSPIS; LKPLRFSSGSPISG; KPLRFSSGSPISGF; PLRFSSGSPISGFR; LRFSSGSPISGFRK; RFSSGSPISGFRKH; FSSGSPISGFRKHS; SSGSPISGFRKHST; SGSPISGFRKHSTS; GSPISGFRKHSTSV; SPISGFRKHSTSVI; PISGFRKHSTSVIA; ISGFRKHSTSVIAS; SGFRKHSTSVIAST; GFRKHSTSVIASTP; FRKHSTSVIASTPV; RKHSTSVIASTPVL; KHSTSVIASTPVLT; HSTSVIASTPVLTS; STSVIASTPVLTSR; TSVIASTPVLTSRT; SVIASTPVLTSRTS; VIASTPVLTSRTST; IASTPVLTSRTSTP; ASTPVLTSRTSTPP; STPVLTSRTSTPPF; TPVLTSRTSTPPFI; PVLTSRTSTPPFIS; VLTSRTSTPPFISS; LTSRTSTPPFISSF; TSRTSTPPFISSFG; SRTSTPPFISSFGT; RTSTPPFISSFGTC; TSTPPFISSFGTCT; STPPFISSFGTCTG; TPPFISSFGTCTGS; PPFISSFGTCTGSF; PFISSFGTCTGSFG; FISSFGTCTGSFGF; ISSFGTCTGSFGFL; SSFGTCTGSFGFLG; SFGTCTGSFGFLGA; FGTCTGSFGFLGAA; GTCTGSFGFLGAAP; TCTGSFGFLGAAPG; CTGSFGFLGAAPGH; TGSFGFLGAAPGHS; GSFGFLGAAPGHSP; SFGFLGAAPGHSPF; FGFLGAAPGHSPFL; GFLGAAPGHSPFLL; FLGAAPGHSPFLLV; LGAAPGHSPFLLVG; GAAPGHSPFLLVGA; AAPGHSPFLLVGAI; APGHSPFLLVGAIF; PGHSPFLLVGAIFI; GHSPFLLVGAIFIC; HSPFLLVGAIFICF; SPFLLVGAIFICFK; PFLLVGAIFICFKS; FLLVGAIFICFKSR; LLVGAIFICFKSRC; LVGAIFICFKSRCY; VGAIFICFKSRCYS; GAIFICFKSRCYSP; AIFICFKSRCYSPV; IFICFKSRCYSPVQ; FICFKSRCYSPVQA; RQHPLRSSSLISTS; QHPLRSSSLISTSW; HPLRSSSLISTSWG; PLRSSSLISTSWGN; LRSSSLISTSWGNS; RSSSLISTSWGNSF; SSSLISTSWGNSFF; SSLISTSWGNSFFY; SLISTSWGNSFFYK; LISTSWGNSFFYKL; ISTSWGNSFFYKLS; VHSLCNFFYTVSII; HSLCNFFYTVSIIY; SLCNFFYTVSIIYT; LCNFFYTVSIIYTI; CNFFYTVSIIYTIS; NFFYTVSIIYTISM; FFYTVSIIYTISMA; FYTVSIIYTISMAK; YTVSIIYTISMAKM; TVSIIYTISMAKMY; VSIIYTISMAKMYT; SIIYTISMAKMYTG; IIYTISMAKMYTGT; IYTISMAKMYTGTF; YTISMAKMYTGTFP; TISMAKMYTGTFPF; ISMAKMYTGTFPFS; SMAKMYTGTFPFSY; MAKMYTGTFPFSYL; AKMYTGTFPFSYLS; KMYTGTFPFSYLSN; MYTGTFPFSYLSNH; GPNRGKIRIILLNI; PNRGKIRIILLNII; NRGKIRIILLNIII; RGKIRIILLNIIIK; GKIRIILLNIIIKV; KIRIILLNIIIKVY; IRIILLNIIIKVYR; RIILLNIIIKVYRG; IILLNIIIKVYRGI; ILLNIIIKVYRGIY; LLNIIIKVYRGIYN; LNIIIKVYRGIYNC; NIIIKVYRGIYNCP; IIIKVYRGIYNCPG; IIKVYRGIYNCPGS; IKVYRGIYNCPGSF; KVYRGIYNCPGSFL; VYRGIYNCPGSFLQ; YRGIYNCPGSFLQK; RGIYNCPGSFLQKS; GIYNCPGSFLQKSS; IYNCPGSFLQKSSQ; YNCPGSFLQKSSQG; NCPGSFLQKSSQGV; CPGSFLQKSSQGVS; PGSFLQKSSQGVSK; GSFLQKSSQGVSKK; SFLQKSSQGVSKKS; FLQKSSQGVSKKSF; LQKSSQGVSKKSFC; QKSSQGVSKKSFCS; KSSQGVSKKSFCSS; SSQGVSKKSFCSSL; SQGVSKKSFCSSLQ; QGVSKKSFCSSLQF; GVSKKSFCSSLQFL; GYRRYIIPNNMPQS; YRRYIIPNNMPQSL; RRYIIPNNMPQSLG; RYIIPNNMPQSLGN; YIIPNNMPQSLGNS; IIPNNMPQSLGNSS; IPNNMPQSLGNSSK; PNNMPQSLGNSSKQ; NNMPQSLGNSSKQR; NMPQSLGNSSKQRR; MPQSLGNSSKQRRT; PQSLGNSSKQRRTP; QSLGNSSKQRRTPM; SLGNSSKQRRTPMP; LGNSSKQRRTPMPR; GNSSKQRRTPMPRI; NSSKQRRTPMPRIK; SSKQRRTPMPRIKV; SKQRRTPMPRIKVL; KQRRTPMPRIKVLN; QRRTPMPRIKVLNI; RRTPMPRIKVLNII; RTPMPRIKVLNIIN; TPMPRIKVLNIINK; PMPRIKVLNIINKS; MPRIKVLNIINKSI; PRIKVLNIINKSIY; RIKVLNIINKSIYT; IKVLNIINKSIYTR; KVLNIINKSIYTRK; VLNIINKSIYTRKQ; LNIINKSIYTRKQN; NIINKSIYTRKQNI; IINKSIYTRKQNII; INKSIYTRKQNIIV; NKSIYTRKQNIIVL; KSIYTRKQNIIVLI; SIYTRKQNIIVLIW; IYTRKQNIIVLIWV; YTRKQNIIVLIWVK; TRKQNIIVLIWVKQ; RKQNIIVLIWVKQF; KQNIIVLIWVKQFQ; QNIIVLIWVKQFQS; NIIVLIWVKQFQSH; IIVLIWVKQFQSHA; LLIEAYSGNFVIPI; LIEAYSGNFVIPII; IEAYSGNFVIPIIK; EAYSGNFVIPIIKE; AYSGNFVIPIIKEL; YSGNFVIPIIKELI; SGNFVIPIIKELIP; GNFVIPIIKELIPY; NFVIPIIKELIPYL; FVIPIIKELIPYLS; SSKPSNSPRSTSNY; SKPSNSPRSTSNYS; KPSNSPRSTSNYSI; PSNSPRSTSNYSIC; SNSPRSTSNYSICL; NSPRSTSNYSICLR; SPRSTSNYSICLRS; GTCYALYSSKGCNL; TCYALYSSKGCNLN; CYALYSSKGCNLNF; YALYSSKGCNLNFY; ALYSSKGCNLNFYS; LYSSKGCNLNFYSS; YSSKGCNLNFYSSS; SSKGCNLNFYSSSS; SKGCNLNFYSSSSL; KGCNLNFYSSSSLP; GCNLNFYSSSSLPS; CNLNFYSSSSLPSS; NLNFYSSSSLPSSN; LNFYSSSSLPSSNF; NFYSSSSLPSSNFS; FYSSSSLPSSNFSH; SSTHEPGNTKKKGL; STHEPGNTKKKGLL; THEPGNTKKKGLLT; ESFTESFTAGKAVV; SFTESFTAGKAVVL; FTESFTAGKAVVLL; TESFTAGKAVVLLF; ESFTAGKAVVLLFF; SFTAGKAVVLLFFP; FTAGKAVVLLFFPS; TAGKAVVLLFFPST; AGKAVVLLFFPSTL; GKAVVLLFFPSTLS; KAVVLLFFPSTLSS; AVVLLFFPSTLSSP; VVLLFFPSTLSSPL; VLLFFPSTLSSPLQ; LLFFPSTLSSPLQN; LFFPSTLSSPLQNS; FFPSTLSSPLQNSS; FPSTLSSPLQNSSK; PSTLSSPLQNSSKS; STLSSPLQNSSKSS; TLSSPLQNSSKSSK; LSSPLQNSSKSSKI; SSPLQNSSKSSKIK; SPLQNSSKSSKIKI; PLQNSSKSSKIKIK; LQNSSKSSKIKIKI; QNSSKSSKIKIKIL; ALFFVPVQVLPTFT; LFFVPVQVLPTFTE; FFVPVQVLPTFTEA; FVPVQVLPTFTEAC; VPVQVLPTFTEACR; PVQVLPTFTEACRD; VQVLPTFTEACRDS; QVLPTFTEACRDSW; VLPTFTEACRDSWR; LPTFTEACRDSWRR; PTFTEACRDSWRRT; TFTEACRDSWRRTM; FTEACRDSWRRTMA; TEACRDSWRRTMAF; EACRDSWRRTMAFV; ACRDSWRRTMAFVQ; CRDSWRRTMAFVQF; RDSWRRTMAFVQFN; DSWRRTMAFVQFNW; SWRRTMAFVQFNWG; WRRTMAFVQFNWGQ; RRTMAFVQFNWGQG; RTMAFVQFNWGQGQ; TMAFVQFNWGQGQD; MAFVQFNWGQGQDS; ARKTCLSCTFLPEV; RKTCLSCTFLPEVM; KTCLSCTFLPEVMV; TCLSCTFLPEVMVW; CLSCTFLPEVMVWL; LSCTFLPEVMVWLH; SCTFLPEVMVWLHS; CTFLPEVMVWLHSM; TFLPEVMVWLHSMG; FLPEVMVWLHSMGK; LPEVMVWLHSMGKQ; PEVMVWLHSMGKQL; EVMVWLHSMGKQLL; VMVWLHSMGKQLLP; MVWLHSMGKQLLPV; VWLHSMGKQLLPVS; WLHSMGKQLLPVSH; LHSMGKQLLPVSHA; HSMGKQLLPVSHAL; SMGKQLLPVSHALS; MGKQLLPVSHALSF; GKQLLPVSHALSFL; KQLLPVSHALSFLR; QLLPVSHALSFLRS; LLPVSHALSFLRSW; LPVSHALSFLRSWF; PVSHALSFLRSWFG; VSHALSFLRSWFGC; SHALSFLRSWFGCI; HALSFLRSWFGCIP; ALSFLRSWFGCIPL; GLAKLFGEIPILLQ; LAKLFGEIPILLQF; AKLFGEIPILLQFL; KLFGEIPILLQFLQ 15 mers: MDKVLNREESMELMD; DKVLNREESMELMDL; KVLNREESMELMDLL; VLNREESMELMDLLG; LNREESMELMDLLGL; NREESMELMDLLGLE; REESMELMDLLGLER; EESMELMDLLGLERA; ESMELMDLLGLERAA; SMELMDLLGLERAAW; MELMDLLGLERAAWG; ELMDLLGLERAAWGN; LMDLLGLERAAWGNL; MDLLGLERAAWGNLP; DLLGLERAAWGNLPL; LLGLERAAWGNLPLM; LGLERAAWGNLPLMR; GLERAAWGNLPLMRK; LERAAWGNLPLMRKA; ERAAWGNLPLMRKAY; RAAWGNLPLMRKAYL; AAWGNLPLMRKAYLR; AWGNLPLMRKAYLRK; WGNLPLMRKAYLRKC; GNLPLMRKAYLRKCK; NLPLMRKAYLRKCKE; LPLMRKAYLRKCKEF; PLMRKAYLRKCKEFH; LMRKAYLRKCKEFHP; MRKAYLRKCKEFHPD; RKAYLRKCKEFHPDK; KAYLRKCKEFHPDKG; AYLRKCKEFHPDKGG; YLRKCKEFHPDKGGD; LRKCKEFHPDKGGDE; RKCKEFHPDKGGDED; KCKEFHPDKGGDEDK; CKEFHPDKGGDEDKM; KEFHPDKGGDEDKMK; EFHPDKGGDEDKMKR; FHPDKGGDEDKMKRM; HPDKGGDEDKMKRMN; PDKGGDEDKMKRMNT; DKGGDEDKMKRMNTL; KGGDEDKMKRMNTLY; GGDEDKMKRMNTLYK; GDEDKMKRMNTLYKK; DEDKMKRMNTLYKKM; EDKMKRMNTLYKKME; DKMKRMNTLYKKMEQ; KMKRMNTLYKKMEQD; MKRMNTLYKKMEQDV; KRMNTLYKKMEQDVK; RMNTLYKKMEQDVKV; MNTLYKKMEQDVKVA; NTLYKKMEQDVKVAH; TLYKKMEQDVKVAHQ; LYKKMEQDVKVAHQP; YKKMEQDVKVAHQPD; KKMEQDVKVAHQPDF; KMEQDVKVAHQPDFG; MEQDVKVAHQPDFGT; EQDVKVAHQPDFGTW; QDVKVAHQPDFGTWS; DVKVAHQPDFGTWSS; VKVAHQPDFGTWSSS; KVAHQPDFGTWSSSE; VAHQPDFGTWSSSEV; AHQPDFGTWSSSEVC; HQPDFGTWSSSEVCA; QPDFGTWSSSEVCAD; PDFGTWSSSEVCADF; DFGTWSSSEVCADFP; FGTWSSSEVCADFPL; GTWSSSEVCADFPLC; TWSSSEVCADFPLCP; WSSSEVCADFPLCPD; SSSEVCADFPLCPDT; SSEVCADFPLCPDTL; SEVCADFPLCPDTLY; EVCADFPLCPDTLYC; VCADFPLCPDTLYCK; CADFPLCPDTLYCKE; ADFPLCPDTLYCKEW; DFPLCPDTLYCKEWP; FPLCPDTLYCKEWPI; PLCPDTLYCKEWPIC; LCPDTLYCKEWPICS; CPDTLYCKEWPICSK; PDTLYCKEWPICSKK; DTLYCKEWPICSKKP; TLYCKEWPICSKKPS; LYCKEWPICSKKPSV; YCKEWPICSKKPSVH; CKEWPICSKKPSVHC; KEWPICSKKPSVHCP; EWPICSKKPSVHCPC; WPICSKKPSVHCPCM; PICSKKPSVHCPCML; ICSKKPSVHCPCMLC; CSKKPSVHCPCMLCQ; SKKPSVHCPCMLCQL; KKPSVHCPCMLCQLR; KPSVHCPCMLCQLRL; PSVHCPCMLCQLRLR; SVHCPCMLCQLRLRH; VHCPCMLCQLRLRHL; HCPCMLCQLRLRHLN; CPCMLCQLRLRHLNR; PCMLCQLRLRHLNRK; CMLCQLRLRHLNRKF; MLCQLRLRHLNRKFL; LCQLRLRHLNRKFLR; CQLRLRHLNRKFLRK; QLRLRHLNRKFLRKE; LRLRHLNRKFLRKEP; RLRHLNRKFLRKEPL; LRHLNRKFLRKEPLV; RHLNRKFLRKEPLVW; HLNRKFLRKEPLVWI; LNRKFLRKEPLVWID; NRKFLRKEPLVWIDC; RKFLRKEPLVWIDCY; KFLRKEPLVWIDCYC; FLRKEPLVWIDCYCI; LRKEPLVWIDCYCID; RKEPLVWIDCYCIDC; KEPLVWIDCYCIDCF; EPLVWIDCYCIDCFT; PLVWIDCYCIDCFTQ; LVWIDCYCIDCFTQW; VWIDCYCIDCFTQWF; WIDCYCIDCFTQWFG; IDCYCIDCFTQWFGL; DCYCIDCFTQWFGLD; CYCIDCFTQWFGLDL; YCIDCFTQWFGLDLT; CIDCFTQWFGLDLTE; IDCFTQWFGLDLTEE; DCFTQWFGLDLTEET; CFTQWFGLDLTEETL; FTQWFGLDLTEETLQ; TQWFGLDLTEETLQW; QWFGLDLTEETLQWW; WFGLDLTEETLQWWV; FGLDLTEETLQWWVQ; GLDLTEETLQWWVQI; LDLTEETLQWWVQII; DLTEETLQWWVQIIG; LTEETLQWWVQIIGE; TEETLQWWVQIIGET; EETLQWWVQIIGETP; ETLQWWVQIIGETPF; TLQWWVQIIGETPFR; LQWWVQIIGETPFRD; QWWVQIIGETPFRDL; WWVQIIGETPFRDLK; WVQIIGETPFRDLKL; KALSNYFFYRCQPME; ALSNYFFYRCQPMEQ; LSNYFFYRCQPMEQK; SNYFFYRCQPMEQKS; NYFFYRCQPMEQKSG; YFFYRCQPMEQKSGS; FFYRCQPMEQKSGSP; FYRCQPMEQKSGSPG; YRCQPMEQKSGSPGG; RCQPMEQKSGSPGGV; CQPMEQKSGSPGGVP; QPMEQKSGSPGGVPL; PMEQKSGSPGGVPLM; MEQKSGSPGGVPLMK; EQKSGSPGGVPLMKN; QKSGSPGGVPLMKNG; KSGSPGGVPLMKNGM; SGSPGGVPLMKNGMK; GSPGGVPLMKNGMKI; SPGGVPLMKNGMKIY; PGGVPLMKNGMKIYF; GGVPLMKNGMKIYFA; GVPLMKNGMKIYFAM; VPLMKNGMKIYFAMK; PLMKNGMKIYFAMKI; LMKNGMKIYFAMKIC; MKNGMKIYFAMKICL; KNGMKIYFAMKICLP; NGMKIYFAMKICLPV; GMKIYFAMKICLPVM; MKIYFAMKICLPVMK; KIYFAMKICLPVMKK; IYFAMKICLPVMKKQ; YFAMKICLPVMKKQQ; FAMKICLPVMKKQQQ; AMKICLPVMKKQQQI; MKICLPVMKKQQQIL; KICLPVMKKQQQILN; ICLPVMKKQQQILNT; CLPVMKKQQQILNTQ; LPVMKKQQQILNTQH; PVMKKQQQILNTQHH; VMKKQQQILNTQHHP; MKKQQQILNTQHHPK; KKQQQILNTQHHPKK; KQQQILNTQHHPKKK; QQQILNTQHHPKKKE; QQILNTQHHPKKKER; KTLKTFPLIYTSFLV; TLKTFPLIYTSFLVK; LKTFPLIYTSFLVKL; KTFPLIYTSFLVKLY; TFPLIYTSFLVKLYL; FPLIYTSFLVKLYLV; PLIYTSFLVKLYLVI; LIYTSFLVKLYLVIE; IYTSFLVKLYLVIEP; YTSFLVKLYLVIEPL; TSFLVKLYLVIEPLP; SFLVKLYLVIEPLPA; FLVKLYLVIEPLPAL; LVKLYLVIEPLPALL; VKLYLVIEPLPALLC; KLYLVIEPLPALLCI; LYLVIEPLPALLCIL; YLVIEPLPALLCILL; LVIEPLPALLCILLK; VIEPLPALLCILLKK; IEPLPALLCILLKKK; EPLPALLCILLKKKL; PLPALLCILLKKKLK; LPALLCILLKKKLKF; PALLCILLKKKLKFC; ALLCILLKKKLKFCI; LLCILLKKKLKFCIK; LCILLKKKLKFCIKN; CILLKKKLKFCIKNL; ILLKKKLKFCIKNLW; LLKKKLKFCIKNLWK; LKKKLKFCIKNLWKN; KKKLKFCIKNLWKNI; KKLKFCIKNLWKNIL; LLLVDTCVLGIILYS; LLVDTCVLGIILYSF; LHIDIEFLQLIISVK; HIDIEFLQLIISVKS; IDIEFLQLIISVKSC; DIEFLQLIISVKSCV; IEFLQLIISVKSCVP; EFLQLIISVKSCVPL; FLQLIISVKSCVPLV; LQLIISVKSCVPLVF; RSMILAQKSLKKQSR; SMILAQKSLKKQSRC; MILAQKSLKKQSRCL; ILAQKSLKKQSRCLG; LAQKSLKKQSRCLGN; RSVKSVRKKTSLITL; SVKSVRKKTSLITLS; VKSVRKKTSLITLSI; KSVRKKTSLITLSIM; SVRKKTSLITLSIMK; VRKKTSLITLSIMKS; RKKTSLITLSIMKST; KKTSLITLSIMKSTL; KTSLITLSIMKSTLQ; TSLITLSIMKSTLQM; SLITLSIMKSTLQML; LITLSIMKSTLQMLL; ITLSIMKSTLQMLLF; TLSIMKSTLQMLLFL; LSIMKSTLQMLLFLQ; SIMKSTLQMLLFLQK; IMKSTLQMLLFLQKV; MKSTLQMLLFLQKVK; KSTLQMLLFLQKVKI; STLQMLLFLQKVKIK; TLQMLLFLQKVKIKK; LQMLLFLQKVKIKKV; QMLLFLQKVKIKKVF; MLLFLQKVKIKKVFV; LLFLQKVKIKKVFVS; LFLQKVKIKKVFVSK; FLQKVKIKKVFVSKQ; NNIWQVLLGCTVCYL; NIWQVLLGCTVCYLK; IWQVLLGCTVCYLKW; WQVLLGCTVCYLKWI; QVLLGCTVCYLKWIL; YLIFCTVLFSMYLKE; LIFCTVLFSMYLKED; IFCTVLFSMYLKEDT; FCTVLFSMYLKEDTG; CTVLFSMYLKEDTGY; TVLFSMYLKEDTGYL; VLFSMYLKEDTGYLK; LFSMYLKEDTGYLKV; FSMYLKEDTGYLKVP; SMYLKEDTGYLKVPL; MYLKEDTGYLKVPLI; YLKEDTGYLKVPLIV; LKEDTGYLKVPLIVE; KEDTGYLKVPLIVEK; EDTGYLKVPLIVEKQ; DTGYLKVPLIVEKQH; KGQELNQRICLQDME; ENPYKTQSSYLKKEF; NPYKTQSSYLKKEFY; PYKTQSSYLKKEFYK; YKTQSSYLKKEFYKV; KTQSSYLKKEFYKVE; LILQLIYNLELLNGR; ILQLIYNLELLNGRK; LQLIYNLELLNGRKG; QLIYNLELLNGRKGW; LIYNLELLNGRKGWI; IYNLELLNGRKGWIL; YNLELLNGRKGWILR; NIIYAWGNVFLILQE; IIYAWGNVFLILQEK; IYAWGNVFLILQEKR; YAWGNVFLILQEKRI; AWGNVFLILQEKRIQ; WGNVFLILQEKRIQK; GNVFLILQEKRIQKL; NVFLILQEKRIQKLK; VFLILQEKRIQKLKT; FLILQEKRIQKLKTL; LILQEKRIQKLKTLD; ILQEKRIQKLKTLDM; LQEKRIQKLKTLDMD; QEKRIQKLKTLDMDQ; EKRIQKLKTLDMDQA; KRIQKLKTLDMDQAL; RIQKLKTLDMDQALN; IQKLKTLDMDQALNP; QKLKTLDMDQALNPN; KLKTLDMDQALNPNH; LKTLDMDQALNPNHN; KTLDMDQALNPNHNA; TLDMDQALNPNHNAL; LDMDQALNPNHNALP; DMDQALNPNHNALPK; MDQALNPNHNALPKS; DQALNPNHNALPKSQ; QALNPNHNALPKSQI; ALNPNHNALPKSQIL; LNPNHNALPKSQILQ; NPNHNALPKSQILQP; PNHNALPKSQILQPL; NHNALPKSQILQPLL; HNALPKSQILQPLLK; NALPKSQILQPLLKI; ALPKSQILQPLLKIP; LPKSQILQPLLKIPK; PKSQILQPLLKIPKG; KSQILQPLLKIPKGQ; SQILQPLLKIPKGQT; QILQPLLKIPKGQTP; ILQPLLKIPKGQTPI; LQPLLKIPKGQTPIV; QPLLKIPKGQTPIVK; PLLKIPKGQTPIVKS; LLKIPKGQTPIVKSC; LKIPKGQTPIVKSCI; KIPKGQTPIVKSCIC; IPKGQTPIVKSCICV; PKGQTPIVKSCICVK; KGQTPIVKSCICVKA; GQTPIVKSCICVKAF; QTPIVKSCICVKAFS; TPIVKSCICVKAFSV; PIVKSCICVKAFSVL; IVKSCICVKAFSVLK; VKSCICVKAFSVLKG; KSCICVKAFSVLKGL; SCICVKAFSVLKGLK; CICVKAFSVLKGLKH; ICVKAFSVLKGLKHH; CVKAFSVLKGLKHHP; VKAFSVLKGLKHHPQ; KAFSVLKGLKHHPQN; AFSVLKGLKHHPQNN; FSVLKGLKHHPQNNT; SVLKGLKHHPQNNTS; VLKGLKHHPQNNTSL; LKGLKHHPQNNTSLK; KGLKHHPQNNTSLKV; GLKHHPQNNTSLKVA; LKHHPQNNTSLKVAY; KHHPQNNTSLKVAYT; HHPQNNTSLKVAYTK; HPQNNTSLKVAYTKA; PQNNTSLKVAYTKAA; QNNTSLKVAYTKAAF; NNTSLKVAYTKAAFI; NTSLKVAYTKAAFIK; TSLKVAYTKAAFIKC; SLKVAYTKAAFIKCI; LKVAYTKAAFIKCIC; KVAYTKAAFIKCICT; VAYTKAAFIKCICTI; AYTKAAFIKCICTIK; YTKAAFIKCICTIKA; TKAAFIKCICTIKAP; KAAFIKCICTIKAPV; SILVCNCPCLSIYLI; ILVCNCPCLSIYLII; LVCNCPCLSIYLIIS; VCNCPCLSIYLIISG; CNCPCLSIYLIISGS; NCPCLSIYLIISGSP; CPCLSIYLIISGSPG; PCLSIYLIISGSPGS; CLSIYLIISGSPGSL; LSIYLIISGSPGSLS; SIYLIISGSPGSLSV; IYLIISGSPGSLSVP; YLIISGSPGSLSVPS; LIISGSPGSLSVPSN; IISGSPGSLSVPSNT; ISGSPGSLSVPSNTL; SGSPGSLSVPSNTLT; GSPGSLSVPSNTLTS; SPGSLSVPSNTLTSS; PGSLSVPSNTLTSST; GSLSVPSNTLTSSTW; SLSVPSNTLTSSTWD; LSVPSNTLTSSTWDS; SVPSNTLTSSTWDSI; VPSNTLTSSTWDSIP; PSNTLTSSTWDSIPY; SNTLTSSTWDSIPYI; NTLTSSTWDSIPYIG; TLTSSTWDSIPYIGC; LTSSTWDSIPYIGCP; TSSTWDSIPYIGCPS; SSTWDSIPYIGCPST; STWDSIPYIGCPSTL; TWDSIPYIGCPSTLW; WDSIPYIGCPSTLWV; DSIPYIGCPSTLWVL; SIPYIGCPSTLWVLL; IPYIGCPSTLWVLLF; PYIGCPSTLWVLLFI; YIGCPSTLWVLLFIR; IGCPSTLWVLLFIRS; GCPSTLWVLLFIRSL; CPSTLWVLLFIRSLS; PSTLWVLLFIRSLSK; STLWVLLFIRSLSKK; TLWVLLFIRSLSKKE; LWVLLFIRSLSKKEI; WVLLFIRSLSKKEIG; GFFTDLFLRRILKYL; FFTDLFLRRILKYLA; FTDLFLRRILKYLAR; TDLFLRRILKYLARP; DLFLRRILKYLARPL; LFLRRILKYLARPLH; FLRRILKYLARPLHC; LRRILKYLARPLHCC; RRILKYLARPLHCCV; RILKYLARPLHCCVP; ILKYLARPLHCCVPE; LKYLARPLHCCVPEL; KYLARPLHCCVPELL; YLARPLHCCVPELLV; LARPLHCCVPELLVN; ARPLHCCVPELLVNR; RPLHCCVPELLVNRP; PLHCCVPELLVNRPQ; LHCCVPELLVNRPQI; HCCVPELLVNRPQIS; CCVPELLVNRPQISA; CVPELLVNRPQISAA; VPELLVNRPQISAAE; PELLVNRPQISAAET; ELLVNRPQISAAETY; LLVNRPQISAAETYR; LVNRPQISAAETYRL; VNRPQISAAETYRLS; NRPQISAAETYRLSA; RPQISAAETYRLSAL; PQISAAETYRLSALQ; QISAAETYRLSALQR; ISAAETYRLSALQRG; SAAETYRLSALQRGP; AAETYRLSALQRGPT; AETYRLSALQRGPTP; ETYRLSALQRGPTPC; TYRLSALQRGPTPCS; YRLSALQRGPTPCSS; RLSALQRGPTPCSSS; LSALQRGPTPCSSSN; SALQRGPTPCSSSNT; ALQRGPTPCSSSNTV; LQRGPTPCSSSNTVV; QRGPTPCSSSNTVVA; RGPTPCSSSNTVVAV; GPTPCSSSNTVVAVL; PTPCSSSNTVVAVLV; TPCSSSNTVVAVLVT; STGGTFSPPVKVPKY; TGGTFSPPVKVPKYL; GGTFSPPVKVPKYLA; GTFSPPVKVPKYLAF; TFSPPVKVPKYLAFS; FSPPVKVPKYLAFSF; SPPVKVPKYLAFSFL; PPVKVPKYLAFSFLL; PVKVPKYLAFSFLLG; VKVPKYLAFSFLLGS; KVPKYLAFSFLLGSG; VPKYLAFSFLLGSGT; PKYLAFSFLLGSGTQ; KYLAFSFLLGSGTQH; YLAFSFLLGSGTQHS; LAFSFLLGSGTQHST; AFSFLLGSGTQHSTG; ALWSVFITWDWAVGF; LWSVFITWDWAVGFL; WSVFITWDWAVGFLG; SVFITWDWAVGFLGV; VFITWDWAVGFLGVI; FITWDWAVGFLGVIV; ITWDWAVGFLGVIVP; TWDWAVGFLGVIVPS; WDWAVGFLGVIVPSG; DWAVGFLGVIVPSGY; WAVGFLGVIVPSGYF; AVGFLGVIVPSGYFD; VGFLGVIVPSGYFDL; FISTPCISKGSPPTA; ISTPCISKGSPPTAK; STPCISKGSPPTAKK; TPCISKGSPPTAKKW; PCISKGSPPTAKKWK; CISKGSPPTAKKWKL; ISKGSPPTAKKWKLL; SKGSPPTAKKWKLLP; IGFPPPCSCTFCDPA; RLSMLVIPITSVCTV; LSMLVIPITSVCTVT; SMLVIPITSVCTVTA; MLVIPITSVCTVTAS; LVIPITSVCTVTASH; VIPITSVCTVTASHI; IPITSVCTVTASHIS; PITSVCTVTASHISR; ITSVCTVTASHISRF; TSVCTVTASHISRFP; SVCTVTASHISRFPQ; VCTVTASHISRFPQV; CTVTASHISRFPQVR; TVTASHISRFPQVRS; VTASHISRFPQVRSS; TASHISRFPQVRSSF; ASHISRFPQVRSSFK; SHISRFPQVRSSFKL; HISRFPQVRSSFKLG; ISRFPQVRSSFKLGR; SRFPQVRSSFKLGRG; RFPQVRSSFKLGRGI; FPQVRSSFKLGRGIL; PQVRSSFKLGRGILA; QVRSSFKLGRGILAV; VRSSFKLGRGILAVL; QGSIFLSGLSLLKSF; GSIFLSGLSLLKSFS; SIFLSGLSLLKSFSA; IFLSGLSLLKSFSAL; FLSGLSLLKSFSALS; LSGLSLLKSFSALSF; SGLSLLKSFSALSFR; GLSLLKSFSALSFRL; LSLLKSFSALSFRLK; SLLKSFSALSFRLKP; LLKSFSALSFRLKPL; LKSFSALSFRLKPLR; KSFSALSFRLKPLRF; SFSALSFRLKPLRFS; FSALSFRLKPLRFSS; SALSFRLKPLRFSSG; ALSFRLKPLRFSSGS; LSFRLKPLRFSSGSP; SFRLKPLRFSSGSPI; FRLKPLRFSSGSPIS; RLKPLRFSSGSPISG; LKPLRFSSGSPISGF; KPLRFSSGSPISGFR; PLRFSSGSPISGFRK; LRFSSGSPISGFRKH; RFSSGSPISGFRKHS; FSSGSPISGFRKHST; SSGSPISGFRKHSTS; SGSPISGFRKHSTSV; GSPISGFRKHSTSVI; SPISGFRKHSTSVIA; PISGFRKHSTSVIAS; ISGFRKHSTSVIAST; SGFRKHSTSVIASTP; GFRKHSTSVIASTPV; FRKHSTSVIASTPVL; RKHSTSVIASTPVLT; KHSTSVIASTPVLTS; HSTSVIASTPVLTSR; STSVIASTPVLTSRT; TSVIASTPVLTSRTS; SVIASTPVLTSRTST; VIASTPVLTSRTSTP; IASTPVLTSRTSTPP; ASTPVLTSRTSTPPF; STPVLTSRTSTPPFI; TPVLTSRTSTPPFIS; PVLTSRTSTPPFISS; VLTSRTSTPPFISSF; LTSRTSTPPFISSFG; TSRTSTPPFISSFGT; SRTSTPPFISSFGTC; RTSTPPFISSFGTCT; TSTPPFISSFGTCTG; STPPFISSFGTCTGS; TPPFISSFGTCTGSF; PPFISSFGTCTGSFG; PFISSFGTCTGSFGF; FISSFGTCTGSFGFL; ISSFGTCTGSFGFLG; SSFGTCTGSFGFLGA; SFGTCTGSFGFLGAA; FGTCTGSFGFLGAAP; GTCTGSFGFLGAAPG; TCTGSFGFLGAAPGH; CTGSFGFLGAAPGHS; TGSFGFLGAAPGHSP; GSFGFLGAAPGHSPF; SFGFLGAAPGHSPFL; FGFLGAAPGHSPFLL; GFLGAAPGHSPFLLV; FLGAAPGHSPFLLVG; LGAAPGHSPFLLVGA; GAAPGHSPFLLVGAI; AAPGHSPFLLVGAIF; APGHSPFLLVGAIFI; PGHSPFLLVGAIFIC; GHSPFLLVGAIFICF; HSPFLLVGAIFICFK; SPFLLVGAIFICFKS; PFLLVGAIFICFKSR; FLLVGAIFICFKSRC; LLVGAIFICFKSRCY; LVGAIFICFKSRCYS; VGAIFICFKSRCYSP; GAIFICFKSRCYSPV; AIFICFKSRCYSPVQ; IFICFKSRCYSPVQA; RQHPLRSSSLISTSW; QHPLRSSSLISTSWG; HPLRSSSLISTSWGN; PLRSSSLISTSWGNS; LRSSSLISTSWGNSF; RSSSLISTSWGNSFF; SSSLISTSWGNSFFY; SSLISTSWGNSFFYK; SLISTSWGNSFFYKL; LISTSWGNSFFYKLS; VHSLCNFFYTVSIIY; HSLCNFFYTVSIIYT; SLCNFFYTVSIIYTI; LCNFFYTVSIIYTIS; CNFFYTVSIIYTISM; NFFYTVSIIYTISMA; FFYTVSIIYTISMAK; FYTVSIIYTISMAKM; YTVSIIYTISMAKMY; TVSIIYTISMAKMYT; VSIIYTISMAKMYTG; SIIYTISMAKMYTGT; IIYTISMAKMYTGTF; IYTISMAKMYTGTFP; YTISMAKMYTGTFPF; TISMAKMYTGTFPFS; ISMAKMYTGTFPFSY; SMAKMYTGTFPFSYL; MAKMYTGTFPFSYLS; AKMYTGTFPFSYLSN; KMYTGTFPFSYLSNH; GPNRGKIRIILLNII; PNRGKIRIILLNIII; NRGKIRIILLNIIIK; RGKIRIILLNIIIKV; GKIRIILLNIIIKVY; KIRIILLNIIIKVYR; IRIILLNIIIKVYRG; RIILLNIIIKVYRGI; IILLNIIIKVYRGIY; ILLNIIIKVYRGIYN; LLNIIIKVYRGIYNC; LNIIIKVYRGIYNCP; NIIIKVYRGIYNCPG; IIIKVYRGIYNCPGS; IIKVYRGIYNCPGSF; IKVYRGIYNCPGSFL; KVYRGIYNCPGSFLQ; VYRGIYNCPGSFLQK; YRGIYNCPGSFLQKS; RGIYNCPGSFLQKSS; GIYNCPGSFLQKSSQ; IYNCPGSFLQKSSQG; YNCPGSFLQKSSQGV; NCPGSFLQKSSQGVS; CPGSFLQKSSQGVSK; PGSFLQKSSQGVSKK; GSFLQKSSQGVSKKS; SFLQKSSQGVSKKSF; FLQKSSQGVSKKSFC; LQKSSQGVSKKSFCS; QKSSQGVSKKSFCSS; KSSQGVSKKSFCSSL; SSQGVSKKSFCSSLQ; SQGVSKKSFCSSLQF; QGVSKKSFCSSLQFL; GYRRYIIPNNMPQSL; YRRYIIPNNMPQSLG; RRYIIPNNMPQSLGN; RYIIPNNMPQSLGNS; YIIPNNMPQSLGNSS; IIPNNMPQSLGNSSK; IPNNMPQSLGNSSKQ; PNNMPQSLGNSSKQR; NNMPQSLGNSSKQRR; NMPQSLGNSSKQRRT; MPQSLGNSSKQRRTP; PQSLGNSSKQRRTPM; QSLGNSSKQRRTPMP; SLGNSSKQRRTPMPR; LGNSSKQRRTPMPRI; GNSSKQRRTPMPRIK; NSSKQRRTPMPRIKV; SSKQRRTPMPRIKVL; SKQRRTPMPRIKVLN; KQRRTPMPRIKVLNI; QRRTPMPRIKVLNII; RRTPMPRIKVLNIIN; RTPMPRIKVLNIINK; TPMPRIKVLNIINKS; PMPRIKVLNIINKSI; MPRIKVLNIINKSIY; PRIKVLNIINKSIYT; RIKVLNIINKSIYTR; IKVLNIINKSIYTRK; KVLNIINKSIYTRKQ; VLNIINKSIYTRKQN; LNIINKSIYTRKQNI; NIINKSIYTRKQNII; IINKSIYTRKQNIIV; INKSIYTRKQNIIVL; NKSIYTRKQNIIVLI; KSIYTRKQNIIVLIW; SIYTRKQNIIVLIWV; IYTRKQNIIVLIWVK; YTRKQNIIVLIWVKQ; TRKQNIIVLIWVKQF; RKQNIIVLIWVKQFQ; KQNIIVLIWVKQFQS; QNIIVLIWVKQFQSH; NIIVLIWVKQFQSHA; LLIEAYSGNFVIPII; LIEAYSGNFVIPIIK; IEAYSGNFVIPIIKE; EAYSGNFVIPIIKEL; AYSGNFVIPIIKELI; YSGNFVIPIIKELIP; SGNFVIPIIKELIPY; GNFVIPIIKELIPYL; NFVIPIIKELIPYLS; SSKPSNSPRSTSNYS; SKPSNSPRSTSNYSI; KPSNSPRSTSNYSIC; PSNSPRSTSNYSICL; SNSPRSTSNYSICLR; NSPRSTSNYSICLRS; GTCYALYSSKGCNLN; TCYALYSSKGCNLNF; CYALYSSKGCNLNFY; YALYSSKGCNLNFYS; ALYSSKGCNLNFYSS; LYSSKGCNLNFYSSS; YSSKGCNLNFYSSSS; SSKGCNLNFYSSSSL; SKGCNLNFYSSSSLP; KGCNLNFYSSSSLPS; GCNLNFYSSSSLPSS; CNLNFYSSSSLPSSN; NLNFYSSSSLPSSNF; LNFYSSSSLPSSNFS; NFYSSSSLPSSNFSH; SSTHEPGNTKKKGLL; STHEPGNTKKKGLLT; ESFTESFTAGKAVVL; SFTESFTAGKAVVLL; FTESFTAGKAVVLLF; TESFTAGKAVVLLFF; ESFTAGKAVVLLFFP; SFTAGKAVVLLFFPS; FTAGKAVVLLFFPST; TAGKAVVLLFFPSTL; AGKAVVLLFFPSTLS; GKAVVLLFFPSTLSS; KAVVLLFFPSTLSSP; AVVLLFFPSTLSSPL; VVLLFFPSTLSSPLQ; VLLFFPSTLSSPLQN; LLFFPSTLSSPLQNS; LFFPSTLSSPLQNSS; FFPSTLSSPLQNSSK; FPSTLSSPLQNSSKS; PSTLSSPLQNSSKSS; STLSSPLQNSSKSSK; TLSSPLQNSSKSSKI; LSSPLQNSSKSSKIK; SSPLQNSSKSSKIKI; SPLQNSSKSSKIKIK; PLQNSSKSSKIKIKI; LQNSSKSSKIKIKIL; ALFFVPVQVLPTFTE; LFFVPVQVLPTFTEA; FFVPVQVLPTFTEAC; FVPVQVLPTFTEACR; VPVQVLPTFTEACRD; PVQVLPTFTEACRDS; VQVLPTFTEACRDSW; QVLPTFTEACRDSWR; VLPTFTEACRDSWRR; LPTFTEACRDSWRRT; PTFTEACRDSWRRTM; TFTEACRDSWRRTMA; FTEACRDSWRRTMAF; TEACRDSWRRTMAFV; EACRDSWRRTMAFVQ; ACRDSWRRTMAFVQF; CRDSWRRTMAFVQFN; RDSWRRTMAFVQFNW; DSWRRTMAFVQFNWG; SWRRTMAFVQFNWGQ; WRRTMAFVQFNWGQG; RRTMAFVQFNWGQGQ; RTMAFVQFNWGQGQD; TMAFVQFNWGQGQDS; ARKTCLSCTFLPEVM; RKTCLSCTFLPEVMV; KTCLSCTFLPEVMVW; TCLSCTFLPEVMVWL; CLSCTFLPEVMVWLH; LSCTFLPEVMVWLHS; SCTFLPEVMVWLHSM; CTFLPEVMVWLHSMG; TFLPEVMVWLHSMGK; FLPEVMVWLHSMGKQ; LPEVMVWLHSMGKQL; PEVMVWLHSMGKQLL; EVMVWLHSMGKQLLP; VMVWLHSMGKQLLPV; MVWLHSMGKQLLPVS; VWLHSMGKQLLPVSH; WLHSMGKQLLPVSHA; LHSMGKQLLPVSHAL; HSMGKQLLPVSHALS; SMGKQLLPVSHALSF; MGKQLLPVSHALSFL; GKQLLPVSHALSFLR; KQLLPVSHALSFLRS; QLLPVSHALSFLRSW; LLPVSHALSFLRSWF; LPVSHALSFLRSWFG; PVSHALSFLRSWFGC; VSHALSFLRSWFGCI; SHALSFLRSWFGCIP; HALSFLRSWFGCIPL; GLAKLFGEIPILLQF; LAKLFGEIPILLQFL; AKLFGEIPILLQFLQ 16 mers: MDKVLNREESMELMDL; DKVLNREESMELMDLL; KVLNREESMELMDLLG; VLNREESMELMDLLGL; LNREESMELMDLLGLE; NREESMELMDLLGLER; REESMELMDLLGLERA; EESMELMDLLGLERAA; ESMELMDLLGLERAAW; SMELMDLLGLERAAWG; MELMDLLGLERAAWGN; ELMDLLGLERAAWGNL; LMDLLGLERAAWGNLP; MDLLGLERAAWGNLPL; DLLGLERAAWGNLPLM; LLGLERAAWGNLPLMR; LGLERAAWGNLPLMRK; GLERAAWGNLPLMRKA; LERAAWGNLPLMRKAY; ERAAWGNLPLMRKAYL; RAAWGNLPLMRKAYLR; AAWGNLPLMRKAYLRK; AWGNLPLMRKAYLRKC; WGNLPLMRKAYLRKCK; GNLPLMRKAYLRKCKE; NLPLMRKAYLRKCKEF; LPLMRKAYLRKCKEFH; PLMRKAYLRKCKEFHP; LMRKAYLRKCKEFHPD; MRKAYLRKCKEFHPDK; RKAYLRKCKEFHPDKG; KAYLRKCKEFHPDKGG; AYLRKCKEFHPDKGGD; YLRKCKEFHPDKGGDE; LRKCKEFHPDKGGDED; RKCKEFHPDKGGDEDK; KCKEFHPDKGGDEDKM; CKEFHPDKGGDEDKMK; KEFHPDKGGDEDKMKR; EFHPDKGGDEDKMKRM; FHPDKGGDEDKMKRMN; HPDKGGDEDKMKRMNT; PDKGGDEDKMKRMNTL; DKGGDEDKMKRMNTLY; KGGDEDKMKRMNTLYK; GGDEDKMKRMNTLYKK; GDEDKMKRMNTLYKKM; DEDKMKRMNTLYKKME; EDKMKRMNTLYKKMEQ; DKMKRMNTLYKKMEQD; KMKRMNTLYKKMEQDV; MKRMNTLYKKMEQDVK; KRMNTLYKKMEQDVKV; RMNTLYKKMEQDVKVA; MNTLYKKMEQDVKVAH; NTLYKKMEQDVKVAHQ; TLYKKMEQDVKVAHQP; LYKKMEQDVKVAHQPD; YKKMEQDVKVAHQPDF; KKMEQDVKVAHQPDFG; KMEQDVKVAHQPDFGT; MEQDVKVAHQPDFGTW; EQDVKVAHQPDFGTWS; QDVKVAHQPDFGTWSS; DVKVAHQPDFGTWSSS; VKVAHQPDFGTWSSSE; KVAHQPDFGTWSSSEV; VAHQPDFGTWSSSEVC; AHQPDFGTWSSSEVCA; HQPDFGTWSSSEVCAD; QPDFGTWSSSEVCADF; PDFGTWSSSEVCADFP; DFGTWSSSEVCADFPL; FGTWSSSEVCADFPLC; GTWSSSEVCADFPLCP; TWSSSEVCADFPLCPD; WSSSEVCADFPLCPDT; SSSEVCADFPLCPDTL; SSEVCADFPLCPDTLY; SEVCADFPLCPDTLYC; EVCADFPLCPDTLYCK; VCADFPLCPDTLYCKE; CADFPLCPDTLYCKEW; ADFPLCPDTLYCKEWP; DFPLCPDTLYCKEWPI; FPLCPDTLYCKEWPIC; PLCPDTLYCKEWPICS; LCPDTLYCKEWPICSK; CPDTLYCKEWPICSKK; PDTLYCKEWPICSKKP; DTLYCKEWPICSKKPS; TLYCKEWPICSKKPSV; LYCKEWPICSKKPSVH; YCKEWPICSKKPSVHC; CKEWPICSKKPSVHCP; KEWPICSKKPSVHCPC; EWPICSKKPSVHCPCM; WPICSKKPSVHCPCML; PICSKKPSVHCPCMLC; ICSKKPSVHCPCMLCQ; CSKKPSVHCPCMLCQL; SKKPSVHCPCMLCQLR; KKPSVHCPCMLCQLRL; KPSVHCPCMLCQLRLR; PSVHCPCMLCQLRLRH; SVHCPCMLCQLRLRHL; VHCPCMLCQLRLRHLN; HCPCMLCQLRLRHLNR; CPCMLCQLRLRHLNRK; PCMLCQLRLRHLNRKF; CMLCQLRLRHLNRKFL; MLCQLRLRHLNRKFLR; LCQLRLRHLNRKFLRK; CQLRLRHLNRKFLRKE; QLRLRHLNRKFLRKEP; LRLRHLNRKFLRKEPL; RLRHLNRKFLRKEPLV; LRHLNRKFLRKEPLVW; RHLNRKFLRKEPLVWI; HLNRKFLRKEPLVWID; LNRKFLRKEPLVWIDC; NRKFLRKEPLVWIDCY; RKFLRKEPLVWIDCYC; KFLRKEPLVWIDCYCI; FLRKEPLVWIDCYCID; LRKEPLVWIDCYCIDC; RKEPLVWIDCYCIDCF; KEPLVWIDCYCIDCFT; EPLVWIDCYCIDCFTQ; PLVWIDCYCIDCFTQW; LVWIDCYCIDCFTQWF; VWIDCYCIDCFTQWFG; WIDCYCIDCFTQWFGL; IDCYCIDCFTQWFGLD; DCYCIDCFTQWFGLDL; CYCIDCFTQWFGLDLT; YCIDCFTQWFGLDLTE; CIDCFTQWFGLDLTEE; IDCFTQWFGLDLTEET; DCFTQWFGLDLTEETL; CFTQWFGLDLTEETLQ; FTQWFGLDLTEETLQW; TQWFGLDLTEETLQWW; QWFGLDLTEETLQWWV; WFGLDLTEETLQWWVQ; FGLDLTEETLQWWVQI; GLDLTEETLQWWVQII; LDLTEETLQWWVQIIG; DLTEETLQWWVQIIGE; LTEETLQWWVQIIGET; TEETLQWWVQIIGETP; EETLQWWVQIIGETPF; ETLQWWVQIIGETPFR; TLQWWVQIIGETPFRD; LQWWVQIIGETPFRDL; QWWVQIIGETPFRDLK; WWVQIIGETPFRDLKL; KALSNYFFYRCQPMEQ; ALSNYFFYRCQPMEQK; LSNYFFYRCQPMEQKS; SNYFFYRCQPMEQKSG; NYFFYRCQPMEQKSGS; YFFYRCQPMEQKSGSP; FFYRCQPMEQKSGSPG; FYRCQPMEQKSGSPGG; YRCQPMEQKSGSPGGV; RCQPMEQKSGSPGGVP; CQPMEQKSGSPGGVPL; QPMEQKSGSPGGVPLM; PMEQKSGSPGGVPLMK; MEQKSGSPGGVPLMKN; EQKSGSPGGVPLMKNG; QKSGSPGGVPLMKNGM; KSGSPGGVPLMKNGMK; SGSPGGVPLMKNGMKI; GSPGGVPLMKNGMKIY; SPGGVPLMKNGMKIYF; PGGVPLMKNGMKIYFA; GGVPLMKNGMKIYFAM; GVPLMKNGMKIYFAMK; VPLMKNGMKIYFAMKI; PLMKNGMKIYFAMKIC; LMKNGMKIYFAMKICL; MKNGMKIYFAMKICLP; KNGMKIYFAMKICLPV; NGMKIYFAMKICLPVM; GMKIYFAMKICLPVMK; MKIYFAMKICLPVMKK; KIYFAMKICLPVMKKQ; IYFAMKICLPVMKKQQ; YFAMKICLPVMKKQQQ; FAMKICLPVMKKQQQI; AMKICLPVMKKQQQIL; MKICLPVMKKQQQILN; KICLPVMKKQQQILNT; ICLPVMKKQQQILNTQ; CLPVMKKQQQILNTQH; LPVMKKQQQILNTQHH; PVMKKQQQILNTQHHP; VMKKQQQILNTQHHPK; MKKQQQILNTQHHPKK; KKQQQILNTQHHPKKK; KQQQILNTQHHPKKKE; QQQILNTQHHPKKKER; KTLKTFPLIYTSFLVK; TLKTFPLIYTSFLVKL; LKTFPLIYTSFLVKLY; KTFPLIYTSFLVKLYL; TFPLIYTSFLVKLYLV; FPLIYTSFLVKLYLVI; PLIYTSFLVKLYLVIE; LIYTSFLVKLYLVIEP; IYTSFLVKLYLVIEPL; YTSFLVKLYLVIEPLP; TSFLVKLYLVIEPLPA; SFLVKLYLVIEPLPAL; FLVKLYLVIEPLPALL; LVKLYLVIEPLPALLC; VKLYLVIEPLPALLCI; KLYLVIEPLPALLCIL; LYLVIEPLPALLCILL; YLVIEPLPALLCILLK; LVIEPLPALLCILLKK; VIEPLPALLCILLKKK; IEPLPALLCILLKKKL; EPLPALLCILLKKKLK; PLPALLCILLKKKLKF; LPALLCILLKKKLKFC; PALLCILLKKKLKFCI; ALLCILLKKKLKFCIK; LLCILLKKKLKFCIKN; LCILLKKKLKFCIKNL; CILLKKKLKFCIKNLW; ILLKKKLKFCIKNLWK; LLKKKLKFCIKNLWKN; LKKKLKFCIKNLWKNI; KKKLKFCIKNLWKNIL; LLLVDTCVLGIILYSF; LHIDIEFLQLIISVKS; HIDIEFLQLIISVKSC; IDIEFLQLIISVKSCV; DIEFLQLIISVKSCVP; IEFLQLIISVKSCVPL; EFLQLIISVKSCVPLV; FLQLIISVKSCVPLVF; RSMILAQKSLKKQSRC; SMILAQKSLKKQSRCL; MILAQKSLKKQSRCLG; ILAQKSLKKQSRCLGN; RSVKSVRKKTSLITLS; SVKSVRKKTSLITLSI; VKSVRKKTSLITLSIM; KSVRKKTSLITLSIMK; SVRKKTSLITLSIMKS; VRKKTSLITLSIMKST; RKKTSLITLSIMKSTL; KKTSLITLSIMKSTLQ; KTSLITLSIMKSTLQM; TSLITLSIMKSTLQML; SLITLSIMKSTLQMLL; LITLSIMKSTLQMLLF; ITLSIMKSTLQMLLFL; TLSIMKSTLQMLLFLQ; LSIMKSTLQMLLFLQK; SIMKSTLQMLLFLQKV; IMKSTLQMLLFLQKVK; MKSTLQMLLFLQKVKI; KSTLQMLLFLQKVKIK; STLQMLLFLQKVKIKK; TLQMLLFLQKVKIKKV; LQMLLFLQKVKIKKVF; QMLLFLQKVKIKKVFV; MLLFLQKVKIKKVFVS; LLFLQKVKIKKVFVSK; LFLQKVKIKKVFVSKQ; NNIWQVLLGCTVCYLK; NIWQVLLGCTVCYLKW; IWQVLLGCTVCYLKWI; WQVLLGCTVCYLKWIL; YLIFCTVLFSMYLKED; LIFCTVLFSMYLKEDT; IFCTVLFSMYLKEDTG; FCTVLFSMYLKEDTGY; CTVLFSMYLKEDTGYL; TVLFSMYLKEDTGYLK; VLFSMYLKEDTGYLKV; LFSMYLKEDTGYLKVP; FSMYLKEDTGYLKVPL; SMYLKEDTGYLKVPLI; MYLKEDTGYLKVPLIV; YLKEDTGYLKVPLIVE; LKEDTGYLKVPLIVEK; KEDTGYLKVPLIVEKQ; EDTGYLKVPLIVEKQH; ENPYKTQSSYLKKEFY; NPYKTQSSYLKKEFYK; PYKTQSSYLKKEFYKV; YKTQSSYLKKEFYKVE; LILQLIYNLELLNGRK; ILQLIYNLELLNGRKG; LQLIYNLELLNGRKGW; QLIYNLELLNGRKGWI; LIYNLELLNGRKGWIL; IYNLELLNGRKGWILR; NIIYAWGNVFLILQEK; IIYAWGNVFLILQEKR; IYAWGNVFLILQEKRI; YAWGNVFLILQEKRIQ; AWGNVFLILQEKRIQK; WGNVFLILQEKRIQKL; GNVFLILQEKRIQKLK; NVFLILQEKRIQKLKT; VFLILQEKRIQKLKTL; FLILQEKRIQKLKTLD; LILQEKRIQKLKTLDM; ILQEKRIQKLKTLDMD; LQEKRIQKLKTLDMDQ; QEKRIQKLKTLDMDQA; EKRIQKLKTLDMDQAL; KRIQKLKTLDMDQALN; RIQKLKTLDMDQALNP; IQKLKTLDMDQALNPN; QKLKTLDMDQALNPNH; KLKTLDMDQALNPNHN; LKTLDMDQALNPNHNA; KTLDMDQALNPNHNAL; TLDMDQALNPNHNALP; LDMDQALNPNHNALPK; DMDQALNPNHNALPKS; MDQALNPNHNALPKSQ; DQALNPNHNALPKSQI; QALNPNHNALPKSQIL; ALNPNHNALPKSQILQ; LNPNHNALPKSQILQP; NPNHNALPKSQILQPL; PNHNALPKSQILQPLL; NHNALPKSQILQPLLK; HNALPKSQILQPLLKI; NALPKSQILQPLLKIP; ALPKSQILQPLLKIPK; LPKSQILQPLLKIPKG; PKSQILQPLLKIPKGQ; KSQILQPLLKIPKGQT; SQILQPLLKIPKGQTP; QILQPLLKIPKGQTPI; ILQPLLKIPKGQTPIV; LQPLLKIPKGQTPIVK; QPLLKIPKGQTPIVKS; PLLKIPKGQTPIVKSC; LLKIPKGQTPIVKSCI; LKIPKGQTPIVKSCIC; KIPKGQTPIVKSCICV; IPKGQTPIVKSCICVK; PKGQTPIVKSCICVKA; KGQTPIVKSCICVKAF; GQTPIVKSCICVKAFS; QTPIVKSCICVKAFSV; TPIVKSCICVKAFSVL; PIVKSCICVKAFSVLK; IVKSCICVKAFSVLKG; VKSCICVKAFSVLKGL; KSCICVKAFSVLKGLK; SCICVKAFSVLKGLKH; CICVKAFSVLKGLKHH; ICVKAFSVLKGLKHHP; CVKAFSVLKGLKHHPQ; VKAFSVLKGLKHHPQN; KAFSVLKGLKHHPQNN; AFSVLKGLKHHPQNNT; FSVLKGLKHHPQNNTS; SVLKGLKHHPQNNTSL; VLKGLKHHPQNNTSLK; LKGLKHHPQNNTSLKV; KGLKHHPQNNTSLKVA; GLKHHPQNNTSLKVAY; LKHHPQNNTSLKVAYT; KHHPQNNTSLKVAYTK; HHPQNNTSLKVAYTKA; HPQNNTSLKVAYTKAA; PQNNTSLKVAYTKAAF; QNNTSLKVAYTKAAFI; NNTSLKVAYTKAAFIK; NTSLKVAYTKAAFIKC; TSLKVAYTKAAFIKCI; SLKVAYTKAAFIKCIC; LKVAYTKAAFIKCICT; KVAYTKAAFIKCICTI; VAYTKAAFIKCICTIK; AYTKAAFIKCICTIKA; YTKAAFIKCICTIKAP; TKAAFIKCICTIKAPV; SILVCNCPCLSIYLII; ILVCNCPCLSIYLIIS; LVCNCPCLSIYLIISG; VCNCPCLSIYLIISGS; CNCPCLSIYLIISGSP; NCPCLSIYLIISGSPG; CPCLSIYLIISGSPGS; PCLSIYLIISGSPGSL; CLSIYLIISGSPGSLS; LSIYLIISGSPGSLSV; SIYLIISGSPGSLSVP; IYLIISGSPGSLSVPS; YLIISGSPGSLSVPSN; LIISGSPGSLSVPSNT; IISGSPGSLSVPSNTL; ISGSPGSLSVPSNTLT; SGSPGSLSVPSNTLTS; GSPGSLSVPSNTLTSS; SPGSLSVPSNTLTSST; PGSLSVPSNTLTSSTW; GSLSVPSNTLTSSTWD; SLSVPSNTLTSSTWDS; LSVPSNTLTSSTWDSI; SVPSNTLTSSTWDSIP; VPSNTLTSSTWDSIPY; PSNTLTSSTWDSIPYI; SNTLTSSTWDSIPYIG; NTLTSSTWDSIPYIGC; TLTSSTWDSIPYIGCP; LTSSTWDSIPYIGCPS; TSSTWDSIPYIGCPST; SSTWDSIPYIGCPSTL; STWDSIPYIGCPSTLW; TWDSIPYIGCPSTLWV; WDSIPYIGCPSTLWVL; DSIPYIGCPSTLWVLL; SIPYIGCPSTLWVLLF; IPYIGCPSTLWVLLFI; PYIGCPSTLWVLLFIR; YIGCPSTLWVLLFIRS; IGCPSTLWVLLFIRSL; GCPSTLWVLLFIRSLS; CPSTLWVLLFIRSLSK; PSTLWVLLFIRSLSKK; STLWVLLFIRSLSKKE; TLWVLLFIRSLSKKEI; LWVLLFIRSLSKKEIG; GFFTDLFLRRILKYLA; FFTDLFLRRILKYLAR; FTDLFLRRILKYLARP; TDLFLRRILKYLARPL; DLFLRRILKYLARPLH; LFLRRILKYLARPLHC; FLRRILKYLARPLHCC; LRRILKYLARPLHCCV; RRILKYLARPLHCCVP; RILKYLARPLHCCVPE; ILKYLARPLHCCVPEL; LKYLARPLHCCVPELL; KYLARPLHCCVPELLV; YLARPLHCCVPELLVN; LARPLHCCVPELLVNR; ARPLHCCVPELLVNRP; RPLHCCVPELLVNRPQ; PLHCCVPELLVNRPQI; LHCCVPELLVNRPQIS; HCCVPELLVNRPQISA; CCVPELLVNRPQISAA; CVPELLVNRPQISAAE; VPELLVNRPQISAAET; PELLVNRPQISAAETY; ELLVNRPQISAAETYR; LLVNRPQISAAETYRL; LVNRPQISAAETYRLS; VNRPQISAAETYRLSA; NRPQISAAETYRLSAL; RPQISAAETYRLSALQ; PQISAAETYRLSALQR; QISAAETYRLSALQRG; ISAAETYRLSALQRGP; SAAETYRLSALQRGPT; AAETYRLSALQRGPTP; AETYRLSALQRGPTPC; ETYRLSALQRGPTPCS; TYRLSALQRGPTPCSS; YRLSALQRGPTPCSSS; RLSALQRGPTPCSSSN; LSALQRGPTPCSSSNT; SALQRGPTPCSSSNTV; ALQRGPTPCSSSNTVV; LQRGPTPCSSSNTVVA; QRGPTPCSSSNTVVAV; RGPTPCSSSNTVVAVL; GPTPCSSSNTVVAVLV; PTPCSSSNTVVAVLVT; STGGTFSPPVKVPKYL; TGGTFSPPVKVPKYLA; GGTFSPPVKVPKYLAF; GTFSPPVKVPKYLAFS; TFSPPVKVPKYLAFSF; FSPPVKVPKYLAFSFL; SPPVKVPKYLAFSFLL; PPVKVPKYLAFSFLLG; PVKVPKYLAFSFLLGS; VKVPKYLAFSFLLGSG; KVPKYLAFSFLLGSGT; VPKYLAFSFLLGSGTQ; PKYLAFSFLLGSGTQH; KYLAFSFLLGSGTQHS; YLAFSFLLGSGTQHST; LAFSFLLGSGTQHSTG; ALWSVFITWDWAVGFL; LWSVFITWDWAVGFLG; WSVFITWDWAVGFLGV; SVFITWDWAVGFLGVI; VFITWDWAVGFLGVIV; FITWDWAVGFLGVIVP; ITWDWAVGFLGVIVPS; TWDWAVGFLGVIVPSG; WDWAVGFLGVIVPSGY; DWAVGFLGVIVPSGYF; WAVGFLGVIVPSGYFD; AVGFLGVIVPSGYFDL; FISTPCISKGSPPTAK; ISTPCISKGSPPTAKK; STPCISKGSPPTAKKW; TPCISKGSPPTAKKWK; PCISKGSPPTAKKWKL; CISKGSPPTAKKWKLL; ISKGSPPTAKKWKLLP; RLSMLVIPITSVCTVT; LSMLVIPITSVCTVTA; SMLVIPITSVCTVTAS; MLVIPITSVCTVTASH; LVIPITSVCTVTASHI; VIPITSVCTVTASHIS; IPITSVCTVTASHISR; PITSVCTVTASHISRF; ITSVCTVTASHISRFP; TSVCTVTASHISRFPQ; SVCTVTASHISRFPQV; VCTVTASHISRFPQVR; CTVTASHISRFPQVRS; TVTASHISRFPQVRSS; VTASHISRFPQVRSSF; TASHISRFPQVRSSFK; ASHISRFPQVRSSFKL; SHISRFPQVRSSFKLG; HISRFPQVRSSFKLGR; ISRFPQVRSSFKLGRG; SRFPQVRSSFKLGRGI; RFPQVRSSFKLGRGIL; FPQVRSSFKLGRGILA; PQVRSSFKLGRGILAV; QVRSSFKLGRGILAVL; QGSIFLSGLSLLKSFS; GSIFLSGLSLLKSFSA; SIFLSGLSLLKSFSAL; IFLSGLSLLKSFSALS; FLSGLSLLKSFSALSF; LSGLSLLKSFSALSFR; SGLSLLKSFSALSFRL; GLSLLKSFSALSFRLK; LSLLKSFSALSFRLKP; SLLKSFSALSFRLKPL; LLKSFSALSFRLKPLR; LKSFSALSFRLKPLRF; KSFSALSFRLKPLRFS; SFSALSFRLKPLRFSS; FSALSFRLKPLRFSSG; SALSFRLKPLRFSSGS; ALSFRLKPLRFSSGSP; LSFRLKPLRFSSGSPI; SFRLKPLRFSSGSPIS; FRLKPLRFSSGSPISG; RLKPLRFSSGSPISGF; LKPLRFSSGSPISGFR; KPLRFSSGSPISGFRK; PLRFSSGSPISGFRKH; LRFSSGSPISGFRKHS; RFSSGSPISGFRKHST; FSSGSPISGFRKHSTS; SSGSPISGFRKHSTSV; SGSPISGFRKHSTSVI; GSPISGFRKHSTSVIA; SPISGFRKHSTSVIAS; PISGFRKHSTSVIAST; ISGFRKHSTSVIASTP; SGFRKHSTSVIASTPV; GFRKHSTSVIASTPVL; FRKHSTSVIASTPVLT; RKHSTSVIASTPVLTS; KHSTSVIASTPVLTSR; HSTSVIASTPVLTSRT; STSVIASTPVLTSRTS; TSVIASTPVLTSRTST; SVIASTPVLTSRTSTP; VIASTPVLTSRTSTPP; IASTPVLTSRTSTPPF; ASTPVLTSRTSTPPFI; STPVLTSRTSTPPFIS; TPVLTSRTSTPPFISS; PVLTSRTSTPPFISSF; VLTSRTSTPPFISSFG; LTSRTSTPPFISSFGT; TSRTSTPPFISSFGTC; SRTSTPPFISSFGTCT; RTSTPPFISSFGTCTG; TSTPPFISSFGTCTGS; STPPFISSFGTCTGSF; TPPFISSFGTCTGSFG; PPFISSFGTCTGSFGF; PFISSFGTCTGSFGFL; FISSFGTCTGSFGFLG; ISSFGTCTGSFGFLGA; SSFGTCTGSFGFLGAA; SFGTCTGSFGFLGAAP; FGTCTGSFGFLGAAPG; GTCTGSFGFLGAAPGH; TCTGSFGFLGAAPGHS; CTGSFGFLGAAPGHSP; TGSFGFLGAAPGHSPF; GSFGFLGAAPGHSPFL; SFGFLGAAPGHSPFLL; FGFLGAAPGHSPFLLV; GFLGAAPGHSPFLLVG; FLGAAPGHSPFLLVGA; LGAAPGHSPFLLVGAI; GAAPGHSPFLLVGAIF; AAPGHSPFLLVGAIFI; APGHSPFLLVGAIFIC; PGHSPFLLVGAIFICF; GHSPFLLVGAIFICFK; HSPFLLVGAIFICFKS; SPFLLVGAIFICFKSR; PFLLVGAIFICFKSRC; FLLVGAIFICFKSRCY; LLVGAIFICFKSRCYS; LVGAIFICFKSRCYSP; VGAIFICFKSRCYSPV; GAIFICFKSRCYSPVQ; AIFICFKSRCYSPVQA; RQHPLRSSSLISTSWG; QHPLRSSSLISTSWGN; HPLRSSSLISTSWGNS; PLRSSSLISTSWGNSF; LRSSSLISTSWGNSFF; RSSSLISTSWGNSFFY; SSSLISTSWGNSFFYK; SSLISTSWGNSFFYKL; SLISTSWGNSFFYKLS; VHSLCNFFYTVSIIYT; HSLCNFFYTVSIIYTI; SLCNFFYTVSIIYTIS; LCNFFYTVSIIYTISM; CNFFYTVSIIYTISMA; NFFYTVSIIYTISMAK; FFYTVSIIYTISMAKM; FYTVSIIYTISMAKMY; YTVSIIYTISMAKMYT; TVSIIYTISMAKMYTG; VSIIYTISMAKMYTGT; SIIYTISMAKMYTGTF; IIYTISMAKMYTGTFP; IYTISMAKMYTGTFPF; YTISMAKMYTGTFPFS; TISMAKMYTGTFPFSY; ISMAKMYTGTFPFSYL; SMAKMYTGTFPFSYLS; MAKMYTGTFPFSYLSN; AKMYTGTFPFSYLSNH; GPNRGKIRIILLNIII; PNRGKIRIILLNIIIK; NRGKIRIILLNIIIKV; RGKIRIILLNIIIKVY; GKIRIILLNIIIKVYR; KIRIILLNIIIKVYRG; IRIILLNIIIKVYRGI; RIILLNIIIKVYRGIY; IILLNIIIKVYRGIYN; ILLNIIIKVYRGIYNC; LLNIIIKVYRGIYNCP; LNIIIKVYRGIYNCPG; NIIIKVYRGIYNCPGS; IIIKVYRGIYNCPGSF; IIKVYRGIYNCPGSFL; IKVYRGIYNCPGSFLQ; KVYRGIYNCPGSFLQK; VYRGIYNCPGSFLQKS; YRGIYNCPGSFLQKSS; RGIYNCPGSFLQKSSQ; GIYNCPGSFLQKSSQG; IYNCPGSFLQKSSQGV; YNCPGSFLQKSSQGVS; NCPGSFLQKSSQGVSK; CPGSFLQKSSQGVSKK; PGSFLQKSSQGVSKKS; GSFLQKSSQGVSKKSF; SFLQKSSQGVSKKSFC; FLQKSSQGVSKKSFCS; LQKSSQGVSKKSFCSS; QKSSQGVSKKSFCSSL; KSSQGVSKKSFCSSLQ; SSQGVSKKSFCSSLQF; SQGVSKKSFCSSLQFL; GYRRYIIPNNMPQSLG; YRRYIIPNNMPQSLGN; RRYIIPNNMPQSLGNS; RYIIPNNMPQSLGNSS; YIIPNNMPQSLGNSSK; IIPNNMPQSLGNSSKQ; IPNNMPQSLGNSSKQR; PNNMPQSLGNSSKQRR; NNMPQSLGNSSKQRRT; NMPQSLGNSSKQRRTP; MPQSLGNSSKQRRTPM; PQSLGNSSKQRRTPMP; QSLGNSSKQRRTPMPR; SLGNSSKQRRTPMPRI; LGNSSKQRRTPMPRIK; GNSSKQRRTPMPRIKV; NSSKQRRTPMPRIKVL; SSKQRRTPMPRIKVLN; SKQRRTPMPRIKVLNI; KQRRTPMPRIKVLNII; QRRTPMPRIKVLNIIN; RRTPMPRIKVLNIINK; RTPMPRIKVLNIINKS; TPMPRIKVLNIINKSI; PMPRIKVLNIINKSIY; MPRIKVLNIINKSIYT; PRIKVLNIINKSIYTR; RIKVLNIINKSIYTRK; IKVLNIINKSIYTRKQ; KVLNIINKSIYTRKQN; VLNIINKSIYTRKQNI; LNIINKSIYTRKQNII; NIINKSIYTRKQNIIV; IINKSIYTRKQNIIVL; INKSIYTRKQNIIVLI; NKSIYTRKQNIIVLIW; KSIYTRKQNIIVLIWV; SIYTRKQNIIVLIWVK; IYTRKQNIIVLIWVKQ; YTRKQNIIVLIWVKQF; TRKQNIIVLIWVKQFQ; RKQNIIVLIWVKQFQS; KQNIIVLIWVKQFQSH; QNIIVLIWVKQFQSHA; LLIEAYSGNFVIPIIK; LIEAYSGNFVIPIIKE; IEAYSGNFVIPIIKEL; EAYSGNFVIPIIKELI; AYSGNFVIPIIKELIP; YSGNFVIPIIKELIPY; SGNFVIPIIKELIPYL; GNFVIPIIKELIPYLS; SSKPSNSPRSTSNYSI; SKPSNSPRSTSNYSIC; KPSNSPRSTSNYSICL; PSNSPRSTSNYSICLR; SNSPRSTSNYSICLRS; GTCYALYSSKGCNLNF; TCYALYSSKGCNLNFY; CYALYSSKGCNLNFYS; YALYSSKGCNLNFYSS; ALYSSKGCNLNFYSSS; LYSSKGCNLNFYSSSS; YSSKGCNLNFYSSSSL; SSKGCNLNFYSSSSLP; SKGCNLNFYSSSSLPS; KGCNLNFYSSSSLPSS; GCNLNFYSSSSLPSSN; CNLNFYSSSSLPSSNF; NLNFYSSSSLPSSNFS; LNFYSSSSLPSSNFSH; SSTHEPGNTKKKGLLT; ESFTESFTAGKAVVLL; SFTESFTAGKAVVLLF; FTESFTAGKAVVLLFF; TESFTAGKAVVLLFFP; ESFTAGKAVVLLFFPS; SFTAGKAVVLLFFPST; FTAGKAVVLLFFPSTL; TAGKAVVLLFFPSTLS; AGKAVVLLFFPSTLSS; GKAVVLLFFPSTLSSP; KAVVLLFFPSTLSSPL; AVVLLFFPSTLSSPLQ; VVLLFFPSTLSSPLQN; VLLFFPSTLSSPLQNS; LLFFPSTLSSPLQNSS; LFFPSTLSSPLQNSSK; FFPSTLSSPLQNSSKS; FPSTLSSPLQNSSKSS; PSTLSSPLQNSSKSSK; STLSSPLQNSSKSSKI; TLSSPLQNSSKSSKIK; LSSPLQNSSKSSKIKI; SSPLQNSSKSSKIKIK; SPLQNSSKSSKIKIKI; PLQNSSKSSKIKIKIL; ALFFVPVQVLPTFTEA; LFFVPVQVLPTFTEAC; FFVPVQVLPTFTEACR; FVPVQVLPTFTEACRD; VPVQVLPTFTEACRDS; PVQVLPTFTEACRDSW; VQVLPTFTEACRDSWR; QVLPTFTEACRDSWRR; VLPTFTEACRDSWRRT; LPTFTEACRDSWRRTM; PTFTEACRDSWRRTMA; TFTEACRDSWRRTMAF; FTEACRDSWRRTMAFV; TEACRDSWRRTMAFVQ; EACRDSWRRTMAFVQF; ACRDSWRRTMAFVQFN; CRDSWRRTMAFVQFNW; RDSWRRTMAFVQFNWG; DSWRRTMAFVQFNWGQ; SWRRTMAFVQFNWGQG; WRRTMAFVQFNWGQGQ; RRTMAFVQFNWGQGQD; RTMAFVQFNWGQGQDS; ARKTCLSCTFLPEVMV; RKTCLSCTFLPEVMVW; KTCLSCTFLPEVMVWL; TCLSCTFLPEVMVWLH; CLSCTFLPEVMVWLHS; LSCTFLPEVMVWLHSM; SCTFLPEVMVWLHSMG; CTFLPEVMVWLHSMGK; TFLPEVMVWLHSMGKQ; FLPEVMVWLHSMGKQL; LPEVMVWLHSMGKQLL; PEVMVWLHSMGKQLLP; EVMVWLHSMGKQLLPV; VMVWLHSMGKQLLPVS; MVWLHSMGKQLLPVSH; VWLHSMGKQLLPVSHA; WLHSMGKQLLPVSHAL; LHSMGKQLLPVSHALS; HSMGKQLLPVSHALSF; SMGKQLLPVSHALSFL; MGKQLLPVSHALSFLR; GKQLLPVSHALSFLRS; KQLLPVSHALSFLRSW; QLLPVSHALSFLRSWF; LLPVSHALSFLRSWFG; LPVSHALSFLRSWFGC; PVSHALSFLRSWFGCI; VSHALSFLRSWFGCIP; SHALSFLRSWFGCIPL; GLAKLFGEIPILLQFL; LAKLFGEIPILLQFLQ BK virus reverse reading frame 2 13 mers: WIKFLTGKNPWSS; IKFLTGKNPWSSW; KFLTGKNPWSSWT; FLTGKNPWSSWTF; GSVRNFTLTKGAT; SVRNFTLTKGATR; VRNFTLTKGATRI; RNFTLTKGATRIK; LISLILEPGVAQR; ISLILEPGVAQRF; SLILEPGVAQRFV; LILEPGVAQRFVL; ILEPGVAQRFVLI; LEPGVAQRFVLIF; EPGVAQRFVLIFL; PGVAQRFVLIFLF; GVAQRFVLIFLFA; VAQRFVLIFLFAQ; AQRFVLIFLFAQI; QRFVLIFLFAQIP; RFVLIFLFAQIPC; FVLIFLFAQIPCT; VLIFLFAQIPCTA; LIFLFAQIPCTAR; IFLFAQIPCTARN; FLFAQIPCTARNG; LFAQIPCTARNGL; FAQIPCTARNGLF; AQIPCTARNGLFV; QIPCTARNGLFVP; IPCTARNGLFVPK; PCTARNGLFVPKS; CTARNGLFVPKSL; TARNGLFVPKSLL; ARNGLFVPKSLLC; RNGLFVPKSLLCT; NGLFVPKSLLCTA; GLFVPKSLLCTAL; LFVPKSLLCTALA; FVPKSLLCTALAC; VPKSLLCTALACY; PKSLLCTALACYV; KSLLCTALACYVS; SLLCTALACYVSL; LLCTALACYVSLD; IATALTASHSGLA; VIIFFIGANLWNR; IIFFIGANLWNRR; IFFIGANLWNRRV; FFIGANLWNRRVG; FIGANLWNRRVGV; IGANLWNRRVGVL; GANLWNRRVGVLV; ANLWNRRVGVLVE; NLWNRRVGVLVEF; LWNRRVGVLVEFL; RSNSRFSTLNTTQ; SNSRFSTLNTTQK; NSRFSTLNTTQKK; SRFSTLNTTQKKK; RFSTLNTTQKKKK; FSTLNTTQKKKKG; STLNTTQKKKKGR; TLNTTQKKKKGRR; LNTTQKKKKGRRP; RSIPYYRRKHSRG; SIPYYRRKHSRGL; IPYYRRKHSRGLK; PYYRRKHSRGLKG; YYRRKHSRGLKGA; GCVFIIRYVFRIS; CVFIIRYVFRISI; VFIIRYVFRISIQ; FIIRYVFRISIQC; IIRYVFRISIQCR; IRYVFRISIQCRG; RYVFRISIQCRGV; KSKKYLSASSRYS; SKKYLSASSRYSF; KKYLSASSRYSFS; KKSRYPSYDQGRN; KSRYPSYDQGRNA; SRYPSYDQGRNAN; RYPSYDQGRNANR; YPSYDQGRNANRK; PSYDQGRNANRKI; SYDQGRNANRKIQ; YDQGRNANRKIQS; DQGRNANRKIQSY; QGRNANRKIQSYI; GRNANRKIQSYIR; NGFNIWSSWKCCT; GFNIWSSWKCCTR; FNIWSSWKCCTRT; NIWSSWKCCTRTI; IWSSWKCCTRTIY; WSSWKCCTRTIYG; SSWKCCTRTIYGR; SWKCCTRTIYGRC; WKCCTRTIYGRCC; KCCTRTIYGRCCL; CCTRTIYGRCCLA; CTRTIYGRCCLAA; TRTIYGRCCLAAL; RTIYGRCCLAALF; TIYGRCCLAALFA; IYGRCCLAALFAT; WKNNTSCRVIRFV; KNNTSCRVIRFVW; NNTSCRVIRFVWW; SLKCKPTHGKANL; IKGFAFRTWNKQF; KGFAFRTWNKQFR; GFAFRTWNKQFRQ; FAFRTWNKQFRQF; AFRTWNKQFRQFE; FRTWNKQFRQFER; RTWNKQFRQFERL; TWNKQFRQFERLF; WNKQFRQFERLFR; NKQFRQFERLFRW; KQFRQFERLFRWK; QFRQFERLFRWKC; GKFRKETFKQKNP; KFRKETFKQKNPN; FRKETFKQKNPNI; RKETFKQKNPNIS; KETFKQKNPNIST; ETFKQKNPNISTR; TFKQKNPNISTRL; FKQKNPNISTRLG; KQKNPNISTRLGY; QKNPNISTRLGYN; KNPNISTRLGYNE; AQNIFKKILTKLR; QNIFKKILTKLRV; NIFKKILTKLRVL; IFKKILTKLRVLT; KKNFTKWNDLVAT; KNFTKWNDLVATA; NFTKWNDLVATAN; FTKWNDLVATANL; TKWNDLVATANLV; IPITMLFPSLRYF; PITMLFPSLRYFS; ITMLFPSLRYFSP; TMLFPSLRYFSPC; KWLIQKQHLLNVY; WLIQKQHLLNVYV; LIQKQHLLNVYVQ; KHLFKAFWFAIVP; HLFKAFWFAIVPV; LFKAFWFAIVPVC; FKAFWFAIVPVCQ; KAFWFAIVPVCQY; AFWFAIVPVCQYI; FWFAIVPVCQYIL; WFAIVPVCQYILS; FAIVPVCQYILSY; AIVPVCQYILSYL; IVPVCQYILSYLG; VPVCQYILSYLGP; PVCQYILSYLGPL; VCQYILSYLGPLE; CQYILSYLGPLEV; QYILSYLGPLEVF; YILSYLGPLEVFL; ILSYLGPLEVFLC; LSYLGPLEVFLCH; SYLGPLEVFLCHQ; YLGPLEVFLCHQT; LGPLEVFLCHQTP; GHLAKRKLGKDSL; HLAKRKLGKDSLQ; LAKRKLGKDSLQI; AKRKLGKDSLQIF; KRKLGKDSLQIFF; RKLGKDSLQIFFS; KLGKDSLQIFFSG; LGKDSLQIFFSGG; GKDSLQIFFSGGS; NILQGLSTVVFQS; ILQGLSTVVFQSC; TGHKYQQLKHTGY; GHKYQQLKHTGYQ; HKYQQLKHTGYQL; KYQQLKHTGYQLY; YQQLKHTGYQLYK; QQLKHTGYQLYKE; QLKHTGYQLYKEA; LKHTGYQLYKEAP; KHTGYQLYKEAPH; HTGYQLYKEAPHP; TGYQLYKEAPHPV; GYQLYKEAPHPVH; YQLYKEAPHPVHL; QLYKEAPHPVHLA; LYKEAPHPVHLAT; YKEAPHPVHLATL; KEAPHPVHLATLW; LCWSHEVLGEHFP; CWSHEVLGEHFPL; WSHEVLGEHFPLL; HFHFYWDQVPSTQ; FHFYWDQVPSTQL; HFYWDQVPSTQLD; FYWDQVPSTQLDK; YWDQVPSTQLDKH; WDQVPSTQLDKHC; DQVPSTQLDKHCF; QVPSTQLDKHCFC; VPSTQLDKHCFCP; PSTQLDKHCFCPN; STQLDKHCFCPNR; TQLDKHCFCPNRP; QLDKHCFCPNRPY; LDKHCFCPNRPYG; DKHCFCPNRPYGQ; KHCFCPNRPYGQY; HCFCPNRPYGQYS; CFCPNRPYGQYSL; FCPNRPYGQYSLP; CPNRPYGQYSLPG; PNRPYGQYSLPGT; NRPYGQYSLPGTG; RPYGQYSLPGTGL; PYGQYSLPGTGLL; YGQYSLPGTGLLG; GQYSLPGTGLLGF; YHQGTLTCNSLAL; HQGTLTCNSLALP; QGTLTCNSLALPA; GTLTCNSLALPAF; TLTCNSLALPAFP; LTCNSLALPAFPR; TCNSLALPAFPRV; CNSLALPAFPRVL; NSLALPAFPRVLH; SLALPAFPRVLHL; LALPAFPRVLHLQ; ALPAFPRVLHLQQ; LPAFPRVLHLQQR; PAFPRVLHLQQRS; AFPRVLHLQQRSG; FPRVLHLQQRSGN; PRVLHLQQRSGNY; RVLHLQQRSGNYC; VLHLQQRSGNYCL; LHLQQRSGNYCLE; VFLHHAHALFVTL; FLHHAHALFVTLH; LHHAHALFVTLHE; HHAHALFVTLHEG; PLFVQLQPPTSVD; LFVQLQPPTSVDF; FVQLQPPTSVDFH; VQLQPPTSVDFHR; QLQPPTSVDFHRL; LQPPTSVDFHRLG; QPPTSVDFHRLGP; PPTSVDFHRLGPH; PTSVDFHRLGPHL; TSVDFHRLGPHLN; SVDFHRLGPHLNW; VDFHRLGPHLNWG; DFHRLGPHLNWGG; FHRLGPHLNWGGE; HRLGPHLNWGGEF; RLGPHLNWGGEFL; LGPHLNWGGEFLL; GPHLNWGGEFLLC; PHLNWGGEFLLCC; HLNWGGEFLLCCN; LNWGGEFLLCCNR; NWGGEFLLCCNRE; WGGEFLLCCNREA; GGEFLLCCNREAF; GEFLLCCNREAFF; EFLLCCNREAFFS; FLLCCNREAFFSL; LLCCNREAFFSLG; LCCNREAFFSLGY; CCNREAFFSLGYH; CNREAFFSLGYHC; GFHLDPPFLGLGS; FHLDPPFLGLGSI; HLDPPFLGLGSIL; LDPPFLGLGSILP; DPPFLGLGSILPL; LLELLLLLLLVVL; LELLLLLLLVVLA; ELLLLLLLVVLAL; LLLLLLLVVLALA; LLLLLLVVLALAR; LLLLLVVLALARV; LLLLVVLALARVP; LLLVVLALARVPL; LLVVLALARVPLA; LVVLALARVPLAF; VVLALARVPLAFW; VLALARVPLAFWE; LALARVPLAFWEL; ALARVPLAFWELP; LARVPLAFWELPL; ARVPLAFWELPLD; RVPLAFWELPLDT; VPLAFWELPLDTL; PLAFWELPLDTLL; LAFWELPLDTLLF; AFWELPLDTLLFF; FWELPLDTLLFFW; WELPLDTLLFFWL; ELPLDTLLFFWLG; LPLDTLLFFWLGP; PLDTLLFFWLGPS; LDTLLFFWLGPSS; DTLLFFWLGPSSY; TLLFFWLGPSSYA; LLFFWLGPSSYAS; LFFWLGPSSYASR; FFWLGPSSYASRA; FWLGPSSYASRAG; WLGPSSYASRAGV; LGPSSYASRAGVT; GPSSYASRAGVTV; PSSYASRAGVTVP; SSYASRAGVTVPY; SYASRAGVTVPYR; YASRAGVTVPYRP; ASRAGVTVPYRPR; SRAGVTVPYRPRS; RAGVTVPYRPRSK; AGVTVPYRPRSKG; GVTVPYRPRSKGN; VTVPYRPRSKGNI; TVPYRPRSKGNIH; LAPPGAIVFSINS; APPGAIVFSINSP; PPGAIVFSINSPE; PGAIVFSINSPEC; GAIVFSINSPECT; AIVFSINSPECTL; IVFSINSPECTLC; FLKSILCVTSSIL; LKSILCVTSSILS; KSILCVTSSILSA; SILCVTSSILSAS; ILCVTSSILSASS; LCVTSSILSASSI; CVTSSILSASSIL; VWPKCTRVPSLSA; WPKCTRVPSLSAT; PKCTRVPSLSATC; KCTRVPSLSATCL; CTRVPSLSATCLT; TRVPSLSATCLTI; RVPSLSATCLTIE; VPSLSATCLTIEG; PSLSATCLTIEGL; SLSATCLTIEGLI; LSATCLTIEGLIG; SATCLTIEGLIGE; ATCLTIEGLIGER; TCLTIEGLIGERS; CLTIEGLIGERSE; KFIGAFTIVQVVS; FIGAFTIVQVVSS; IGAFTIVQVVSSK; GAFTIVQVVSSKN; AFTIVQVVSSKNL; FTIVQVVSSKNLA; TIVQVVSSKNLAK; IVQVVSSKNLAKE; VQVVSSKNLAKES; QVVSSKNLAKESL; VVSSKNLAKESLK; VSSKNLAKESLKN; SSKNLAKESLKNL; SKNLAKESLKNLS; KNLAKESLKNLSV; NLAKESLKNLSVL; LAKESLKNLSVLL; AKESLKNLSVLLC; KESLKNLSVLLCN; ESLKNLSVLLCNS; SLKNLSVLLCNSC; LKNLSVLLCNSCE; KNLSVLLCNSCEV; NLSVLLCNSCEVI; LSVLLCNSCEVIE; SVLLCNSCEVIEG; VLLCNSCEVIEGI; LLCNSCEVIEGIS; LCNSCEVIEGISS; CNSCEVIEGISSL; NSCEVIEGISSLI; SCEVIEGISSLIT; CEVIEGISSLITC; EVIEGISSLITCH; VIEGISSLITCHK; IEGISSLITCHKA; EGISSLITCHKAW; GISSLITCHKAWE; ISSLITCHKAWEI; SSLITCHKAWEIV; SLITCHKAWEIVA; LITCHKAWEIVAN; ITCHKAWEIVANK; TCHKAWEIVANKE; CHKAWEIVANKEG; HKAWEIVANKEGP; KAWEIVANKEGPQ; AWEIVANKEGPQC; WEIVANKEGPQCL; EIVANKEGPQCLG; IVANKEGPQCLGS; VANKEGPQCLGSR; ANKEGPQCLGSRY; ILLTKVFTPGNRI; LLTKVFTPGNRIS; YSSGLNNSKAMPD; SSGLNNSKAMPDC; IKAANPAIAPGAP; KAANPAIAPGAPA; AANPAIAPGAPAI; ANPAIAPGAPAIT; NPAIAPGAPAITA; PAIAPGAPAITAY; AIAPGAPAITAYV; GVRPIAAIASEVL; VRPIAAIASEVLV; RPIAAIASEVLVM; PIAAIASEVLVMP; IAAIASEVLVMPS; AAIASEVLVMPST; AIASEVLVMPSTV; IASEVLVMPSTVA; ASEVLVMPSTVAR; SEVLVMPSTVARD; EVLVMPSTVARDA; VLVMPSTVARDAI; TSIAAAASPAAIS; SIAAAASPAAISA; IAAAASPAAISAT; AAAASPAAISATE; AAASPAAISATEN; AASPAAISATENP; ASPAAISATENPV; SPAAISATENPVA; PAAISATENPVAA; AAISATENPVAAA; AISATENPVAAAA; ISATENPVAAAAS; SATENPVAAAASD; ATENPVAAAASDT; TENPVAAAASDTL; ENPVAAAASDTLA; NPVAAAASDTLAT; PVAAAASDTLATR; VAAAASDTLATRS; AAAASDTLATRSP; AAASDTLATRSPK; AASDTLATRSPKS; ASDTLATRSPKSA; SDTLATRSPKSAR; DTLATRSPKSARA; TLATRSPKSARAA; LATRSPKSARAAP; ATRSPKSARAAPM; TRSPKSARAAPMN; RSPKSARAAPMNL; SPKSARAAPMNLE; PKSARAAPMNLEI; KSARAAPMNLEIQ; SARAAPMNLEIQK; ARAAPMNLEIQKK; RAAPMNLEIQKKR; AAPMNLEIQKKRD; APMNLEIQKKRDY; PMNLEIQKKRDYL; MNLEIQKKRDYLP; NLEIQKKRDYLPR; LEIQKKRDYLPRS; EIQKKRDYLPRSL; IQKKRDYLPRSLL; QKKRDYLPRSLLQ; KKRDYLPRSLLQS; KRDYLPRSLLQSL; RDYLPRSLLQSLL; DYLPRSLLQSLLQ; YLPRSLLQSLLQQ; LPRSLLQSLLQQV; PRSLLQSLLQQVK; RSLLQSLLQQVKQ; SLLQSLLQQVKQW; LLQSLLQQVKQWY; LQSLLQQVKQWYF; QSLLQQVKQWYFC; SLLQQVKQWYFCF; LLQQVKQWYFCFS; LQQVKQWYFCFSR; QQVKQWYFCFSRL; QVKQWYFCFSRLH; VKQWYFCFSRLHC; KQWYFCFSRLHCL; QWYFCFSRLHCLH; WYFCFSRLHCLHL; YFCFSRLHCLHLY; FCFSRLHCLHLYK; CFSRLHCLHLYKI; FSRLHCLHLYKIP; SRLHCLHLYKIPA; RLHCLHLYKIPAK; LHCLHLYKIPAKA; HCLHLYKIPAKAL; CLHLYKIPAKALK; KSSELFFLFQSRF; SSELFFLFQSRFY; SELFFLFQSRFYQ; ELFFLFQSRFYQL; LFFLFQSRFYQLS; FFLFQSRFYQLSL; FLFQSRFYQLSLK; LFQSRFYQLSLKL; FQSRFYQLSLKLV; QSRFYQLSLKLVV; SRFYQLSLKLVVT; RFYQLSLKLVVTA; FYQLSLKLVVTAG; YQLSLKLVVTAGA; QLSLKLVVTAGAE; LSLKLVVTAGAEP; SLKLVVTAGAEPW; LKLVVTAGAEPWP; KLVVTAGAEPWPL; LVVTAGAEPWPLS; VVTAGAEPWPLSS; VTAGAEPWPLSSL; TAGAEPWPLSSLT; AGAEPWPLSSLTG; GAEPWPLSSLTGD; AEPWPLSSLTGDK; EPWPLSSLTGDKA; PWPLSSLTGDKAK; WPLSSLTGDKAKI; PLSSLTGDKAKIP; LSSLTGDKAKIPR; SSLTGDKAKIPRL; SLTGDKAKIPRLA; LTGDKAKIPRLAK; TGDKAKIPRLAKH; GDKAKIPRLAKHV; DKAKIPRLAKHVC; KAKIPRLAKHVCH; AKIPRLAKHVCHA; KIPRLAKHVCHAL; IPRLAKHVCHALS; PRLAKHVCHALSF; RLAKHVCHALSFL; LAKHVCHALSFLR; AKHVCHALSFLRS; KHVCHALSFLRSW; HVCHALSFLRSWF; VCHALSFLRSWFG; CHALSFLRSWFGC; HALSFLRSWFGCI; ALSFLRSWFGCIP; LSFLRSWFGCIPW; SFLRSWFGCIPWV; FLRSWFGCIPWVS; LRSWFGCIPWVSS; RSWFGCIPWVSSS; SWFGCIPWVSSSS; WFGCIPWVSSSSL; GHGLAAFPCESCT; HGLAAFPCESCTF; GLAAFPCESCTFL; LAAFPCESCTFLP; AAFPCESCTFLPE; AFPCESCTFLPEV; FPCESCTFLPEVM; PCESCTFLPEVMV; CESCTFLPEVMVW; ESCTFLPEVMVWL; SCTFLPEVMVWLH; CTFLPEVMVWLHS; TFLPEVMVWLHSM; FLPEVMVWLHSMG; LPEVMVWLHSMGK; PEVMVWLHSMGKQ; EVMVWLHSMGKQL; VMVWLHSMGKQLL; MVWLHSMGKQLLP; VWLHSMGKQLLPV; WLHSMGKQLLPVA; LHSMGKQLLPVAF; HSMGKQLLPVAFF; SMGKQLLPVAFFF; MGKQLLPVAFFFI; GKQLLPVAFFFII; KQLLPVAFFFIIY; QLLPVAFFFIIYK; LLPVAFFFIIYKR; LPVAFFFIIYKRP; PVAFFFIIYKRPR; VAFFFIIYKRPRP; AFFFIIYKRPRPP; FFFIIYKRPRPPL; FFIIYKRPRPPLP; FIIYKRPRPPLPP; IIYKRPRPPLPPP; IYKRPRPPLPPPF; YKRPRPPLPPPFL; KRPRPPLPPPFLS; RPRPPLPPPFLSS; PRPPLPPPFLSSS; RPPLPPPFLSSSK; PPLPPPFLSSSKG; PLPPPFLSSSKGV; LPPPFLSSSKGVE; PPPFLSSSKGVEA; PPFLSSSKGVEAF; PFLSSSKGVEAFS; FLSSSKGVEAFSE; LSSSKGVEAFSEA; QNYLGKSLFFCNF; NYLGKSLFFCNFC; YLGKSLFFCNFCK 14 mers: WIKFLTGKNPWSSW; IKFLTGKNPWSSWT; KFLTGKNPWSSWTF; GSVRNFTLTKGATR; SVRNFTLTKGATRI; VRNFTLTKGATRIK; LISLILEPGVAQRF; ISLILEPGVAQRFV; SLILEPGVAQRFVL; LILEPGVAQRFVLI; ILEPGVAQRFVLIF; LEPGVAQRFVLIFL; EPGVAQRFVLIFLF; PGVAQRFVLIFLFA; GVAQRFVLIFLFAQ; VAQRFVLIFLFAQI; AQRFVLIFLFAQIP; QRFVLIFLFAQIPC; RFVLIFLFAQIPCT; FVLIFLFAQIPCTA; VLIFLFAQIPCTAR; LIFLFAQIPCTARN; IFLFAQIPCTARNG; FLFAQIPCTARNGL; LFAQIPCTARNGLF; FAQIPCTARNGLFV; AQIPCTARNGLFVP; QIPCTARNGLFVPK; IPCTARNGLFVPKS; PCTARNGLFVPKSL; CTARNGLFVPKSLL; TARNGLFVPKSLLC; ARNGLFVPKSLLCT; RNGLFVPKSLLCTA; NGLFVPKSLLCTAL; GLFVPKSLLCTALA; LFVPKSLLCTALAC; FVPKSLLCTALACY; VPKSLLCTALACYV; PKSLLCTALACYVS; KSLLCTALACYVSL; SLLCTALACYVSLD; VIIFFIGANLWNRR; IIFFIGANLWNRRV; IFFIGANLWNRRVG; FFIGANLWNRRVGV; FIGANLWNRRVGVL; IGANLWNRRVGVLV; GANLWNRRVGVLVE; ANLWNRRVGVLVEF; NLWNRRVGVLVEFL; RSNSRFSTLNTTQK; SNSRFSTLNTTQKK; NSRFSTLNTTQKKK; SRFSTLNTTQKKKK; RFSTLNTTQKKKKG; FSTLNTTQKKKKGR; STLNTTQKKKKGRR; TLNTTQKKKKGRRP; RSIPYYRRKHSRGL; SIPYYRRKHSRGLK; IPYYRRKHSRGLKG; PYYRRKHSRGLKGA; GCVFIIRYVFRISI; CVFIIRYVFRISIQ; VFIIRYVFRISIQC; FIIRYVFRISIQCR; IIRYVFRISIQCRG; IRYVFRISIQCRGV; KSKKYLSASSRYSF; SKKYLSASSRYSFS; KKSRYPSYDQGRNA; KSRYPSYDQGRNAN; SRYPSYDQGRNANR; RYPSYDQGRNANRK; YPSYDQGRNANRKI; PSYDQGRNANRKIQ; SYDQGRNANRKIQS; YDQGRNANRKIQSY; DQGRNANRKIQSYI; QGRNANRKIQSYIR; NGFNIWSSWKCCTR; GFNIWSSWKCCTRT; FNIWSSWKCCTRTI; NIWSSWKCCTRTIY; IWSSWKCCTRTIYG; WSSWKCCTRTIYGR; SSWKCCTRTIYGRC; SWKCCTRTIYGRCC; WKCCTRTIYGRCCL; KCCTRTIYGRCCLA; CCTRTIYGRCCLAA; CTRTIYGRCCLAAL; TRTIYGRCCLAALF; RTIYGRCCLAALFA; TIYGRCCLAALFAT; WKNNTSCRVIRFVW; KNNTSCRVIRFVWW; IKGFAFRTWNKQFR; KGFAFRTWNKQFRQ; GFAFRTWNKQFRQF; FAFRTWNKQFRQFE; AFRTWNKQFRQFER; FRTWNKQFRQFERL; RTWNKQFRQFERLF; TWNKQFRQFERLFR; WNKQFRQFERLFRW; NKQFRQFERLFRWK; KQFRQFERLFRWKC; GKFRKETFKQKNPN; KFRKETFKQKNPNI; FRKETFKQKNPNIS; RKETFKQKNPNIST; KETFKQKNPNISTR; ETFKQKNPNISTRL; TFKQKNPNISTRLG; FKQKNPNISTRLGY; KQKNPNISTRLGYN; QKNPNISTRLGYNE; AQNIFKKILTKLRV; QNIFKKILTKLRVL; NIFKKILTKLRVLT; KKNFTKWNDLVATA; KNFTKWNDLVATAN; NFTKWNDLVATANL; FTKWNDLVATANLV; IPITMLFPSLRYFS; PITMLFPSLRYFSP; ITMLFPSLRYFSPC; KWLIQKQHLLNVYV; WLIQKQHLLNVYVQ; KHLFKAFWFAIVPV; HLFKAFWFAIVPVC; LFKAFWFAIVPVCQ; FKAFWFAIVPVCQY; KAFWFAIVPVCQYI; AFWFAIVPVCQYIL; FWFAIVPVCQYILS; WFAIVPVCQYILSY; FAIVPVCQYILSYL; AIVPVCQYILSYLG; IVPVCQYILSYLGP; VPVCQYILSYLGPL; PVCQYILSYLGPLE; VCQYILSYLGPLEV; CQYILSYLGPLEVF; QYILSYLGPLEVFL; YILSYLGPLEVFLC; ILSYLGPLEVFLCH; LSYLGPLEVFLCHQ; SYLGPLEVFLCHQT; YLGPLEVFLCHQTP; GHLAKRKLGKDSLQ; HLAKRKLGKDSLQI; LAKRKLGKDSLQIF; AKRKLGKDSLQIFF; KRKLGKDSLQIFFS; RKLGKDSLQIFFSG; KLGKDSLQIFFSGG; LGKDSLQIFFSGGS; NILQGLSTVVFQSC; TGHKYQQLKHTGYQ; GHKYQQLKHTGYQL; HKYQQLKHTGYQLY; KYQQLKHTGYQLYK; YQQLKHTGYQLYKE; QQLKHTGYQLYKEA; QLKHTGYQLYKEAP; LKHTGYQLYKEAPH; KHTGYQLYKEAPHP; HTGYQLYKEAPHPV; TGYQLYKEAPHPVH; GYQLYKEAPHPVHL; YQLYKEAPHPVHLA; QLYKEAPHPVHLAT; LYKEAPHPVHLATL; YKEAPHPVHLATLW; LCWSHEVLGEHFPL; CWSHEVLGEHFPLL; HFHFYWDQVPSTQL; FHFYWDQVPSTQLD; HFYWDQVPSTQLDK; FYWDQVPSTQLDKH; YWDQVPSTQLDKHC; WDQVPSTQLDKHCF; DQVPSTQLDKHCFC; QVPSTQLDKHCFCP; VPSTQLDKHCFCPN; PSTQLDKHCFCPNR; STQLDKHCFCPNRP; TQLDKHCFCPNRPY; QLDKHCFCPNRPYG; LDKHCFCPNRPYGQ; DKHCFCPNRPYGQY; KHCFCPNRPYGQYS; HCFCPNRPYGQYSL; CFCPNRPYGQYSLP; FCPNRPYGQYSLPG; CPNRPYGQYSLPGT; PNRPYGQYSLPGTG; NRPYGQYSLPGTGL; RPYGQYSLPGTGLL; PYGQYSLPGTGLLG; YGQYSLPGTGLLGF; YHQGTLTCNSLALP; HQGTLTCNSLALPA; QGTLTCNSLALPAF; GTLTCNSLALPAFP; TLTCNSLALPAFPR; LTCNSLALPAFPRV; TCNSLALPAFPRVL; CNSLALPAFPRVLH; NSLALPAFPRVLHL; SLALPAFPRVLHLQ; LALPAFPRVLHLQQ; ALPAFPRVLHLQQR; LPAFPRVLHLQQRS; PAFPRVLHLQQRSG; AFPRVLHLQQRSGN; FPRVLHLQQRSGNY; PRVLHLQQRSGNYC; RVLHLQQRSGNYCL; VLHLQQRSGNYCLE; VFLHHAHALFVTLH; FLHHAHALFVTLHE; LHHAHALFVTLHEG; PLFVQLQPPTSVDF; LFVQLQPPTSVDFH; FVQLQPPTSVDFHR; VQLQPPTSVDFHRL; QLQPPTSVDFHRLG; LQPPTSVDFHRLGP; QPPTSVDFHRLGPH; PPTSVDFHRLGPHL; PTSVDFHRLGPHLN; TSVDFHRLGPHLNW; SVDFHRLGPHLNWG; VDFHRLGPHLNWGG; DFHRLGPHLNWGGE; FHRLGPHLNWGGEF; HRLGPHLNWGGEFL; RLGPHLNWGGEFLL; LGPHLNWGGEFLLC; GPHLNWGGEFLLCC; PHLNWGGEFLLCCN; HLNWGGEFLLCCNR; LNWGGEFLLCCNRE; NWGGEFLLCCNREA; WGGEFLLCCNREAF; GGEFLLCCNREAFF; GEFLLCCNREAFFS; EFLLCCNREAFFSL; FLLCCNREAFFSLG; LLCCNREAFFSLGY; LCCNREAFFSLGYH; CCNREAFFSLGYHC; GFHLDPPFLGLGSI; FHLDPPFLGLGSIL; HLDPPFLGLGSILP; LDPPFLGLGSILPL; LLELLLLLLLVVLA; LELLLLLLLVVLAL; ELLLLLLLVVLALA; LLLLLLLVVLALAR; LLLLLLVVLALARV; LLLLLVVLALARVP; LLLLVVLALARVPL; LLLVVLALARVPLA; LLVVLALARVPLAF; LVVLALARVPLAFW; VVLALARVPLAFWE; VLALARVPLAFWEL; LALARVPLAFWELP; ALARVPLAFWELPL; LARVPLAFWELPLD; ARVPLAFWELPLDT; RVPLAFWELPLDTL; VPLAFWELPLDTLL; PLAFWELPLDTLLF; LAFWELPLDTLLFF; AFWELPLDTLLFFW; FWELPLDTLLFFWL; WELPLDTLLFFWLG; ELPLDTLLFFWLGP; LPLDTLLFFWLGPS; PLDTLLFFWLGPSS; LDTLLFFWLGPSSY; DTLLFFWLGPSSYA; TLLFFWLGPSSYAS; LLFFWLGPSSYASR; LFFWLGPSSYASRA; FFWLGPSSYASRAG; FWLGPSSYASRAGV; WLGPSSYASRAGVT; LGPSSYASRAGVTV; GPSSYASRAGVTVP; PSSYASRAGVTVPY; SSYASRAGVTVPYR; SYASRAGVTVPYRP; YASRAGVTVPYRPR; ASRAGVTVPYRPRS; SRAGVTVPYRPRSK; RAGVTVPYRPRSKG; AGVTVPYRPRSKGN; GVTVPYRPRSKGNI; VTVPYRPRSKGNIH; LAPPGAIVFSINSP; APPGAIVFSINSPE; PPGAIVFSINSPEC; PGAIVFSINSPECT; GAIVFSINSPECTL; AIVFSINSPECTLC; FLKSILCVTSSILS; LKSILCVTSSILSA; KSILCVTSSILSAS; SILCVTSSILSASS; ILCVTSSILSASSI; LCVTSSILSASSIL; VWPKCTRVPSLSAT; WPKCTRVPSLSATC; PKCTRVPSLSATCL; KCTRVPSLSATCLT; CTRVPSLSATCLTI; TRVPSLSATCLTIE; RVPSLSATCLTIEG; VPSLSATCLTIEGL; PSLSATCLTIEGLI; SLSATCLTIEGLIG; LSATCLTIEGLIGE; SATCLTIEGLIGER; ATCLTIEGLIGERS; TCLTIEGLIGERSE; KFIGAFTIVQVVSS; FIGAFTIVQVVSSK; IGAFTIVQVVSSKN; GAFTIVQVVSSKNL; AFTIVQVVSSKNLA; FTIVQVVSSKNLAK; TIVQVVSSKNLAKE; IVQVVSSKNLAKES; VQVVSSKNLAKESL; QVVSSKNLAKESLK; VVSSKNLAKESLKN; VSSKNLAKESLKNL; SSKNLAKESLKNLS; SKNLAKESLKNLSV; KNLAKESLKNLSVL; NLAKESLKNLSVLL; LAKESLKNLSVLLC; AKESLKNLSVLLCN; KESLKNLSVLLCNS; ESLKNLSVLLCNSC; SLKNLSVLLCNSCE; LKNLSVLLCNSCEV; KNLSVLLCNSCEVI; NLSVLLCNSCEVIE; LSVLLCNSCEVIEG; SVLLCNSCEVIEGI; VLLCNSCEVIEGIS; LLCNSCEVIEGISS; LCNSCEVIEGISSL; CNSCEVIEGISSLI; NSCEVIEGISSLIT; SCEVIEGISSLITC; CEVIEGISSLITCH; EVIEGISSLITCHK; VIEGISSLITCHKA; IEGISSLITCHKAW; EGISSLITCHKAWE; GISSLITCHKAWEI; ISSLITCHKAWEIV; SSLITCHKAWEIVA; SLITCHKAWEIVAN; LITCHKAWEIVANK; ITCHKAWEIVANKE; TCHKAWEIVANKEG; CHKAWEIVANKEGP; HKAWEIVANKEGPQ; KAWEIVANKEGPQC; AWEIVANKEGPQCL; WEIVANKEGPQCLG; EIVANKEGPQCLGS; IVANKEGPQCLGSR; VANKEGPQCLGSRY; ILLTKVFTPGNRIS; YSSGLNNSKAMPDC; IKAANPAIAPGAPA; KAANPAIAPGAPAI; AANPAIAPGAPAIT; ANPAIAPGAPAITA; NPAIAPGAPAITAY; PAIAPGAPAITAYV; GVRPIAAIASEVLV; VRPIAAIASEVLVM; RPIAAIASEVLVMP; PIAAIASEVLVMPS; IAAIASEVLVMPST; AAIASEVLVMPSTV; AIASEVLVMPSTVA; IASEVLVMPSTVAR; ASEVLVMPSTVARD; SEVLVMPSTVARDA; EVLVMPSTVARDAI; TSIAAAASPAAISA; SIAAAASPAAISAT; IAAAASPAAISATE; AAAASPAAISATEN; AAASPAAISATENP; AASPAAISATENPV; ASPAAISATENPVA; SPAAISATENPVAA; PAAISATENPVAAA; AAISATENPVAAAA; AISATENPVAAAAS; ISATENPVAAAASD; SATENPVAAAASDT; ATENPVAAAASDTL; TENPVAAAASDTLA; ENPVAAAASDTLAT; NPVAAAASDTLATR; PVAAAASDTLATRS; VAAAASDTLATRSP; AAAASDTLATRSPK; AAASDTLATRSPKS; AASDTLATRSPKSA; ASDTLATRSPKSAR; SDTLATRSPKSARA; DTLATRSPKSARAA; TLATRSPKSARAAP; LATRSPKSARAAPM; ATRSPKSARAAPMN; TRSPKSARAAPMNL; RSPKSARAAPMNLE; SPKSARAAPMNLEI; PKSARAAPMNLEIQ; KSARAAPMNLEIQK; SARAAPMNLEIQKK; ARAAPMNLEIQKKR; RAAPMNLEIQKKRD; AAPMNLEIQKKRDY; APMNLEIQKKRDYL; PMNLEIQKKRDYLP; MNLEIQKKRDYLPR; NLEIQKKRDYLPRS; LEIQKKRDYLPRSL; EIQKKRDYLPRSLL; IQKKRDYLPRSLLQ; QKKRDYLPRSLLQS; KKRDYLPRSLLQSL; KRDYLPRSLLQSLL; RDYLPRSLLQSLLQ; DYLPRSLLQSLLQQ; YLPRSLLQSLLQQV; LPRSLLQSLLQQVK; PRSLLQSLLQQVKQ; RSLLQSLLQQVKQW; SLLQSLLQQVKQWY; LLQSLLQQVKQWYF; LQSLLQQVKQWYFC; QSLLQQVKQWYFCF; SLLQQVKQWYFCFS; LLQQVKQWYFCFSR; LQQVKQWYFCFSRL; QQVKQWYFCFSRLH; QVKQWYFCFSRLHC; VKQWYFCFSRLHCL; KQWYFCFSRLHCLH; QWYFCFSRLHCLHL; WYFCFSRLHCLHLY; YFCFSRLHCLHLYK; FCFSRLHCLHLYKI; CFSRLHCLHLYKIP; FSRLHCLHLYKIPA; SRLHCLHLYKIPAK; RLHCLHLYKIPAKA; LHCLHLYKIPAKAL; HCLHLYKIPAKALK; KSSELFFLFQSRFY; SSELFFLFQSRFYQ; SELFFLFQSRFYQL; ELFFLFQSRFYQLS; LFFLFQSRFYQLSL; FFLFQSRFYQLSLK; FLFQSRFYQLSLKL; LFQSRFYQLSLKLV; FQSRFYQLSLKLVV; QSRFYQLSLKLVVT; SRFYQLSLKLVVTA; RFYQLSLKLVVTAG; FYQLSLKLVVTAGA; YQLSLKLVVTAGAE; QLSLKLVVTAGAEP; LSLKLVVTAGAEPW; SLKLVVTAGAEPWP; LKLVVTAGAEPWPL; KLVVTAGAEPWPLS; LVVTAGAEPWPLSS; VVTAGAEPWPLSSL; VTAGAEPWPLSSLT; TAGAEPWPLSSLTG; AGAEPWPLSSLTGD; GAEPWPLSSLTGDK; AEPWPLSSLTGDKA; EPWPLSSLTGDKAK; PWPLSSLTGDKAKI; WPLSSLTGDKAKIP; PLSSLTGDKAKIPR; LSSLTGDKAKIPRL; SSLTGDKAKIPRLA; SLTGDKAKIPRLAK; LTGDKAKIPRLAKH; TGDKAKIPRLAKHV; GDKAKIPRLAKHVC; DKAKIPRLAKHVCH; KAKIPRLAKHVCHA; AKIPRLAKHVCHAL; KIPRLAKHVCHALS; IPRLAKHVCHALSF; PRLAKHVCHALSFL; RLAKHVCHALSFLR; LAKHVCHALSFLRS; AKHVCHALSFLRSW; KHVCHALSFLRSWF; HVCHALSFLRSWFG; VCHALSFLRSWFGC; CHALSFLRSWFGCI; HALSFLRSWFGCIP; ALSFLRSWFGCIPW; LSFLRSWFGCIPWV; SFLRSWFGCIPWVS; FLRSWFGCIPWVSS; LRSWFGCIPWVSSS; RSWFGCIPWVSSSS; SWFGCIPWVSSSSL; GHGLAAFPCESCTF; HGLAAFPCESCTFL; GLAAFPCESCTFLP; LAAFPCESCTFLPE; AAFPCESCTFLPEV; AFPCESCTFLPEVM; FPCESCTFLPEVMV; PCESCTFLPEVMVW; CESCTFLPEVMVWL; ESCTFLPEVMVWLH; SCTFLPEVMVWLHS; CTFLPEVMVWLHSM; TFLPEVMVWLHSMG; FLPEVMVWLHSMGK; LPEVMVWLHSMGKQ; PEVMVWLHSMGKQL; EVMVWLHSMGKQLL; VMVWLHSMGKQLLP; MVWLHSMGKQLLPV; VWLHSMGKQLLPVA; WLHSMGKQLLPVAF; LHSMGKQLLPVAFF; HSMGKQLLPVAFFF; SMGKQLLPVAFFFI; MGKQLLPVAFFFII; GKQLLPVAFFFIIY; KQLLPVAFFFIIYK; QLLPVAFFFIIYKR; LLPVAFFFIIYKRP; LPVAFFFIIYKRPR; PVAFFFIIYKRPRP; VAFFFIIYKRPRPP; AFFFIIYKRPRPPL; FFFIIYKRPRPPLP; FFIIYKRPRPPLPP; FIIYKRPRPPLPPP; IIYKRPRPPLPPPF; IYKRPRPPLPPPFL; YKRPRPPLPPPFLS; KRPRPPLPPPFLSS; RPRPPLPPPFLSSS; PRPPLPPPFLSSSK; RPPLPPPFLSSSKG; PPLPPPFLSSSKGV; PLPPPFLSSSKGVE; LPPPFLSSSKGVEA; PPPFLSSSKGVEAF; PPFLSSSKGVEAFS; PFLSSSKGVEAFSE; FLSSSKGVEAFSEA; QNYLGKSLFFCNFC; NYLGKSLFFCNFCK 15 mers: WIKFLTGKNPWSSWT; IKFLTGKNPWSSWTF; GSVRNFTLTKGATRI; SVRNFTLTKGATRIK; LISLILEPGVAQRFV; ISLILEPGVAQRFVL; SLILEPGVAQRFVLI; LILEPGVAQRFVLIF; ILEPGVAQRFVLIFL; LEPGVAQRFVLIFLF; EPGVAQRFVLIFLFA; PGVAQRFVLIFLFAQ; GVAQRFVLIFLFAQI; VAQRFVLIFLFAQIP; AQRFVLIFLFAQIPC; QRFVLIFLFAQIPCT; RFVLIFLFAQIPCTA; FVLIFLFAQIPCTAR; VLIFLFAQIPCTARN; LIFLFAQIPCTARNG; IFLFAQIPCTARNGL; FLFAQIPCTARNGLF; LFAQIPCTARNGLFV; FAQIPCTARNGLFVP; AQIPCTARNGLFVPK; QIPCTARNGLFVPKS; IPCTARNGLFVPKSL; PCTARNGLFVPKSLL; CTARNGLFVPKSLLC; TARNGLFVPKSLLCT; ARNGLFVPKSLLCTA; RNGLFVPKSLLCTAL; NGLFVPKSLLCTALA; GLFVPKSLLCTALAC; LFVPKSLLCTALACY; FVPKSLLCTALACYV; VPKSLLCTALACYVS; PKSLLCTALACYVSL; KSLLCTALACYVSLD; VIIFFIGANLWNRRV; IIFFIGANLWNRRVG; IFFIGANLWNRRVGV; FFIGANLWNRRVGVL; FIGANLWNRRVGVLV; IGANLWNRRVGVLVE; GANLWNRRVGVLVEF; ANLWNRRVGVLVEFL; RSNSRFSTLNTTQKK; SNSRFSTLNTTQKKK; NSRFSTLNTTQKKKK; SRFSTLNTTQKKKKG; RFSTLNTTQKKKKGR; FSTLNTTQKKKKGRR; STLNTTQKKKKGRRP; RSIPYYRRKHSRGLK; SIPYYRRKHSRGLKG; IPYYRRKHSRGLKGA; GCVFIIRYVFRISIQ; CVFIIRYVFRISIQC; VFIIRYVFRISIQCR; FIIRYVFRISIQCRG; IIRYVFRISIQCRGV; KSKKYLSASSRYSFS; KKSRYPSYDQGRNAN; KSRYPSYDQGRNANR; SRYPSYDQGRNANRK; RYPSYDQGRNANRKI; YPSYDQGRNANRKIQ; PSYDQGRNANRKIQS; SYDQGRNANRKIQSY; YDQGRNANRKIQSYI; DQGRNANRKIQSYIR; NGFNIWSSWKCCTRT; GFNIWSSWKCCTRTI; FNIWSSWKCCTRTIY; NIWSSWKCCTRTIYG; IWSSWKCCTRTIYGR; WSSWKCCTRTIYGRC; SSWKCCTRTIYGRCC; SWKCCTRTIYGRCCL; WKCCTRTIYGRCCLA; KCCTRTIYGRCCLAA; CCTRTIYGRCCLAAL; CTRTIYGRCCLAALF; TRTIYGRCCLAALFA; RTIYGRCCLAALFAT; WKNNTSCRVIRFVWW; IKGFAFRTWNKQFRQ; KGFAFRTWNKQFRQF; GFAFRTWNKQFRQFE; FAFRTWNKQFRQFER; AFRTWNKQFRQFERL; FRTWNKQFRQFERLF; RTWNKQFRQFERLFR; TWNKQFRQFERLFRW; WNKQFRQFERLFRWK; NKQFRQFERLFRWKC; GKFRKETFKQKNPNI; KFRKETFKQKNPNIS; FRKETFKQKNPNIST; RKETFKQKNPNISTR; KETFKQKNPNISTRL; ETFKQKNPNISTRLG; TFKQKNPNISTRLGY; FKQKNPNISTRLGYN; KQKNPNISTRLGYNE; AQNIFKKILTKLRVL; QNIFKKILTKLRVLT; KKNFTKWNDLVATAN; KNFTKWNDLVATANL; NFTKWNDLVATANLV; IPITMLFPSLRYFSP; PITMLFPSLRYFSPC; KWLIQKQHLLNVYVQ; KHLFKAFWFAIVPVC; HLFKAFWFAIVPVCQ; LFKAFWFAIVPVCQY; FKAFWFAIVPVCQYI; KAFWFAIVPVCQYIL; AFWFAIVPVCQYILS; FWFAIVPVCQYILSY; WFAIVPVCQYILSYL; FAIVPVCQYILSYLG; AIVPVCQYILSYLGP; IVPVCQYILSYLGPL; VPVCQYILSYLGPLE; PVCQYILSYLGPLEV; VCQYILSYLGPLEVF; CQYILSYLGPLEVFL; QYILSYLGPLEVFLC; YILSYLGPLEVFLCH; ILSYLGPLEVFLCHQ; LSYLGPLEVFLCHQT; SYLGPLEVFLCHQTP; GHLAKRKLGKDSLQI; HLAKRKLGKDSLQIF; LAKRKLGKDSLQIFF; AKRKLGKDSLQIFFS; KRKLGKDSLQIFFSG; RKLGKDSLQIFFSGG; KLGKDSLQIFFSGGS; TGHKYQQLKHTGYQL; GHKYQQLKHTGYQLY; HKYQQLKHTGYQLYK; KYQQLKHTGYQLYKE; YQQLKHTGYQLYKEA; QQLKHTGYQLYKEAP; QLKHTGYQLYKEAPH; LKHTGYQLYKEAPHP; KHTGYQLYKEAPHPV; HTGYQLYKEAPHPVH; TGYQLYKEAPHPVHL; GYQLYKEAPHPVHLA; YQLYKEAPHPVHLAT; QLYKEAPHPVHLATL; LYKEAPHPVHLATLW; LCWSHEVLGEHFPLL; HFHFYWDQVPSTQLD; FHFYWDQVPSTQLDK; HFYWDQVPSTQLDKH; FYWDQVPSTQLDKHC; YWDQVPSTQLDKHCF; WDQVPSTQLDKHCFC; DQVPSTQLDKHCFCP; QVPSTQLDKHCFCPN; VPSTQLDKHCFCPNR; PSTQLDKHCFCPNRP; STQLDKHCFCPNRPY; TQLDKHCFCPNRPYG; QLDKHCFCPNRPYGQ; LDKHCFCPNRPYGQY; DKHCFCPNRPYGQYS; KHCFCPNRPYGQYSL; HCFCPNRPYGQYSLP; CFCPNRPYGQYSLPG; FCPNRPYGQYSLPGT; CPNRPYGQYSLPGTG; PNRPYGQYSLPGTGL; NRPYGQYSLPGTGLL; RPYGQYSLPGTGLLG; PYGQYSLPGTGLLGF; YHQGTLTCNSLALPA; HQGTLTCNSLALPAF; QGTLTCNSLALPAFP; GTLTCNSLALPAFPR; TLTCNSLALPAFPRV; LTCNSLALPAFPRVL; TCNSLALPAFPRVLH; CNSLALPAFPRVLHL; NSLALPAFPRVLHLQ; SLALPAFPRVLHLQQ; LALPAFPRVLHLQQR; ALPAFPRVLHLQQRS; LPAFPRVLHLQQRSG; PAFPRVLHLQQRSGN; AFPRVLHLQQRSGNY; FPRVLHLQQRSGNYC; PRVLHLQQRSGNYCL; RVLHLQQRSGNYCLE; VFLHHAHALFVTLHE; FLHHAHALFVTLHEG; PLFVQLQPPTSVDFH; LFVQLQPPTSVDFHR; FVQLQPPTSVDFHRL; VQLQPPTSVDFHRLG; QLQPPTSVDFHRLGP; LQPPTSVDFHRLGPH; QPPTSVDFHRLGPHL; PPTSVDFHRLGPHLN; PTSVDFHRLGPHLNW; TSVDFHRLGPHLNWG; SVDFHRLGPHLNWGG; VDFHRLGPHLNWGGE; DFHRLGPHLNWGGEF; FHRLGPHLNWGGEFL; HRLGPHLNWGGEFLL; RLGPHLNWGGEFLLC; LGPHLNWGGEFLLCC; GPHLNWGGEFLLCCN; PHLNWGGEFLLCCNR; HLNWGGEFLLCCNRE; LNWGGEFLLCCNREA; NWGGEFLLCCNREAF; WGGEFLLCCNREAFF; GGEFLLCCNREAFFS; GEFLLCCNREAFFSL; EFLLCCNREAFFSLG; FLLCCNREAFFSLGY; LLCCNREAFFSLGYH; LCCNREAFFSLGYHC; GFHLDPPFLGLGSIL; FHLDPPFLGLGSILP; HLDPPFLGLGSILPL; LLELLLLLLLVVLAL; LELLLLLLLVVLALA; ELLLLLLLVVLALAR; LLLLLLLVVLALARV; LLLLLLVVLALARVP; LLLLLVVLALARVPL; LLLLVVLALARVPLA; LLLVVLALARVPLAF; LLVVLALARVPLAFW; LVVLALARVPLAFWE; VVLALARVPLAFWEL; VLALARVPLAFWELP; LALARVPLAFWELPL; ALARVPLAFWELPLD; LARVPLAFWELPLDT; ARVPLAFWELPLDTL; RVPLAFWELPLDTLL; VPLAFWELPLDTLLF; PLAFWELPLDTLLFF; LAFWELPLDTLLFFW; AFWELPLDTLLFFWL; FWELPLDTLLFFWLG; WELPLDTLLFFWLGP; ELPLDTLLFFWLGPS; LPLDTLLFFWLGPSS; PLDTLLFFWLGPSSY; LDTLLFFWLGPSSYA; DTLLFFWLGPSSYAS; TLLFFWLGPSSYASR; LLFFWLGPSSYASRA; LFFWLGPSSYASRAG; FFWLGPSSYASRAGV; FWLGPSSYASRAGVT; WLGPSSYASRAGVTV; LGPSSYASRAGVTVP; GPSSYASRAGVTVPY; PSSYASRAGVTVPYR; SSYASRAGVTVPYRP; SYASRAGVTVPYRPR; YASRAGVTVPYRPRS; ASRAGVTVPYRPRSK; SRAGVTVPYRPRSKG; RAGVTVPYRPRSKGN; AGVTVPYRPRSKGNI; GVTVPYRPRSKGNIH; LAPPGAIVFSINSPE; APPGAIVFSINSPEC; PPGAIVFSINSPECT; PGAIVFSINSPECTL; GAIVFSINSPECTLC; FLKSILCVTSSILSA; LKSILCVTSSILSAS; KSILCVTSSILSASS; SILCVTSSILSASSI; ILCVTSSILSASSIL; VWPKCTRVPSLSATC; WPKCTRVPSLSATCL; PKCTRVPSLSATCLT; KCTRVPSLSATCLTI; CTRVPSLSATCLTIE; TRVPSLSATCLTIEG; RVPSLSATCLTIEGL; VPSLSATCLTIEGLI; PSLSATCLTIEGLIG; SLSATCLTIEGLIGE; LSATCLTIEGLIGER; SATCLTIEGLIGERS; ATCLTIEGLIGERSE; KFIGAFTIVQVVSSK; FIGAFTIVQVVSSKN; IGAFTIVQVVSSKNL; GAFTIVQVVSSKNLA; AFTIVQVVSSKNLAK; FTIVQVVSSKNLAKE; TIVQVVSSKNLAKES; IVQVVSSKNLAKESL; VQVVSSKNLAKESLK; QVVSSKNLAKESLKN; VVSSKNLAKESLKNL; VSSKNLAKESLKNLS; SSKNLAKESLKNLSV; SKNLAKESLKNLSVL; KNLAKESLKNLSVLL; NLAKESLKNLSVLLC; LAKESLKNLSVLLCN; AKESLKNLSVLLCNS; KESLKNLSVLLCNSC; ESLKNLSVLLCNSCE; SLKNLSVLLCNSCEV; LKNLSVLLCNSCEVI; KNLSVLLCNSCEVIE; NLSVLLCNSCEVIEG; LSVLLCNSCEVIEGI; SVLLCNSCEVIEGIS; VLLCNSCEVIEGISS; LLCNSCEVIEGISSL; LCNSCEVIEGISSLI; CNSCEVIEGISSLIT; NSCEVIEGISSLITC; SCEVIEGISSLITCH; CEVIEGISSLITCHK; EVIEGISSLITCHKA; VIEGISSLITCHKAW; IEGISSLITCHKAWE; EGISSLITCHKAWEI; GISSLITCHKAWEIV; ISSLITCHKAWEIVA; SSLITCHKAWEIVAN; SLITCHKAWEIVANK; LITCHKAWEIVANKE; ITCHKAWEIVANKEG; TCHKAWEIVANKEGP; CHKAWEIVANKEGPQ; HKAWEIVANKEGPQC; KAWEIVANKEGPQCL; AWEIVANKEGPQCLG; WEIVANKEGPQCLGS; EIVANKEGPQCLGSR; IVANKEGPQCLGSRY; IKAANPAIAPGAPAI; KAANPAIAPGAPAIT; AANPAIAPGAPAITA; ANPAIAPGAPAITAY; NPAIAPGAPAITAYV; GVRPIAAIASEVLVM; VRPIAAIASEVLVMP; RPIAAIASEVLVMPS; PIAAIASEVLVMPST; IAAIASEVLVMPSTV; AAIASEVLVMPSTVA; AIASEVLVMPSTVAR; IASEVLVMPSTVARD; ASEVLVMPSTVARDA; SEVLVMPSTVARDAI; TSIAAAASPAAISAT; SIAAAASPAAISATE; IAAAASPAAISATEN; AAAASPAAISATENP; AAASPAAISATENPV; AASPAAISATENPVA; ASPAAISATENPVAA; SPAAISATENPVAAA; PAAISATENPVAAAA; AAISATENPVAAAAS; AISATENPVAAAASD; ISATENPVAAAASDT; SATENPVAAAASDTL; ATENPVAAAASDTLA; TENPVAAAASDTLAT; ENPVAAAASDTLATR; NPVAAAASDTLATRS; PVAAAASDTLATRSP; VAAAASDTLATRSPK; AAAASDTLATRSPKS; AAASDTLATRSPKSA; AASDTLATRSPKSAR; ASDTLATRSPKSARA; SDTLATRSPKSARAA; DTLATRSPKSARAAP; TLATRSPKSARAAPM; LATRSPKSARAAPMN; ATRSPKSARAAPMNL; TRSPKSARAAPMNLE; RSPKSARAAPMNLEI; SPKSARAAPMNLEIQ; PKSARAAPMNLEIQK; KSARAAPMNLEIQKK; SARAAPMNLEIQKKR; ARAAPMNLEIQKKRD; RAAPMNLEIQKKRDY; AAPMNLEIQKKRDYL; APMNLEIQKKRDYLP; PMNLEIQKKRDYLPR; MNLEIQKKRDYLPRS; NLEIQKKRDYLPRSL; LEIQKKRDYLPRSLL; EIQKKRDYLPRSLLQ; IQKKRDYLPRSLLQS; QKKRDYLPRSLLQSL; KKRDYLPRSLLQSLL; KRDYLPRSLLQSLLQ; RDYLPRSLLQSLLQQ; DYLPRSLLQSLLQQV; YLPRSLLQSLLQQVK; LPRSLLQSLLQQVKQ; PRSLLQSLLQQVKQW; RSLLQSLLQQVKQWY; SLLQSLLQQVKQWYF; LLQSLLQQVKQWYFC; LQSLLQQVKQWYFCF; QSLLQQVKQWYFCFS; SLLQQVKQWYFCFSR; LLQQVKQWYFCFSRL; LQQVKQWYFCFSRLH; QQVKQWYFCFSRLHC; QVKQWYFCFSRLHCL; VKQWYFCFSRLHCLH; KQWYFCFSRLHCLHL; QWYFCFSRLHCLHLY; WYFCFSRLHCLHLYK; YFCFSRLHCLHLYKI; FCFSRLHCLHLYKIP; CFSRLHCLHLYKIPA; FSRLHCLHLYKIPAK; SRLHCLHLYKIPAKA; RLHCLHLYKIPAKAL; LHCLHLYKIPAKALK; KSSELFFLFQSRFYQ; SSELFFLFQSRFYQL; SELFFLFQSRFYQLS; ELFFLFQSRFYQLSL; LFFLFQSRFYQLSLK; FFLFQSRFYQLSLKL; FLFQSRFYQLSLKLV; LFQSRFYQLSLKLVV; FQSRFYQLSLKLVVT; QSRFYQLSLKLVVTA; SRFYQLSLKLVVTAG; RFYQLSLKLVVTAGA; FYQLSLKLVVTAGAE; YQLSLKLVVTAGAEP; QLSLKLVVTAGAEPW; LSLKLVVTAGAEPWP; SLKLVVTAGAEPWPL; LKLVVTAGAEPWPLS; KLVVTAGAEPWPLSS; LVVTAGAEPWPLSSL; VVTAGAEPWPLSSLT; VTAGAEPWPLSSLTG; TAGAEPWPLSSLTGD; AGAEPWPLSSLTGDK; GAEPWPLSSLTGDKA; AEPWPLSSLTGDKAK; EPWPLSSLTGDKAKI; PWPLSSLTGDKAKIP; WPLSSLTGDKAKIPR; PLSSLTGDKAKIPRL; LSSLTGDKAKIPRLA; SSLTGDKAKIPRLAK; SLTGDKAKIPRLAKH; LTGDKAKIPRLAKHV; TGDKAKIPRLAKHVC; GDKAKIPRLAKHVCH; DKAKIPRLAKHVCHA; KAKIPRLAKHVCHAL; AKIPRLAKHVCHALS; KIPRLAKHVCHALSF; IPRLAKHVCHALSFL; PRLAKHVCHALSFLR; RLAKHVCHALSFLRS; LAKHVCHALSFLRSW; AKHVCHALSFLRSWF; KHVCHALSFLRSWFG; HVCHALSFLRSWFGC; VCHALSFLRSWFGCI; CHALSFLRSWFGCIP; HALSFLRSWFGCIPW; ALSFLRSWFGCIPWV; LSFLRSWFGCIPWVS; SFLRSWFGCIPWVSS; FLRSWFGCIPWVSSS; LRSWFGCIPWVSSSS; RSWFGCIPWVSSSSL; GHGLAAFPCESCTFL; HGLAAFPCESCTFLP; GLAAFPCESCTFLPE; LAAFPCESCTFLPEV; AAFPCESCTFLPEVM; AFPCESCTFLPEVMV; FPCESCTFLPEVMVW; PCESCTFLPEVMVWL; CESCTFLPEVMVWLH; ESCTFLPEVMVWLHS; SCTFLPEVMVWLHSM; CTFLPEVMVWLHSMG; TFLPEVMVWLHSMGK; FLPEVMVWLHSMGKQ; LPEVMVWLHSMGKQL; PEVMVWLHSMGKQLL; EVMVWLHSMGKQLLP; VMVWLHSMGKQLLPV; MVWLHSMGKQLLPVA; VWLHSMGKQLLPVAF; WLHSMGKQLLPVAFF; LHSMGKQLLPVAFFF; HSMGKQLLPVAFFFI; SMGKQLLPVAFFFII; MGKQLLPVAFFFIIY; GKQLLPVAFFFIIYK; KQLLPVAFFFIIYKR; QLLPVAFFFIIYKRP; LLPVAFFFIIYKRPR; LPVAFFFIIYKRPRP; PVAFFFIIYKRPRPP; VAFFFIIYKRPRPPL; AFFFIIYKRPRPPLP; FFFIIYKRPRPPLPP; FFIIYKRPRPPLPPP; FIIYKRPRPPLPPPF; IIYKRPRPPLPPPFL; IYKRPRPPLPPPFLS; YKRPRPPLPPPFLSS; KRPRPPLPPPFLSSS; RPRPPLPPPFLSSSK; PRPPLPPPFLSSSKG; RPPLPPPFLSSSKGV; PPLPPPFLSSSKGVE; PLPPPFLSSSKGVEA; LPPPFLSSSKGVEAF; PPPFLSSSKGVEAFS; PPFLSSSKGVEAFSE; PFLSSSKGVEAFSEA; QNYLGKSLFFCNFCK 16 mers: WIKFLTGKNPWSSWTF; GSVRNFTLTKGATRIK; LISLILEPGVAQRFVL; ISLILEPGVAQRFVLI; SLILEPGVAQRFVLIF; LILEPGVAQRFVLIFL; ILEPGVAQRFVLIFLF; LEPGVAQRFVLIFLFA; EPGVAQRFVLIFLFAQ; PGVAQRFVLIFLFAQI; GVAQRFVLIFLFAQIP; VAQRFVLIFLFAQIPC; AQRFVLIFLFAQIPCT; QRFVLIFLFAQIPCTA; RFVLIFLFAQIPCTAR; FVLIFLFAQIPCTARN; VLIFLFAQIPCTARNG; LIFLFAQIPCTARNGL; IFLFAQIPCTARNGLF; FLFAQIPCTARNGLFV; LFAQIPCTARNGLFVP; FAQIPCTARNGLFVPK; AQIPCTARNGLFVPKS; QIPCTARNGLFVPKSL; IPCTARNGLFVPKSLL; PCTARNGLFVPKSLLC; CTARNGLFVPKSLLCT; TARNGLFVPKSLLCTA; ARNGLFVPKSLLCTAL; RNGLFVPKSLLCTALA; NGLFVPKSLLCTALAC; GLFVPKSLLCTALACY; LFVPKSLLCTALACYV; FVPKSLLCTALACYVS; VPKSLLCTALACYVSL; PKSLLCTALACYVSLD; VIIFFIGANLWNRRVG; IIFFIGANLWNRRVGV; IFFIGANLWNRRVGVL; FFIGANLWNRRVGVLV; FIGANLWNRRVGVLVE; IGANLWNRRVGVLVEF; GANLWNRRVGVLVEFL; RSNSRFSTLNTTQKKK; SNSRFSTLNTTQKKKK; NSRFSTLNTTQKKKKG; SRFSTLNTTQKKKKGR; RFSTLNTTQKKKKGRR; FSTLNTTQKKKKGRRP; RSIPYYRRKHSRGLKG; SIPYYRRKHSRGLKGA; GCVFIIRYVFRISIQC; CVFIIRYVFRISIQCR; VFIIRYVFRISIQCRG; FIIRYVFRISIQCRGV; KKSRYPSYDQGRNANR; KSRYPSYDQGRNANRK; SRYPSYDQGRNANRKI; RYPSYDQGRNANRKIQ; YPSYDQGRNANRKIQS; PSYDQGRNANRKIQSY; SYDQGRNANRKIQSYI; YDQGRNANRKIQSYIR; NGFNIWSSWKCCTRTI; GFNIWSSWKCCTRTIY; FNIWSSWKCCTRTIYG; NIWSSWKCCTRTIYGR; IWSSWKCCTRTIYGRC; WSSWKCCTRTIYGRCC; SSWKCCTRTIYGRCCL; SWKCCTRTIYGRCCLA; WKCCTRTIYGRCCLAA; KCCTRTIYGRCCLAAL; CCTRTIYGRCCLAALF; CTRTIYGRCCLAALFA; TRTIYGRCCLAALFAT; IKGFAFRTWNKQFRQF; KGFAFRTWNKQFRQFE; GFAFRTWNKQFRQFER; FAFRTWNKQFRQFERL; AFRTWNKQFRQFERLF; FRTWNKQFRQFERLFR; RTWNKQFRQFERLFRW; TWNKQFRQFERLFRWK; WNKQFRQFERLFRWKC; GKFRKETFKQKNPNIS; KFRKETFKQKNPNIST; FRKETFKQKNPNISTR; RKETFKQKNPNISTRL; KETFKQKNPNISTRLG; ETFKQKNPNISTRLGY; TFKQKNPNISTRLGYN; FKQKNPNISTRLGYNE; AQNIFKKILTKLRVLT; KKNFTKWNDLVATANL; KNFTKWNDLVATANLV; IPITMLFPSLRYFSPC; KHLFKAFWFAIVPVCQ; HLFKAFWFAIVPVCQY; LFKAFWFAIVPVCQYI; FKAFWFAIVPVCQYIL; KAFWFAIVPVCQYILS; AFWFAIVPVCQYILSY; FWFAIVPVCQYILSYL; WFAIVPVCQYILSYLG; FAIVPVCQYILSYLGP; AIVPVCQYILSYLGPL; IVPVCQYILSYLGPLE; VPVCQYILSYLGPLEV; PVCQYILSYLGPLEVF; VCQYILSYLGPLEVFL; CQYILSYLGPLEVFLC; QYILSYLGPLEVFLCH; YILSYLGPLEVFLCHQ; ILSYLGPLEVFLCHQT; LSYLGPLEVFLCHQTP; GHLAKRKLGKDSLQIF; HLAKRKLGKDSLQIFF; LAKRKLGKDSLQIFFS; AKRKLGKDSLQIFFSG; KRKLGKDSLQIFFSGG; RKLGKDSLQIFFSGGS; TGHKYQQLKHTGYQLY; GHKYQQLKHTGYQLYK; HKYQQLKHTGYQLYKE; KYQQLKHTGYQLYKEA; YQQLKHTGYQLYKEAP; QQLKHTGYQLYKEAPH; QLKHTGYQLYKEAPHP; LKHTGYQLYKEAPHPV; KHTGYQLYKEAPHPVH; HTGYQLYKEAPHPVHL; TGYQLYKEAPHPVHLA; GYQLYKEAPHPVHLAT; YQLYKEAPHPVHLATL; QLYKEAPHPVHLATLW; HFHFYWDQVPSTQLDK; FHFYWDQVPSTQLDKH; HFYWDQVPSTQLDKHC; FYWDQVPSTQLDKHCF; YWDQVPSTQLDKHCFC; WDQVPSTQLDKHCFCP; DQVPSTQLDKHCFCPN; QVPSTQLDKHCFCPNR; VPSTQLDKHCFCPNRP; PSTQLDKHCFCPNRPY; STQLDKHCFCPNRPYG; TQLDKHCFCPNRPYGQ; QLDKHCFCPNRPYGQY; LDKHCFCPNRPYGQYS; DKHCFCPNRPYGQYSL; KHCFCPNRPYGQYSLP; HCFCPNRPYGQYSLPG; CFCPNRPYGQYSLPGT; FCPNRPYGQYSLPGTG; CPNRPYGQYSLPGTGL; PNRPYGQYSLPGTGLL; NRPYGQYSLPGTGLLG; RPYGQYSLPGTGLLGF; YHQGTLTCNSLALPAF; HQGTLTCNSLALPAFP; QGTLTCNSLALPAFPR; GTLTCNSLALPAFPRV; TLTCNSLALPAFPRVL; LTCNSLALPAFPRVLH; TCNSLALPAFPRVLHL; CNSLALPAFPRVLHLQ; NSLALPAFPRVLHLQQ; SLALPAFPRVLHLQQR; LALPAFPRVLHLQQRS; ALPAFPRVLHLQQRSG; LPAFPRVLHLQQRSGN; PAFPRVLHLQQRSGNY; AFPRVLHLQQRSGNYC; FPRVLHLQQRSGNYCL; PRVLHLQQRSGNYCLE; VFLHHAHALFVTLHEG; PLFVQLQPPTSVDFHR; LFVQLQPPTSVDFHRL; FVQLQPPTSVDFHRLG; VQLQPPTSVDFHRLGP; QLQPPTSVDFHRLGPH; LQPPTSVDFHRLGPHL; QPPTSVDFHRLGPHLN; PPTSVDFHRLGPHLNW; PTSVDFHRLGPHLNWG; TSVDFHRLGPHLNWGG; SVDFHRLGPHLNWGGE; VDFHRLGPHLNWGGEF; DFHRLGPHLNWGGEFL; FHRLGPHLNWGGEFLL; HRLGPHLNWGGEFLLC; RLGPHLNWGGEFLLCC; LGPHLNWGGEFLLCCN; GPHLNWGGEFLLCCNR; PHLNWGGEFLLCCNRE; HLNWGGEFLLCCNREA; LNWGGEFLLCCNREAF; NWGGEFLLCCNREAFF; WGGEFLLCCNREAFFS; GGEFLLCCNREAFFSL; GEFLLCCNREAFFSLG; EFLLCCNREAFFSLGY; FLLCCNREAFFSLGYH; LLCCNREAFFSLGYHC; GFHLDPPFLGLGSILP; FHLDPPFLGLGSILPL; LLELLLLLLLVVLALA; LELLLLLLLVVLALAR; ELLLLLLLVVLALARV; LLLLLLLVVLALARVP; LLLLLLVVLALARVPL; LLLLLVVLALARVPLA; LLLLVVLALARVPLAF; LLLVVLALARVPLAFW; LLVVLALARVPLAFWE; LVVLALARVPLAFWEL; VVLALARVPLAFWELP; VLALARVPLAFWELPL; LALARVPLAFWELPLD; ALARVPLAFWELPLDT; LARVPLAFWELPLDTL; ARVPLAFWELPLDTLL; RVPLAFWELPLDTLLF; VPLAFWELPLDTLLFF; PLAFWELPLDTLLFFW; LAFWELPLDTLLFFWL; AFWELPLDTLLFFWLG; FWELPLDTLLFFWLGP; WELPLDTLLFFWLGPS; ELPLDTLLFFWLGPSS; LPLDTLLFFWLGPSSY; PLDTLLFFWLGPSSYA; LDTLLFFWLGPSSYAS; DTLLFFWLGPSSYASR; TLLFFWLGPSSYASRA; LLFFWLGPSSYASRAG; LFFWLGPSSYASRAGV; FFWLGPSSYASRAGVT; FWLGPSSYASRAGVTV; WLGPSSYASRAGVTVP; LGPSSYASRAGVTVPY; GPSSYASRAGVTVPYR; PSSYASRAGVTVPYRP; SSYASRAGVTVPYRPR; SYASRAGVTVPYRPRS; YASRAGVTVPYRPRSK; ASRAGVTVPYRPRSKG; SRAGVTVPYRPRSKGN; RAGVTVPYRPRSKGNI; AGVTVPYRPRSKGNIH; LAPPGAIVFSINSPEC; APPGAIVFSINSPECT; PPGAIVFSINSPECTL; PGAIVFSINSPECTLC; FLKSILCVTSSILSAS; LKSILCVTSSILSASS; KSILCVTSSILSASSI; SILCVTSSILSASSIL; VWPKCTRVPSLSATCL; WPKCTRVPSLSATCLT; PKCTRVPSLSATCLTI; KCTRVPSLSATCLTIE; CTRVPSLSATCLTIEG; TRVPSLSATCLTIEGL; RVPSLSATCLTIEGLI; VPSLSATCLTIEGLIG; PSLSATCLTIEGLIGE; SLSATCLTIEGLIGER; LSATCLTIEGLIGERS; SATCLTIEGLIGERSE; KFIGAFTIVQVVSSKN; FIGAFTIVQVVSSKNL; IGAFTIVQVVSSKNLA; GAFTIVQVVSSKNLAK; AFTIVQVVSSKNLAKE; FTIVQVVSSKNLAKES; TIVQVVSSKNLAKESL; IVQVVSSKNLAKESLK; VQVVSSKNLAKESLKN; QVVSSKNLAKESLKNL; VVSSKNLAKESLKNLS; VSSKNLAKESLKNLSV; SSKNLAKESLKNLSVL; SKNLAKESLKNLSVLL; KNLAKESLKNLSVLLC; NLAKESLKNLSVLLCN; LAKESLKNLSVLLCNS; AKESLKNLSVLLCNSC; KESLKNLSVLLCNSCE; ESLKNLSVLLCNSCEV; SLKNLSVLLCNSCEVI; LKNLSVLLCNSCEVIE; KNLSVLLCNSCEVIEG; NLSVLLCNSCEVIEGI; LSVLLCNSCEVIEGIS; SVLLCNSCEVIEGISS; VLLCNSCEVIEGISSL; LLCNSCEVIEGISSLI; LCNSCEVIEGISSLIT; CNSCEVIEGISSLITC; NSCEVIEGISSLITCH; SCEVIEGISSLITCHK; CEVIEGISSLITCHKA; EVIEGISSLITCHKAW; VIEGISSLITCHKAWE; IEGISSLITCHKAWEI; EGISSLITCHKAWEIV; GISSLITCHKAWEIVA; ISSLITCHKAWEIVAN; SSLITCHKAWEIVANK; SLITCHKAWEIVANKE; LITCHKAWEIVANKEG; ITCHKAWEIVANKEGP; TCHKAWEIVANKEGPQ; CHKAWEIVANKEGPQC; HKAWEIVANKEGPQCL; KAWEIVANKEGPQCLG; AWEIVANKEGPQCLGS; WEIVANKEGPQCLGSR; EIVANKEGPQCLGSRY; IKAANPAIAPGAPAIT; KAANPAIAPGAPAITA; AANPAIAPGAPAITAY; ANPAIAPGAPAITAYV; GVRPIAAIASEVLVMP; VRPIAAIASEVLVMPS; RPIAAIASEVLVMPST; PIAAIASEVLVMPSTV; IAAIASEVLVMPSTVA; AAIASEVLVMPSTVAR; AIASEVLVMPSTVARD; IASEVLVMPSTVARDA; ASEVLVMPSTVARDAI; TSIAAAASPAAISATE; SIAAAASPAAISATEN; IAAAASPAAISATENP; AAAASPAAISATENPV; AAASPAAISATENPVA; AASPAAISATENPVAA; ASPAAISATENPVAAA; SPAAISATENPVAAAA; PAAISATENPVAAAAS; AAISATENPVAAAASD; AISATENPVAAAASDT; ISATENPVAAAASDTL; SATENPVAAAASDTLA; ATENPVAAAASDTLAT; TENPVAAAASDTLATR; ENPVAAAASDTLATRS; NPVAAAASDTLATRSP; PVAAAASDTLATRSPK; VAAAASDTLATRSPKS; AAAASDTLATRSPKSA; AAASDTLATRSPKSAR; AASDTLATRSPKSARA; ASDTLATRSPKSARAA; SDTLATRSPKSARAAP; DTLATRSPKSARAAPM; TLATRSPKSARAAPMN; LATRSPKSARAAPMNL; ATRSPKSARAAPMNLE; TRSPKSARAAPMNLEI; RSPKSARAAPMNLEIQ; SPKSARAAPMNLEIQK; PKSARAAPMNLEIQKK; KSARAAPMNLEIQKKR; SARAAPMNLEIQKKRD; ARAAPMNLEIQKKRDY; RAAPMNLEIQKKRDYL; AAPMNLEIQKKRDYLP; APMNLEIQKKRDYLPR; PMNLEIQKKRDYLPRS; MNLEIQKKRDYLPRSL; NLEIQKKRDYLPRSLL; LEIQKKRDYLPRSLLQ; EIQKKRDYLPRSLLQS; IQKKRDYLPRSLLQSL; QKKRDYLPRSLLQSLL; KKRDYLPRSLLQSLLQ; KRDYLPRSLLQSLLQQ; RDYLPRSLLQSLLQQV; DYLPRSLLQSLLQQVK; YLPRSLLQSLLQQVKQ; LPRSLLQSLLQQVKQW; PRSLLQSLLQQVKQWY; RSLLQSLLQQVKQWYF; SLLQSLLQQVKQWYFC; LLQSLLQQVKQWYFCF; LQSLLQQVKQWYFCFS; QSLLQQVKQWYFCFSR; SLLQQVKQWYFCFSRL; LLQQVKQWYFCFSRLH; LQQVKQWYFCFSRLHC; QQVKQWYFCFSRLHCL; QVKQWYFCFSRLHCLH; VKQWYFCFSRLHCLHL; KQWYFCFSRLHCLHLY; QWYFCFSRLHCLHLYK; WYFCFSRLHCLHLYKI; YFCFSRLHCLHLYKIP; FCFSRLHCLHLYKIPA; CFSRLHCLHLYKIPAK; FSRLHCLHLYKIPAKA; SRLHCLHLYKIPAKAL; RLHCLHLYKIPAKALK; KSSELFFLFQSRFYQL; SSELFFLFQSRFYQLS; SELFFLFQSRFYQLSL; ELFFLFQSRFYQLSLK; LFFLFQSRFYQLSLKL; FFLFQSRFYQLSLKLV; FLFQSRFYQLSLKLVV; LFQSRFYQLSLKLVVT; FQSRFYQLSLKLVVTA; QSRFYQLSLKLVVTAG; SRFYQLSLKLVVTAGA; RFYQLSLKLVVTAGAE; FYQLSLKLVVTAGAEP; YQLSLKLVVTAGAEPW; QLSLKLVVTAGAEPWP; LSLKLVVTAGAEPWPL; SLKLVVTAGAEPWPLS; LKLVVTAGAEPWPLSS; KLVVTAGAEPWPLSSL; LVVTAGAEPWPLSSLT; VVTAGAEPWPLSSLTG; VTAGAEPWPLSSLTGD; TAGAEPWPLSSLTGDK; AGAEPWPLSSLTGDKA; GAEPWPLSSLTGDKAK; AEPWPLSSLTGDKAKI; EPWPLSSLTGDKAKIP; PWPLSSLTGDKAKIPR; WPLSSLTGDKAKIPRL; PLSSLTGDKAKIPRLA; LSSLTGDKAKIPRLAK; SSLTGDKAKIPRLAKH; SLTGDKAKIPRLAKHV; LTGDKAKIPRLAKHVC; TGDKAKIPRLAKHVCH; GDKAKIPRLAKHVCHA; DKAKIPRLAKHVCHAL; KAKIPRLAKHVCHALS; AKIPRLAKHVCHALSF; KIPRLAKHVCHALSFL; IPRLAKHVCHALSFLR; PRLAKHVCHALSFLRS; RLAKHVCHALSFLRSW; LAKHVCHALSFLRSWF; AKHVCHALSFLRSWFG; KHVCHALSFLRSWFGC; HVCHALSFLRSWFGCI; VCHALSFLRSWFGCIP; CHALSFLRSWFGCIPW; HALSFLRSWFGCIPWV; ALSFLRSWFGCIPWVS; LSFLRSWFGCIPWVSS; SFLRSWFGCIPWVSSS; FLRSWFGCIPWVSSSS; LRSWFGCIPWVSSSSL; GHGLAAFPCESCTFLP; HGLAAFPCESCTFLPE; GLAAFPCESCTFLPEV; LAAFPCESCTFLPEVM; AAFPCESCTFLPEVMV; AFPCESCTFLPEVMVW; FPCESCTFLPEVMVWL; PCESCTFLPEVMVWLH; CESCTFLPEVMVWLHS; ESCTFLPEVMVWLHSM; SCTFLPEVMVWLHSMG; CTFLPEVMVWLHSMGK; TFLPEVMVWLHSMGKQ; FLPEVMVWLHSMGKQL; LPEVMVWLHSMGKQLL; PEVMVWLHSMGKQLLP; EVMVWLHSMGKQLLPV; VMVWLHSMGKQLLPVA; MVWLHSMGKQLLPVAF; VWLHSMGKQLLPVAFF; WLHSMGKQLLPVAFFF; LHSMGKQLLPVAFFFI; HSMGKQLLPVAFFFII; SMGKQLLPVAFFFIIY; MGKQLLPVAFFFIIYK; GKQLLPVAFFFIIYKR; KQLLPVAFFFIIYKRP; QLLPVAFFFIIYKRPR; LLPVAFFFIIYKRPRP; LPVAFFFIIYKRPRPP; PVAFFFIIYKRPRPPL; VAFFFIIYKRPRPPLP; AFFFIIYKRPRPPLPP; FFFIIYKRPRPPLPPP; FFIIYKRPRPPLPPPF; FIIYKRPRPPLPPPFL; IIYKRPRPPLPPPFLS; IYKRPRPPLPPPFLSS; YKRPRPPLPPPFLSSS; KRPRPPLPPPFLSSSK; RPRPPLPPPFLSSSKG; PRPPLPPPFLSSSKGV; RPPLPPPFLSSSKGVE; PPLPPPFLSSSKGVEA; PLPPPFLSSSKGVEAF; LPPPFLSSSKGVEAFS; PPPFLSSSKGVEAFSE; PPFLSSSKGVEAFSEA BK virus, reverse reading frame 3 13 mers: QGRIHGAHGPFRP; KSCLGKSSLNEKS; SCLGKSSLNEKSL; CLGKSSLNEKSLF; LGKSSLNEKSLFK; GKSSLNEKSLFKE; KSSLNEKSLFKEV; FSSLPRYPVLQGM; SSLPRYPVLQGMA; SLPRYPVLQGMAY; LPRYPVLQGMAYL; PRYPVLQGMAYLF; RYPVLQGMAYLFQ; YPVLQGMAYLFQK; PVLQGMAYLFQKA; VLQGMAYLFQKAF; LQGMAYLFQKAFC; QGMAYLFQKAFCA; GMAYLFQKAFCAL; MAYLFQKAFCALP; AYLFQKAFCALPL; YLFQKAFCALPLH; LFQKAFCALPLHA; FQKAFCALPLHAM; QKAFCALPLHAMS; KAFCALPLHAMSA; KIFKKRALGLDRL; IFKKRALGLDRLL; FKKRALGLDRLLL; KKRALGLDRLLLH; RNSAMVGPNNWRN; NSAMVGPNNWRNS; SAMVGPNNWRNSL; AMVGPNNWRNSLQ; MVGPNNWRNSLQR; VGPNNWRNSLQRS; GPNNWRNSLQRSK; PNNWRNSLQRSKA; NNWRNSLQRSKAL; NWRNSLQRSKALR; VPTYGTEEWESWW; PTYGTEEWESWWS; TYGTEEWESWWSS; YGTEEWESWWSSF; GTEEWESWWSSFN; TEEWESWWSSFNE; EEWESWWSSFNEK; EWESWWSSFNEKW; WESWWSSFNEKWD; ESWWSSFNEKWDE; SWWSSFNEKWDED; WWSSFNEKWDEDL; WSSFNEKWDEDLF; SSFNEKWDEDLFC; SFNEKWDEDLFCH; FNEKWDEDLFCHE; NEKWDEDLFCHED; EKWDEDLFCHEDM; KWDEDLFCHEDMF; WDEDLFCHEDMFA; DEDLFCHEDMFAS; EDLFCHEDMFASD; DLFCHEDMFASDE; LFCHEDMFASDEE; FCHEDMFASDEEA; CHEDMFASDEEAT; HEDMFASDEEATA; EDMFASDEEATAD; DMFASDEEATADS; MFASDEEATADSQ; FASDEEATADSQH; ASDEEATADSQHS; SDEEATADSQHST; DEEATADSQHSTP; EEATADSQHSTPP; EATADSQHSTPPK; ATADSQHSTPPKK; TADSQHSTPPKKK; ADSQHSTPPKKKR; DSQHSTPPKKKRK; SQHSTPPKKKRKV; QHSTPPKKKRKVE; HSTPPKKKRKVED; STPPKKKRKVEDP; TPPKKKRKVEDPK; PPKKKRKVEDPKD; PKKKRKVEDPKDF; KKKRKVEDPKDFP; KKRKVEDPKDFPS; KRKVEDPKDFPSD; RKVEDPKDFPSDL; KVEDPKDFPSDLH; VEDPKDFPSDLHQ; EDPKDFPSDLHQF; DPKDFPSDLHQFL; PKDFPSDLHQFLS; KDFPSDLHQFLSQ; DFPSDLHQFLSQA; FPSDLHQFLSQAV; PSDLHQFLSQAVF; SDLHQFLSQAVFS; DLHQFLSQAVFSN; LHQFLSQAVFSNR; HQFLSQAVFSNRT; QFLSQAVFSNRTL; FLSQAVFSNRTLA; LSQAVFSNRTLAC; SQAVFSNRTLACF; QAVFSNRTLACFA; AVFSNRTLACFAV; VFSNRTLACFAVY; FSNRTLACFAVYT; SNRTLACFAVYTT; NRTLACFAVYTTK; RTLACFAVYTTKE; TLACFAVYTTKEK; LACFAVYTTKEKA; ACFAVYTTKEKAQ; CFAVYTTKEKAQI; FAVYTTKEKAQIL; AVYTTKEKAQILY; VYTTKEKAQILYK; YTTKEKAQILYKK; TTKEKAQILYKKL; TKEKAQILYKKLM; KEKAQILYKKLME; EKAQILYKKLMEK; KAQILYKKLMEKY; AQILYKKLMEKYS; QILYKKLMEKYSV; ILYKKLMEKYSVT; LYKKLMEKYSVTF; YKKLMEKYSVTFI; KKLMEKYSVTFIS; KLMEKYSVTFISR; LMEKYSVTFISRH; MEKYSVTFISRHM; EKYSVTFISRHMC; KYSVTFISRHMCA; YSVTFISRHMCAG; SVTFISRHMCAGH; VTFISRHMCAGHN; TFISRHMCAGHNI; FISRHMCAGHNII; ISRHMCAGHNIIF; SRHMCAGHNIIFF; RHMCAGHNIIFFL; HMCAGHNIIFFLT; MCAGHNIIFFLTP; CAGHNIIFFLTPH; AGHNIIFFLTPHR; GHNIIFFLTPHRH; HNIIFFLTPHRHR; NIIFFLTPHRHRV; IIFFLTPHRHRVS; IFFLTPHRHRVSA; FFLTPHRHRVSAI; FLTPHRHRVSAIN; LTPHRHRVSAINN; TPHRHRVSAINNF; PHRHRVSAINNFC; HRHRVSAINNFCQ; RHRVSAINNFCQK; HRVSAINNFCQKL; RVSAINNFCQKLC; VSAINNFCQKLCT; SAINNFCQKLCTF; AINNFCQKLCTFS; INNFCQKLCTFSF; NNFCQKLCTFSFL; NFCQKLCTFSFLI; FCQKLCTFSFLIC; CQKLCTFSFLICK; QKLCTFSFLICKG; KLCTFSFLICKGV; LCTFSFLICKGVN; CTFSFLICKGVNK; TFSFLICKGVNKE; FSFLICKGVNKEY; SFLICKGVNKEYL; FLICKGVNKEYLL; LICKGVNKEYLLY; ICKGVNKEYLLYS; CKGVNKEYLLYSA; KGVNKEYLLYSAL; GVNKEYLLYSALT; VNKEYLLYSALTR; NKEYLLYSALTRD; KEYLLYSALTRDP; EYLLYSALTRDPY; YLLYSALTRDPYH; LLYSALTRDPYHT; LYSALTRDPYHTI; YSALTRDPYHTIE; SALTRDPYHTIEE; ALTRDPYHTIEES; LTRDPYHTIEESI; TRDPYHTIEESIQ; RDPYHTIEESIQG; DPYHTIEESIQGG; PYHTIEESIQGGL; YHTIEESIQGGLK; HTIEESIQGGLKE; TIEESIQGGLKEH; IEESIQGGLKEHD; EESIQGGLKEHDF; ESIQGGLKEHDFS; SIQGGLKEHDFSP; IQGGLKEHDFSPE; QGGLKEHDFSPEE; GGLKEHDFSPEEP; GLKEHDFSPEEPE; LKEHDFSPEEPEE; KEHDFSPEEPEET; EHDFSPEEPEETK; HDFSPEEPEETKQ; DFSPEEPEETKQV; FSPEEPEETKQVS; SPEEPEETKQVSW; PEEPEETKQVSWK; EEPEETKQVSWKL; EPEETKQVSWKLI; PEETKQVSWKLIT; EETKQVSWKLITE; ETKQVSWKLITEY; TKQVSWKLITEYA; KQVSWKLITEYAV; QVSWKLITEYAVE; VSWKLITEYAVET; SWKLITEYAVETK; WKLITEYAVETKC; KLITEYAVETKCE; LITEYAVETKCED; ITEYAVETKCEDV; TEYAVETKCEDVF; EYAVETKCEDVFL; YAVETKCEDVFLL; AVETKCEDVFLLL; VETKCEDVFLLLG; ETKCEDVFLLLGM; TKCEDVFLLLGMY; KCEDVFLLLGMYL; CEDVFLLLGMYLE; EDVFLLLGMYLEF; DVFLLLGMYLEFQ; VFLLLGMYLEFQY; FLLLGMYLEFQYN; LLLGMYLEFQYNV; LLGMYLEFQYNVE; LGMYLEFQYNVEE; GMYLEFQYNVEEC; MYLEFQYNVEECK; YLEFQYNVEECKK; LEFQYNVEECKKC; EFQYNVEECKKCQ; FQYNVEECKKCQK; QYNVEECKKCQKK; YNVEECKKCQKKD; NVEECKKCQKKDQ; VEECKKCQKKDQP; EECKKCQKKDQPY; ECKKCQKKDQPYH; CKKCQKKDQPYHF; KKCQKKDQPYHFK; KCQKKDQPYHFKY; CQKKDQPYHFKYH; QKKDQPYHFKYHE; KKDQPYHFKYHEK; KDQPYHFKYHEKH; DQPYHFKYHEKHF; QPYHFKYHEKHFA; PYHFKYHEKHFAN; YHFKYHEKHFANA; HFKYHEKHFANAI; FKYHEKHFANAII; KYHEKHFANAIIF; YHEKHFANAIIFA; HEKHFANAIIFAE; EKHFANAIIFAES; KHFANAIIFAESK; HFANAIIFAESKN; FANAIIFAESKNQ; ANAIIFAESKNQK; NAIIFAESKNQKS; AIIFAESKNQKSI; IIFAESKNQKSIC; IFAESKNQKSICQ; FAESKNQKSICQQ; AESKNQKSICQQA; ESKNQKSICQQAV; SKNQKSICQQAVD; KNQKSICQQAVDT; NQKSICQQAVDTV; QKSICQQAVDTVL; KSICQQAVDTVLA; SICQQAVDTVLAK; ICQQAVDTVLAKK; CQQAVDTVLAKKR; QQAVDTVLAKKRV; QAVDTVLAKKRVD; AVDTVLAKKRVDT; VDTVLAKKRVDTL; DTVLAKKRVDTLH; TVLAKKRVDTLHM; VLAKKRVDTLHMT; LAKKRVDTLHMTR; AKKRVDTLHMTRE; KKRVDTLHMTREE; KRVDTLHMTREEM; RVDTLHMTREEML; VDTLHMTREEMLT; DTLHMTREEMLTE; TLHMTREEMLTER; LHMTREEMLTERF; HMTREEMLTERFN; MTREEMLTERFNH; TREEMLTERFNHI; REEMLTERFNHIL; EEMLTERFNHILD; EMLTERFNHILDK; MLTERFNHILDKM; LTERFNHILDKMD; TERFNHILDKMDL; ERFNHILDKMDLI; RFNHILDKMDLIF; FNHILDKMDLIFG; NHILDKMDLIFGA; HILDKMDLIFGAH; ILDKMDLIFGAHG; LDKMDLIFGAHGN; DKMDLIFGAHGNA; KMDLIFGAHGNAV; MDLIFGAHGNAVL; DLIFGAHGNAVLE; LIFGAHGNAVLEQ; IFGAHGNAVLEQY; FGAHGNAVLEQYM; GAHGNAVLEQYMA; AHGNAVLEQYMAG; HGNAVLEQYMAGV; GNAVLEQYMAGVA; NAVLEQYMAGVAW; AVLEQYMAGVAWL; VLEQYMAGVAWLH; LEQYMAGVAWLHC; EQYMAGVAWLHCL; QYMAGVAWLHCLL; YMAGVAWLHCLLP; MAGVAWLHCLLPK; AGVAWLHCLLPKM; GVAWLHCLLPKMD; VAWLHCLLPKMDS; AWLHCLLPKMDSV; WLHCLLPKMDSVI; LHCLLPKMDSVIF; HCLLPKMDSVIFD; CLLPKMDSVIFDF; LLPKMDSVIFDFL; LPKMDSVIFDFLH; PKMDSVIFDFLHC; KMDSVIFDFLHCI; MDSVIFDFLHCIV; DSVIFDFLHCIVF; SVIFDFLHCIVFN; VIFDFLHCIVFNV; IFDFLHCIVFNVP; FDFLHCIVFNVPK; DFLHCIVFNVPKR; FLHCIVFNVPKRR; LHCIVFNVPKRRY; HCIVFNVPKRRYW; CIVFNVPKRRYWL; IVFNVPKRRYWLF; VFNVPKRRYWLFK; FNVPKRRYWLFKG; NVPKRRYWLFKGP; VPKRRYWLFKGPI; PKRRYWLFKGPID; KRRYWLFKGPIDS; RRYWLFKGPIDSG; RYWLFKGPIDSGK; YWLFKGPIDSGKT; WLFKGPIDSGKTT; LFKGPIDSGKTTL; FKGPIDSGKTTLA; KGPIDSGKTTLAA; GPIDSGKTTLAAG; PIDSGKTTLAAGL; IDSGKTTLAAGLL; DSGKTTLAAGLLD; SGKTTLAAGLLDL; GKTTLAAGLLDLC; KTTLAAGLLDLCG; TTLAAGLLDLCGG; TLAAGLLDLCGGK; LAAGLLDLCGGKA; AAGLLDLCGGKAL; AGLLDLCGGKALN; GLLDLCGGKALNV; LLDLCGGKALNVN; LDLCGGKALNVNL; DLCGGKALNVNLP; LCGGKALNVNLPM; CGGKALNVNLPME; GGKALNVNLPMER; GKALNVNLPMERL; KALNVNLPMERLT; ALNVNLPMERLTF; LNVNLPMERLTFE; NVNLPMERLTFEL; VNLPMERLTFELG; NLPMERLTFELGV; LPMERLTFELGVA; PMERLTFELGVAI; MERLTFELGVAID; ERLTFELGVAIDQ; RLTFELGVAIDQY; LTFELGVAIDQYM; TFELGVAIDQYMV; FELGVAIDQYMVV; ELGVAIDQYMVVF; LGVAIDQYMVVFE; GVAIDQYMVVFED; VAIDQYMVVFEDV; AIDQYMVVFEDVK; IDQYMVVFEDVKG; DQYMVVFEDVKGT; QYMVVFEDVKGTG; YMVVFEDVKGTGA; MVVFEDVKGTGAE; VVFEDVKGTGAES; VFEDVKGTGAESK; FEDVKGTGAESKD; EDVKGTGAESKDL; DVKGTGAESKDLP; VKGTGAESKDLPS; KGTGAESKDLPSG; GTGAESKDLPSGH; TGAESKDLPSGHG; GAESKDLPSGHGI; AESKDLPSGHGIN; ESKDLPSGHGINN; SKDLPSGHGINNL; KDLPSGHGINNLD; DLPSGHGINNLDS; LPSGHGINNLDSL; PSGHGINNLDSLR; SGHGINNLDSLRD; GHGINNLDSLRDY; HGINNLDSLRDYL; GINNLDSLRDYLD; INNLDSLRDYLDG; NNLDSLRDYLDGS; NLDSLRDYLDGSV; LDSLRDYLDGSVK; DSLRDYLDGSVKV; SLRDYLDGSVKVN; LRDYLDGSVKVNL; RDYLDGSVKVNLE; DYLDGSVKVNLEK; YLDGSVKVNLEKK; LDGSVKVNLEKKH; DGSVKVNLEKKHL; GSVKVNLEKKHLN; SVKVNLEKKHLNK; VKVNLEKKHLNKR; KVNLEKKHLNKRT; VNLEKKHLNKRTQ; NLEKKHLNKRTQI; LEKKHLNKRTQIF; EKKHLNKRTQIFP; KKHLNKRTQIFPP; KHLNKRTQIFPPG; HLNKRTQIFPPGL; LNKRTQIFPPGLV; NKRTQIFPPGLVT; KRTQIFPPGLVTM; RTQIFPPGLVTMN; TQIFPPGLVTMNE; QIFPPGLVTMNEY; IFPPGLVTMNEYP; FPPGLVTMNEYPV; PPGLVTMNEYPVP; PGLVTMNEYPVPK; GLVTMNEYPVPKT; LVTMNEYPVPKTL; VTMNEYPVPKTLQ; TMNEYPVPKTLQA; MNEYPVPKTLQAR; NEYPVPKTLQARF; EYPVPKTLQARFV; YPVPKTLQARFVR; PVPKTLQARFVRQ; VPKTLQARFVRQI; PKTLQARFVRQID; KTLQARFVRQIDF; TLQARFVRQIDFR; LQARFVRQIDFRP; QARFVRQIDFRPK; ARFVRQIDFRPKI; RFVRQIDFRPKIY; FVRQIDFRPKIYL; VRQIDFRPKIYLR; RQIDFRPKIYLRK; QIDFRPKIYLRKS; IDFRPKIYLRKSL; DFRPKIYLRKSLQ; FRPKIYLRKSLQN; RPKIYLRKSLQNS; PKIYLRKSLQNSE; KIYLRKSLQNSEF; IYLRKSLQNSEFL; YLRKSLQNSEFLL; LRKSLQNSEFLLE; RKSLQNSEFLLEK; KSLQNSEFLLEKR; SLQNSEFLLEKRI; LQNSEFLLEKRIL; QNSEFLLEKRILQ; NSEFLLEKRILQS; SEFLLEKRILQSG; EFLLEKRILQSGM; FLLEKRILQSGMT; LLEKRILQSGMTL; LEKRILQSGMTLL; EKRILQSGMTLLL; KRILQSGMTLLLL; RILQSGMTLLLLL; ILQSGMTLLLLLI; LQSGMTLLLLLIW; QSGMTLLLLLIWF; SGMTLLLLLIWFR; GMTLLLLLIWFRP; MTLLLLLIWFRPV; TLLLLLIWFRPVA; LLLLLIWFRPVAD; LLLLIWFRPVADF; LLLIWFRPVADFA; LLIWFRPVADFAT; LIWFRPVADFATD; IWFRPVADFATDI; WFRPVADFATDIQ; FRPVADFATDIQS; RPVADFATDIQSR; PVADFATDIQSRI; VADFATDIQSRIV; ADFATDIQSRIVE; DFATDIQSRIVEW; FATDIQSRIVEWK; ATDIQSRIVEWKE; TDIQSRIVEWKER; DIQSRIVEWKERL; IQSRIVEWKERLD; QSRIVEWKERLDS; SRIVEWKERLDSE; RIVEWKERLDSEI; IVEWKERLDSEIS; VEWKERLDSEISM; EWKERLDSEISMY; WKERLDSEISMYT; KERLDSEISMYTF; ERLDSEISMYTFS; RLDSEISMYTFSR; LDSEISMYTFSRM; DSEISMYTFSRMK; SEISMYTFSRMKY; EISMYTFSRMKYN; ISMYTFSRMKYNI; SMYTFSRMKYNIC; MYTFSRMKYNICM; YTFSRMKYNICMG; TFSRMKYNICMGK; FSRMKYNICMGKC; SRMKYNICMGKCI; RMKYNICMGKCIL; MKYNICMGKCILD; KYNICMGKCILDI; YNICMGKCILDIT; NICMGKCILDITR; ICMGKCILDITRE; CMGKCILDITREE; MGKCILDITREED; GKCILDITREEDS; KCILDITREEDSE; CILDITREEDSET; ILDITREEDSETE; LDITREEDSETED; DITREEDSETEDS; ITREEDSETEDSG; TREEDSETEDSGH; REEDSETEDSGHG; EEDSETEDSGHGS; EDSETEDSGHGSS; DSETEDSGHGSST; SETEDSGHGSSTE; ETEDSGHGSSTES; TEDSGHGSSTESQ; EDSGHGSSTESQS; DSGHGSSTESQSQ; SGHGSSTESQSQC; GHGSSTESQSQCS; HGSSTESQSQCSS; GSSTESQSQCSSQ; SSTESQSQCSSQV; STESQSQCSSQVS; TESQSQCSSQVSD; ESQSQCSSQVSDT; SQSQCSSQVSDTS; QSQCSSQVSDTSA; SQCSSQVSDTSAP; QCSSQVSDTSAPA; CSSQVSDTSAPAE; SSQVSDTSAPAED; SQVSDTSAPAEDS; QVSDTSAPAEDSQ; VSDTSAPAEDSQR; SDTSAPAEDSQRS; DTSAPAEDSQRSD; TSAPAEDSQRSDP; SAPAEDSQRSDPH; APAEDSQRSDPHS; PAEDSQRSDPHSQ; AEDSQRSDPHSQE; EDSQRSDPHSQEL; DSQRSDPHSQELH; SQRSDPHSQELHL; QRSDPHSQELHLC; RSDPHSQELHLCK; SDPHSQELHLCKG; DPHSQELHLCKGF; PHSQELHLCKGFQ; HSQELHLCKGFQC; SQELHLCKGFQCF; QELHLCKGFQCFK; ELHLCKGFQCFKR; LHLCKGFQCFKRP; HLCKGFQCFKRPK; LCKGFQCFKRPKT; CKGFQCFKRPKTP; KGFQCFKRPKTPP; GFQCFKRPKTPPP; FQCFKRPKTPPPK; HKLKSGLYKSSIY; MYMYNKSTCLKHF; YMYNKSTCLKHFG; MYNKSTCLKHFGL; YNKSTCLKHFGLQ; NKSTCLKHFGLQL; KSTCLKHFGLQLS; STCLKHFGLQLSL; TCLKHFGLQLSLF; CLKHFGLQLSLFV; LKHFGLQLSLFVN; KHFGLQLSLFVNI; HFGLQLSLFVNIS; FGLQLSLFVNISY; GLQLSLFVNISYH; LQLSLFVNISYHI; QLSLFVNISYHIW; LSLFVNISYHIWV; SLFVNISYHIWVP; LFVNISYHIWVPW; FVNISYHIWVPWK; VNISYHIWVPWKS; NISYHIWVPWKSF; ISYHIWVPWKSFC; SYHIWVPWKSFCA; YHIWVPWKSFCAI; HIWVPWKSFCAIK; IWVPWKSFCAIKH; WVPWKSFCAIKHP; VPWKSFCAIKHPN; PWKSFCAIKHPNL; WKSFCAIKHPNLF; KSFCAIKHPNLFY; SFCAIKHPNLFYL; FCAIKHPNLFYLG; CAIKHPNLFYLGF; AIKHPNLFYLGFH; IKHPNLFYLGFHT; KHPNLFYLGFHTI; HPNLFYLGFHTIH; PNLFYLGFHTIHR; NLFYLGFHTIHRL; LFYLGFHTIHRLP; FYLGFHTIHRLPI; YLGFHTIHRLPIH; LGFHTIHRLPIHS; GFHTIHRLPIHSL; FHTIHRLPIHSLG; HTIHRLPIHSLGS; TIHRLPIHSLGSP; IHRLPIHSLGSPV; HRLPIHSLGSPVY; RLPIHSLGSPVYK; LPIHSLGSPVYKV; PIHSLGSPVYKVT; QKGNWVRILYRSF; KGNWVRILYRSFS; GNWVRILYRSFSQ; NWVRILYRSFSQA; WVRILYRSFSQAD; VRILYRSFSQADL; RILYRSFSQADLK; ILYRSFSQADLKI; LYRSFSQADLKIS; YRSFSQADLKISC; RSFSQADLKISCK; SFSQADLKISCKA; FSQADLKISCKAS; SQADLKISCKASP; QADLKISCKASPL; ADLKISCKASPLL; DLKISCKASPLLC; LKISCKASPLLCS; KISCKASPLLCSR; ISCKASPLLCSRA; SCKASPLLCSRAV; CKASPLLCSRAVS; KASPLLCSRAVSK; ASPLLCSRAVSKQ; SPLLCSRAVSKQA; PLLCSRAVSKQAT; LLCSRAVSKQATN; LCSRAVSKQATNI; CSRAVSKQATNIS; SRAVSKQATNISS; NIQAISFTKRPHT; IQAISFTKRPHTL; QAISFTKRPHTLF; AISFTKRPHTLFI; QHCGSCVGHMKYW; HCGSCVGHMKYWG; CGSCVGHMKYWGN; GSCVGHMKYWGNI; SCVGHMKYWGNIF; CVGHMKYWGNIFP; VGHMKYWGNIFPS; GHMKYWGNIFPSC; HMKYWGNIFPSCE; MKYWGNIFPSCES; KYWGNIFPSCESP; YWGNIFPSCESPK; WGNIFPSCESPKI; GNIFPSCESPKIP; NIFPSCESPKIPS; IFPSCESPKIPSI; FPSCESPKIPSIF; PSCESPKIPSIFI; SCESPKIPSIFIS; CESPKIPSIFIST; ESPKIPSIFISTG; SPKIPSIFISTGI; PKIPSIFISTGIR; KIPSIFISTGIRY; IPSIFISTGIRYP; PSIFISTGIRYPA; SIFISTGIRYPAL; IFISTGIRYPALN; FISTGIRYPALNW; ISTGIRYPALNWI; STGIRYPALNWIS; TGIRYPALNWISI; GIRYPALNWISIV; IRYPALNWISIVF; RYPALNWISIVFV; YPALNWISIVFVQ; PALNWISIVFVQI; ALNWISIVFVQIG; LNWISIVFVQIGL; NWISIVFVQIGLM; WISIVFVQIGLMV; ISIVFVQIGLMVS; SIVFVQIGLMVSI; IVFVQIGLMVSIH; VFVQIGLMVSIHY; FVQIGLMVSIHYL; VQIGLMVSIHYLG; QIGLMVSIHYLGL; IGLMVSIHYLGLG; GLMVSIHYLGLGC; LMVSIHYLGLGCW; MVSIHYLGLGCWV; VSIHYLGLGCWVF; SIHYLGLGCWVFR; IHYLGLGCWVFRG; HYLGLGCWVFRGY; YLGLGCWVFRGYS; LGLGCWVFRGYST; GLGCWVFRGYSTI; LGCWVFRGYSTIR; GCWVFRGYSTIRV; CWVFRGYSTIRVL; HSLHFQGFSTYSK; SLHFQGFSTYSKE; LHFQGFSTYSKEV; HFQGFSTYSKEVE; FQGFSTYSKEVEI; QGFSTYSKEVEIT; GFSTYSKEVEITA; FSTYSKEVEITAL; STYSKEVEITALN; TYSKEVEITALNR; YSKEVEITALNRF; SKEVEITALNRFS; KEVEITALNRFSS; EVEITALNRFSST; VEITALNRFSSTM; EITALNRFSSTML; ITALNRFSSTMLM; TALNRFSSTMLMH; ALNRFSSTMLMHF; LNRFSSTMLMHFL; PCMKVKHASYSNN; CMKVKHASYSNNL; MKVKHASYSNNLC; KVKHASYSNNLCL; VKHASYSNNLCLY; KHASYSNNLCLYS; HASYSNNLCLYSY; ASYSNNLCLYSYS; SYSNNLCLYSYSL; YSNNLCLYSYSLP; SNNLCLYSYSLPH; NNLCLYSYSLPHQ; IGEGNSCCAVTGK; GEGNSCCAVTGKH; EGNSCCAVTGKHF; GNSCCAVTGKHFS; NSCCAVTGKHFSL; SCCAVTGKHFSLW; CCAVTGKHFSLWA; CAVTGKHFSLWAI; AVTGKHFSLWAIT; VTGKHFSLWAITA; TGKHFSLWAITAK; GKHFSLWAITAKV; KHFSLWAITAKVI; HFSLWAITAKVIF; FSLWAITAKVIFS; SLWAITAKVIFST; TKAPKVFIWIPHF; KAPKVFIWIPHFW; APKVFIWIPHFWV; EAFYLCNSIYPSF; AFYLCNSIYPSFN; FYLCNSIYPSFNF; FWHLHGFLWLFGS; WHLHGFLWLFGSC; HLHGFLWLFGSCP; LHGFLWLFGSCPW; HGFLWLFGSCPWT; GFLWLFGSCPWTL; FLWLFGSCPWTLS; LWLFGSCPWTLSF; WLFGSCPWTLSFS; LFGSCPWTLSFSF; FGSCPWTLSFSFG; GSCPWTLSFSFGW; SCPWTLSFSFGWG; CPWTLSFSFGWGH; PWTLSFSFGWGHL; WTLSFSFGWGHLH; TLSFSFGWGHLHM; LSFSFGWGHLHML; SFSFGWGHLHMLQ; FSFGWGHLHMLQE; SFGWGHLHMLQEQ; FGWGHLHMLQEQV; GWGHLHMLQEQVL; WGHLHMLQEQVLQ; GHLHMLQEQVLQS; HLHMLQEQVLQSR; LHMLQEQVLQSRT; HMLQEQVLQSRTG; MLQEQVLQSRTGL; LQEQVLQSRTGLE; QEQVLQSRTGLEV; EQVLQSRTGLEVK; QVLQSRTGLEVKA; VLQSRTGLEVKAT; LQSRTGLEVKATS; QSRTGLEVKATSI; SRTGLEVKATSIE; RTGLEVKATSIEE; TGLEVKATSIEEQ; GLEVKATSIEEQF; LEVKATSIEEQFF; EVKATSIEEQFFD; TLLNVHFVDFLSP; LLNVHFVDFLSPF; LNVHFVDFLSPFF; NVHFVDFLSPFFV; LLLYCQHHLYYKY; LLYCQHHLYYKYG; LYCQHHLYYKYGQ; YCQHHLYYKYGQN; CQHHLYYKYGQNV; QHHLYYKYGQNVH; HHLYYKYGQNVHG; HLYYKYGQNVHGY; LYYKYGQNVHGYL; YYKYGQNVHGYLP; YKYGQNVHGYLPF; KYGQNVHGYLPFQ; YGQNVHGYLPFQL; GQNVHGYLPFQLL; QNVHGYLPFQLLV; GKDQNNIVEYNYK; KDQNNIVEYNYKS; DQNNIVEYNYKSL; KIFLFFSAIPVRL; QKYLHQETEYHST; KYLHQETEYHSTH; YLHQETEYHSTHL; LHQETEYHSTHLG; TIPKPCLIADRGL; IPKPCLIADRGLQ; PKPCLIADRGLQW; KPCLIADRGLQWK; PCLIADRGLQWKL; CLIADRGLQWKLC; LIADRGLQWKLCD; IADRGLQWKLCDP; ADRGLQWKLCDPN; DRGLQWKLCDPNH; RGLQWKLCDPNHQ; GLQWKLCDPNHQR; LQWKLCDPNHQRT; QWKLCDPNHQRTY; WKLCDPNHQRTYT; KLCDPNHQRTYTL; LCDPNHQRTYTLL; CDPNHQRTYTLLE; DPNHQRTYTLLEL; PNHQRTYTLLELR; NHQRTYTLLELRN; PQEHQQLQHMFEE; QEHQQLQHMFEEL; EHQQLQHMFEELG; HQQLQHMFEELGL; QQQPPQQQFQPLK; QQPPQQQFQPLKI; QPPQQQFQPLKIL; PPQQQFQPLKILW; PQQQFQPLKILWQ; QQQFQPLKILWQQ; QQFQPLKILWQQQ; QFQPLKILWQQQP; FQPLKILWQQQPQ; QPLKILWQQQPQI; PLKILWQQQPQIH; LKILWQQQPQIHW; KILWQQQPQIHWQ; ILWQQQPQIHWQL; LWQQQPQIHWQLG; WQQQPQIHWQLGP; QQQPQIHWQLGPP; QQPQIHWQLGPPK; QPQIHWQLGPPKV; PQIHWQLGPPKVL; QIHWQLGPPKVLE; IHWQLGPPKVLEQ; HWQLGPPKVLEQH; WQLGPPKVLEQHP; TWKYKKKGITYLG; WKYKKKGITYLGV; KYKKKGITYLGVF; YKKKGITYLGVFY; KKKGITYLGVFYR; KKGITYLGVFYRV; KGITYLGVFYRVF; GITYLGVFYRVFY; ITYLGVFYRVFYS; TYLGVFYRVFYSR; SSGTFVFPVYTVF; SGTFVFPVYTVFT; GTFVFPVYTVFTS; TFVFPVYTVFTST; FVFPVYTVFTSTK; VFPVYTVFTSTKF; FPVYTVFTSTKFQ; PVYTVFTSTKFQQ; VYTVFTSTKFQQK; YTVFTSTKFQQKL; NKNKNPLSSFFCS; KNKNPLSSFFCSS; NKNPLSSFFCSSP; KNPLSSFFCSSPG; NPLSSFFCSSPGF; PLSSFFCSSPGFT; LSSFFCSSPGFTN; SSFFCSSPGFTNF; SFFCSSPGFTNFH; LGTRPRFLGSQNM; GTRPRFLGSQNMS; TRPRFLGSQNMSV; RPRFLGSQNMSVM; PRFLGSQNMSVMH; RFLGSQNMSVMHF; FLGSQNMSVMHFP; LGSQNMSVMHFPS; AAPPCESCTFLPE; APPCESCTFLPEV; PPCESCTFLPEVM; PCESCTFLPEVMV; CESCTFLPEVMVW; ESCTFLPEVMVWL; SCTFLPEVMVWLH; CTFLPEVMVWLHS; TFLPEVMVWLHSP; FLPEVMVWLHSPV; LPEVMVWLHSPVS; PEVMVWLHSPVSH; EVMVWLHSPVSHA; VMVWLHSPVSHAL; MVWLHSPVSHALS; VWLHSPVSHALSF; WLHSPVSHALSFL; LHSPVSHALSFLR; HSPVSHALSFLRS; SPVSHALSFLRSW; PVSHALSFLRSWF; VSHALSFLRSWFG; SHALSFLRSWFGC; HALSFLRSWFGCI; ALSFLRSWFGCIP; LSFLRSWFGCIPW; SFLRSWFGCIPWV; FLRSWFGCIPWVS; LRSWFGCIPWVSS; RSWFGCIPWVSSS; SWFGCIPWVSSSS; WFGCIPWVSSSSL; FGCIPWVSSSSLW; GCIPWVSSSSLWP; CIPWVSSSSLWPF; IPWVSSSSLWPFF; PWVSSSSLWPFFL; YIRGRGRLCLHPF; IRGRGRLCLHPFS; RGRGRLCLHPFSQ; GRGRLCLHPFSQV; RGRLCLHPFSQVV; GRLCLHPFSQVVR; RLCLHPFSQVVRV; LCLHPFSQVVRVW; CLHPFSQVVRVWR; LHPFSQVVRVWRL; HPFSQVVRVWRLF; PFSQVVRVWRLFL; FSQVVRVWRLFLR; SQVVRVWRLFLRP; QVVRVWRLFLRPS; VVRVWRLFLRPSK; VRVWRLFLRPSKT; RVWRLFLRPSKTI; VWRLFLRPSKTIW; WRLFLRPSKTIWG; RLFLRPSKTIWGN; LFLRPSKTIWGNP; FLRPSKTIWGNPY; LRPSKTIWGNPYS; RPSKTIWGNPYSF; PSKTIWGNPYSFA; SKTIWGNPYSFAI; KTIWGNPYSFAIF; TIWGNPYSFAIFA; IWGNPYSFAIFAK 14 mers: KSCLGKSSLNEKSL; SCLGKSSLNEKSLF; CLGKSSLNEKSLFK; LGKSSLNEKSLFKE; GKSSLNEKSLFKEV; FSSLPRYPVLQGMA; SSLPRYPVLQGMAY; SLPRYPVLQGMAYL; LPRYPVLQGMAYLF; PRYPVLQGMAYLFQ; RYPVLQGMAYLFQK; YPVLQGMAYLFQKA; PVLQGMAYLFQKAF; VLQGMAYLFQKAFC; LQGMAYLFQKAFCA; QGMAYLFQKAFCAL; GMAYLFQKAFCALP; MAYLFQKAFCALPL; AYLFQKAFCALPLH; YLFQKAFCALPLHA; LFQKAFCALPLHAM; FQKAFCALPLHAMS; QKAFCALPLHAMSA; KIFKKRALGLDRLL; IFKKRALGLDRLLL; FKKRALGLDRLLLH; RNSAMVGPNNWRNS; NSAMVGPNNWRNSL; SAMVGPNNWRNSLQ; AMVGPNNWRNSLQR; MVGPNNWRNSLQRS; VGPNNWRNSLQRSK; GPNNWRNSLQRSKA; PNNWRNSLQRSKAL; NNWRNSLQRSKALR; VPTYGTEEWESWWS; PTYGTEEWESWWSS; TYGTEEWESWWSSF; YGTEEWESWWSSFN; GTEEWESWWSSFNE; TEEWESWWSSFNEK; EEWESWWSSFNEKW; EWESWWSSFNEKWD; WESWWSSFNEKWDE; ESWWSSFNEKWDED; SWWSSFNEKWDEDL; WWSSFNEKWDEDLF; WSSFNEKWDEDLFC; SSFNEKWDEDLFCH; SFNEKWDEDLFCHE; FNEKWDEDLFCHED; NEKWDEDLFCHEDM; EKWDEDLFCHEDMF; KWDEDLFCHEDMFA; WDEDLFCHEDMFAS; DEDLFCHEDMFASD; EDLFCHEDMFASDE; DLFCHEDMFASDEE; LFCHEDMFASDEEA; FCHEDMFASDEEAT; CHEDMFASDEEATA; HEDMFASDEEATAD; EDMFASDEEATADS; DMFASDEEATADSQ; MFASDEEATADSQH; FASDEEATADSQHS; ASDEEATADSQHST; SDEEATADSQHSTP; DEEATADSQHSTPP; EEATADSQHSTPPK; EATADSQHSTPPKK; ATADSQHSTPPKKK; TADSQHSTPPKKKR; ADSQHSTPPKKKRK; DSQHSTPPKKKRKV; SQHSTPPKKKRKVE; QHSTPPKKKRKVED; HSTPPKKKRKVEDP; STPPKKKRKVEDPK; TPPKKKRKVEDPKD; PPKKKRKVEDPKDF; PKKKRKVEDPKDFP; KKKRKVEDPKDFPS; KKRKVEDPKDFPSD; KRKVEDPKDFPSDL; RKVEDPKDFPSDLH; KVEDPKDFPSDLHQ; VEDPKDFPSDLHQF; EDPKDFPSDLHQFL; DPKDFPSDLHQFLS; PKDFPSDLHQFLSQ; KDFPSDLHQFLSQA; DFPSDLHQFLSQAV; FPSDLHQFLSQAVF; PSDLHQFLSQAVFS; SDLHQFLSQAVFSN; DLHQFLSQAVFSNR; LHQFLSQAVFSNRT; HQFLSQAVFSNRTL; QFLSQAVFSNRTLA; FLSQAVFSNRTLAC; LSQAVFSNRTLACF; SQAVFSNRTLACFA; QAVFSNRTLACFAV; AVFSNRTLACFAVY; VFSNRTLACFAVYT; FSNRTLACFAVYTT; SNRTLACFAVYTTK; NRTLACFAVYTTKE; RTLACFAVYTTKEK; TLACFAVYTTKEKA; LACFAVYTTKEKAQ; ACFAVYTTKEKAQI; CFAVYTTKEKAQIL; FAVYTTKEKAQILY; AVYTTKEKAQILYK; VYTTKEKAQILYKK; YTTKEKAQILYKKL; TTKEKAQILYKKLM; TKEKAQILYKKLME; KEKAQILYKKLMEK; EKAQILYKKLMEKY; KAQILYKKLMEKYS; AQILYKKLMEKYSV; QILYKKLMEKYSVT; ILYKKLMEKYSVTF; LYKKLMEKYSVTFI; YKKLMEKYSVTFIS; KKLMEKYSVTFISR; KLMEKYSVTFISRH; LMEKYSVTFISRHM; MEKYSVTFISRHMC; EKYSVTFISRHMCA; KYSVTFISRHMCAG; YSVTFISRHMCAGH; SVTFISRHMCAGHN; VTFISRHMCAGHNI; TFISRHMCAGHNII; FISRHMCAGHNIIF; ISRHMCAGHNIIFF; SRHMCAGHNIIFFL; RHMCAGHNIIFFLT; HMCAGHNIIFFLTP; MCAGHNIIFFLTPH; CAGHNIIFFLTPHR; AGHNIIFFLTPHRH; GHNIIFFLTPHRHR; HNIIFFLTPHRHRV; NIIFFLTPHRHRVS; IIFFLTPHRHRVSA; IFFLTPHRHRVSAI; FFLTPHRHRVSAIN; FLTPHRHRVSAINN; LTPHRHRVSAINNF; TPHRHRVSAINNFC; PHRHRVSAINNFCQ; HRHRVSAINNFCQK; RHRVSAINNFCQKL; HRVSAINNFCQKLC; RVSAINNFCQKLCT; VSAINNFCQKLCTF; SAINNFCQKLCTFS; AINNFCQKLCTFSF; INNFCQKLCTFSFL; NNFCQKLCTFSFLI; NFCQKLCTFSFLIC; FCQKLCTFSFLICK; CQKLCTFSFLICKG; QKLCTFSFLICKGV; KLCTFSFLICKGVN; LCTFSFLICKGVNK; CTFSFLICKGVNKE; TFSFLICKGVNKEY; FSFLICKGVNKEYL; SFLICKGVNKEYLL; FLICKGVNKEYLLY; LICKGVNKEYLLYS; ICKGVNKEYLLYSA; CKGVNKEYLLYSAL; KGVNKEYLLYSALT; GVNKEYLLYSALTR; VNKEYLLYSALTRD; NKEYLLYSALTRDP; KEYLLYSALTRDPY; EYLLYSALTRDPYH; YLLYSALTRDPYHT; LLYSALTRDPYHTI; LYSALTRDPYHTIE; YSALTRDPYHTIEE; SALTRDPYHTIEES; ALTRDPYHTIEESI; LTRDPYHTIEESIQ; TRDPYHTIEESIQG; RDPYHTIEESIQGG; DPYHTIEESIQGGL; PYHTIEESIQGGLK; YHTIEESIQGGLKE; HTIEESIQGGLKEH; TIEESIQGGLKEHD; IEESIQGGLKEHDF; EESIQGGLKEHDFS; ESIQGGLKEHDFSP; SIQGGLKEHDFSPE; IQGGLKEHDFSPEE; QGGLKEHDFSPEEP; GGLKEHDFSPEEPE; GLKEHDFSPEEPEE; LKEHDFSPEEPEET; KEHDFSPEEPEETK; EHDFSPEEPEETKQ; HDFSPEEPEETKQV; DFSPEEPEETKQVS; FSPEEPEETKQVSW; SPEEPEETKQVSWK; PEEPEETKQVSWKL; EEPEETKQVSWKLI; EPEETKQVSWKLIT; PEETKQVSWKLITE; EETKQVSWKLITEY; ETKQVSWKLITEYA; TKQVSWKLITEYAV; KQVSWKLITEYAVE; QVSWKLITEYAVET; VSWKLITEYAVETK; SWKLITEYAVETKC; WKLITEYAVETKCE; KLITEYAVETKCED; LITEYAVETKCEDV; ITEYAVETKCEDVF; TEYAVETKCEDVFL; EYAVETKCEDVFLL; YAVETKCEDVFLLL; AVETKCEDVFLLLG; VETKCEDVFLLLGM; ETKCEDVFLLLGMY; TKCEDVFLLLGMYL; KCEDVFLLLGMYLE; CEDVFLLLGMYLEF; EDVFLLLGMYLEFQ; DVFLLLGMYLEFQY; VFLLLGMYLEFQYN; FLLLGMYLEFQYNV; LLLGMYLEFQYNVE; LLGMYLEFQYNVEE; LGMYLEFQYNVEEC; GMYLEFQYNVEECK; MYLEFQYNVEECKK; YLEFQYNVEECKKC; LEFQYNVEECKKCQ; EFQYNVEECKKCQK; FQYNVEECKKCQKK; QYNVEECKKCQKKD; YNVEECKKCQKKDQ; NVEECKKCQKKDQP; VEECKKCQKKDQPY; EECKKCQKKDQPYH; ECKKCQKKDQPYHF; CKKCQKKDQPYHFK; KKCQKKDQPYHFKY; KCQKKDQPYHFKYH; CQKKDQPYHFKYHE; QKKDQPYHFKYHEK; KKDQPYHFKYHEKH; KDQPYHFKYHEKHF; DQPYHFKYHEKHFA; QPYHFKYHEKHFAN; PYHFKYHEKHFANA; YHFKYHEKHFANAI; HFKYHEKHFANAII; FKYHEKHFANAIIF; KYHEKHFANAIIFA; YHEKHFANAIIFAE; HEKHFANAIIFAES; EKHFANAIIFAESK; KHFANAIIFAESKN; HFANAIIFAESKNQ; FANAIIFAESKNQK; ANAIIFAESKNQKS; NAIIFAESKNQKSI; AIIFAESKNQKSIC; IIFAESKNQKSICQ; IFAESKNQKSICQQ; FAESKNQKSICQQA; AESKNQKSICQQAV; ESKNQKSICQQAVD; SKNQKSICQQAVDT; KNQKSICQQAVDTV; NQKSICQQAVDTVL; QKSICQQAVDTVLA; KSICQQAVDTVLAK; SICQQAVDTVLAKK; ICQQAVDTVLAKKR; CQQAVDTVLAKKRV; QQAVDTVLAKKRVD; QAVDTVLAKKRVDT; AVDTVLAKKRVDTL; VDTVLAKKRVDTLH; DTVLAKKRVDTLHM; TVLAKKRVDTLHMT; VLAKKRVDTLHMTR; LAKKRVDTLHMTRE; AKKRVDTLHMTREE; KKRVDTLHMTREEM; KRVDTLHMTREEML; RVDTLHMTREEMLT; VDTLHMTREEMLTE; DTLHMTREEMLTER; TLHMTREEMLTERF; LHMTREEMLTERFN; HMTREEMLTERFNH; MTREEMLTERFNHI; TREEMLTERFNHIL; REEMLTERFNHILD; EEMLTERFNHILDK; EMLTERFNHILDKM; MLTERFNHILDKMD; LTERFNHILDKMDL; TERFNHILDKMDLI; ERFNHILDKMDLIF; RFNHILDKMDLIFG; FNHILDKMDLIFGA; NHILDKMDLIFGAH; HILDKMDLIFGAHG; ILDKMDLIFGAHGN; LDKMDLIFGAHGNA; DKMDLIFGAHGNAV; KMDLIFGAHGNAVL; MDLIFGAHGNAVLE; DLIFGAHGNAVLEQ; LIFGAHGNAVLEQY; IFGAHGNAVLEQYM; FGAHGNAVLEQYMA; GAHGNAVLEQYMAG; AHGNAVLEQYMAGV; HGNAVLEQYMAGVA; GNAVLEQYMAGVAW; NAVLEQYMAGVAWL; AVLEQYMAGVAWLH; VLEQYMAGVAWLHC; LEQYMAGVAWLHCL; EQYMAGVAWLHCLL; QYMAGVAWLHCLLP; YMAGVAWLHCLLPK; MAGVAWLHCLLPKM; AGVAWLHCLLPKMD; GVAWLHCLLPKMDS; VAWLHCLLPKMDSV; AWLHCLLPKMDSVI; WLHCLLPKMDSVIF; LHCLLPKMDSVIFD; HCLLPKMDSVIFDF; CLLPKMDSVIFDFL; LLPKMDSVIFDFLH; LPKMDSVIFDFLHC; PKMDSVIFDFLHCI; KMDSVIFDFLHCIV; MDSVIFDFLHCIVF; DSVIFDFLHCIVFN; SVIFDFLHCIVFNV; VIFDFLHCIVFNVP; IFDFLHCIVFNVPK; FDFLHCIVFNVPKR; DFLHCIVFNVPKRR; FLHCIVFNVPKRRY; LHCIVFNVPKRRYW; HCIVFNVPKRRYWL; CIVFNVPKRRYWLF; IVFNVPKRRYWLFK; VFNVPKRRYWLFKG; FNVPKRRYWLFKGP; NVPKRRYWLFKGPI; VPKRRYWLFKGPID; PKRRYWLFKGPIDS; KRRYWLFKGPIDSG; RRYWLFKGPIDSGK; RYWLFKGPIDSGKT; YWLFKGPIDSGKTT; WLFKGPIDSGKTTL; LFKGPIDSGKTTLA; FKGPIDSGKTTLAA; KGPIDSGKTTLAAG; GPIDSGKTTLAAGL; PIDSGKTTLAAGLL; IDSGKTTLAAGLLD; DSGKTTLAAGLLDL; SGKTTLAAGLLDLC; GKTTLAAGLLDLCG; KTTLAAGLLDLCGG; TTLAAGLLDLCGGK; TLAAGLLDLCGGKA; LAAGLLDLCGGKAL; AAGLLDLCGGKALN; AGLLDLCGGKALNV; GLLDLCGGKALNVN; LLDLCGGKALNVNL; LDLCGGKALNVNLP; DLCGGKALNVNLPM; LCGGKALNVNLPME; CGGKALNVNLPMER; GGKALNVNLPMERL; GKALNVNLPMERLT; KALNVNLPMERLTF; ALNVNLPMERLTFE; LNVNLPMERLTFEL; NVNLPMERLTFELG; VNLPMERLTFELGV; NLPMERLTFELGVA; LPMERLTFELGVAI; PMERLTFELGVAID; MERLTFELGVAIDQ; ERLTFELGVAIDQY; RLTFELGVAIDQYM; LTFELGVAIDQYMV; TFELGVAIDQYMVV; FELGVAIDQYMVVF; ELGVAIDQYMVVFE; LGVAIDQYMVVFED; GVAIDQYMVVFEDV; VAIDQYMVVFEDVK; AIDQYMVVFEDVKG; IDQYMVVFEDVKGT; DQYMVVFEDVKGTG; QYMVVFEDVKGTGA; YMVVFEDVKGTGAE; MVVFEDVKGTGAES; VVFEDVKGTGAESK; VFEDVKGTGAESKD; FEDVKGTGAESKDL; EDVKGTGAESKDLP; DVKGTGAESKDLPS; VKGTGAESKDLPSG; KGTGAESKDLPSGH; GTGAESKDLPSGHG; TGAESKDLPSGHGI; GAESKDLPSGHGIN; AESKDLPSGHGINN; ESKDLPSGHGINNL; SKDLPSGHGINNLD; KDLPSGHGINNLDS; DLPSGHGINNLDSL; LPSGHGINNLDSLR; PSGHGINNLDSLRD; SGHGINNLDSLRDY; GHGINNLDSLRDYL; HGINNLDSLRDYLD; GINNLDSLRDYLDG; INNLDSLRDYLDGS; NNLDSLRDYLDGSV; NLDSLRDYLDGSVK; LDSLRDYLDGSVKV; DSLRDYLDGSVKVN; SLRDYLDGSVKVNL; LRDYLDGSVKVNLE; RDYLDGSVKVNLEK; DYLDGSVKVNLEKK; YLDGSVKVNLEKKH; LDGSVKVNLEKKHL; DGSVKVNLEKKHLN; GSVKVNLEKKHLNK; SVKVNLEKKHLNKR; VKVNLEKKHLNKRT; KVNLEKKHLNKRTQ; VNLEKKHLNKRTQI; NLEKKHLNKRTQIF; LEKKHLNKRTQIFP; EKKHLNKRTQIFPP; KKHLNKRTQIFPPG; KHLNKRTQIFPPGL; HLNKRTQIFPPGLV; LNKRTQIFPPGLVT; NKRTQIFPPGLVTM; KRTQIFPPGLVTMN; RTQIFPPGLVTMNE; TQIFPPGLVTMNEY; QIFPPGLVTMNEYP; IFPPGLVTMNEYPV; FPPGLVTMNEYPVP; PPGLVTMNEYPVPK; PGLVTMNEYPVPKT; GLVTMNEYPVPKTL; LVTMNEYPVPKTLQ; VTMNEYPVPKTLQA; TMNEYPVPKTLQAR; MNEYPVPKTLQARF; NEYPVPKTLQARFV; EYPVPKTLQARFVR; YPVPKTLQARFVRQ; PVPKTLQARFVRQI; VPKTLQARFVRQID; PKTLQARFVRQIDF; KTLQARFVRQIDFR; TLQARFVRQIDFRP; LQARFVRQIDFRPK; QARFVRQIDFRPKI; ARFVRQIDFRPKIY; RFVRQIDFRPKIYL; FVRQIDFRPKIYLR; VRQIDFRPKIYLRK; RQIDFRPKIYLRKS; QIDFRPKIYLRKSL; IDFRPKIYLRKSLQ; DFRPKIYLRKSLQN; FRPKIYLRKSLQNS; RPKIYLRKSLQNSE; PKIYLRKSLQNSEF; KIYLRKSLQNSEFL; IYLRKSLQNSEFLL; YLRKSLQNSEFLLE; LRKSLQNSEFLLEK; RKSLQNSEFLLEKR; KSLQNSEFLLEKRI; SLQNSEFLLEKRIL; LQNSEFLLEKRILQ; QNSEFLLEKRILQS; NSEFLLEKRILQSG; SEFLLEKRILQSGM; EFLLEKRILQSGMT; FLLEKRILQSGMTL; LLEKRILQSGMTLL; LEKRILQSGMTLLL; EKRILQSGMTLLLL; KRILQSGMTLLLLL; RILQSGMTLLLLLI; ILQSGMTLLLLLIW; LQSGMTLLLLLIWF; QSGMTLLLLLIWFR; SGMTLLLLLIWFRP; GMTLLLLLIWFRPV; MTLLLLLIWFRPVA; TLLLLLIWFRPVAD; LLLLLIWFRPVADF; LLLLIWFRPVADFA; LLLIWFRPVADFAT; LLIWFRPVADFATD; LIWFRPVADFATDI; IWFRPVADFATDIQ; WFRPVADFATDIQS; FRPVADFATDIQSR; RPVADFATDIQSRI; PVADFATDIQSRIV; VADFATDIQSRIVE; ADFATDIQSRIVEW; DFATDIQSRIVEWK; FATDIQSRIVEWKE; ATDIQSRIVEWKER; TDIQSRIVEWKERL; DIQSRIVEWKERLD; IQSRIVEWKERLDS; QSRIVEWKERLDSE; SRIVEWKERLDSEI; RIVEWKERLDSEIS; IVEWKERLDSEISM; VEWKERLDSEISMY; EWKERLDSEISMYT; WKERLDSEISMYTF; KERLDSEISMYTFS; ERLDSEISMYTFSR; RLDSEISMYTFSRM; LDSEISMYTFSRMK; DSEISMYTFSRMKY; SEISMYTFSRMKYN; EISMYTFSRMKYNI; ISMYTFSRMKYNIC; SMYTFSRMKYNICM; MYTFSRMKYNICMG; YTFSRMKYNICMGK; TFSRMKYNICMGKC; FSRMKYNICMGKCI; SRMKYNICMGKCIL; RMKYNICMGKCILD; MKYNICMGKCILDI; KYNICMGKCILDIT; YNICMGKCILDITR; NICMGKCILDITRE; ICMGKCILDITREE; CMGKCILDITREED; MGKCILDITREEDS; GKCILDITREEDSE; KCILDITREEDSET; CILDITREEDSETE; ILDITREEDSETED; LDITREEDSETEDS; DITREEDSETEDSG; ITREEDSETEDSGH; TREEDSETEDSGHG; REEDSETEDSGHGS; EEDSETEDSGHGSS; EDSETEDSGHGSST; DSETEDSGHGSSTE; SETEDSGHGSSTES; ETEDSGHGSSTESQ; TEDSGHGSSTESQS; EDSGHGSSTESQSQ; DSGHGSSTESQSQC; SGHGSSTESQSQCS; GHGSSTESQSQCSS; HGSSTESQSQCSSQ; GSSTESQSQCSSQV; SSTESQSQCSSQVS; STESQSQCSSQVSD; TESQSQCSSQVSDT; ESQSQCSSQVSDTS; SQSQCSSQVSDTSA; QSQCSSQVSDTSAP; SQCSSQVSDTSAPA; QCSSQVSDTSAPAE; CSSQVSDTSAPAED; SSQVSDTSAPAEDS; SQVSDTSAPAEDSQ; QVSDTSAPAEDSQR; VSDTSAPAEDSQRS; SDTSAPAEDSQRSD; DTSAPAEDSQRSDP; TSAPAEDSQRSDPH; SAPAEDSQRSDPHS; APAEDSQRSDPHSQ; PAEDSQRSDPHSQE; AEDSQRSDPHSQEL; EDSQRSDPHSQELH; DSQRSDPHSQELHL; SQRSDPHSQELHLC; QRSDPHSQELHLCK; RSDPHSQELHLCKG; SDPHSQELHLCKGF; DPHSQELHLCKGFQ; PHSQELHLCKGFQC; HSQELHLCKGFQCF; SQELHLCKGFQCFK; QELHLCKGFQCFKR; ELHLCKGFQCFKRP; LHLCKGFQCFKRPK; HLCKGFQCFKRPKT; LCKGFQCFKRPKTP; CKGFQCFKRPKTPP; KGFQCFKRPKTPPP; GFQCFKRPKTPPPK; MYMYNKSTCLKHFG; YMYNKSTCLKHFGL; MYNKSTCLKHFGLQ; YNKSTCLKHFGLQL; NKSTCLKHFGLQLS; KSTCLKHFGLQLSL; STCLKHFGLQLSLF; TCLKHFGLQLSLFV; CLKHFGLQLSLFVN; LKHFGLQLSLFVNI; KHFGLQLSLFVNIS; HFGLQLSLFVNISY; FGLQLSLFVNISYH; GLQLSLFVNISYHI; LQLSLFVNISYHIW; QLSLFVNISYHIWV; LSLFVNISYHIWVP; SLFVNISYHIWVPW; LFVNISYHIWVPWK; FVNISYHIWVPWKS; VNISYHIWVPWKSF; NISYHIWVPWKSFC; ISYHIWVPWKSFCA; SYHIWVPWKSFCAI; YHIWVPWKSFCAIK; HIWVPWKSFCAIKH; IWVPWKSFCAIKHP; WVPWKSFCAIKHPN; VPWKSFCAIKHPNL; PWKSFCAIKHPNLF; WKSFCAIKHPNLFY; KSFCAIKHPNLFYL; SFCAIKHPNLFYLG; FCAIKHPNLFYLGF; CAIKHPNLFYLGFH; AIKHPNLFYLGFHT; IKHPNLFYLGFHTI; KHPNLFYLGFHTIH; HPNLFYLGFHTIHR; PNLFYLGFHTIHRL; NLFYLGFHTIHRLP; LFYLGFHTIHRLPI; FYLGFHTIHRLPIH; YLGFHTIHRLPIHS; LGFHTIHRLPIHSL; GFHTIHRLPIHSLG; FHTIHRLPIHSLGS; HTIHRLPIHSLGSP; TIHRLPIHSLGSPV; IHRLPIHSLGSPVY; HRLPIHSLGSPVYK; RLPIHSLGSPVYKV; LPIHSLGSPVYKVT; QKGNWVRILYRSFS; KGNWVRILYRSFSQ; GNWVRILYRSFSQA; NWVRILYRSFSQAD; WVRILYRSFSQADL; VRILYRSFSQADLK; RILYRSFSQADLKI; ILYRSFSQADLKIS; LYRSFSQADLKISC; YRSFSQADLKISCK; RSFSQADLKISCKA; SFSQADLKISCKAS; FSQADLKISCKASP; SQADLKISCKASPL; QADLKISCKASPLL; ADLKISCKASPLLC; DLKISCKASPLLCS; LKISCKASPLLCSR; KISCKASPLLCSRA; ISCKASPLLCSRAV; SCKASPLLCSRAVS; CKASPLLCSRAVSK; KASPLLCSRAVSKQ; ASPLLCSRAVSKQA; SPLLCSRAVSKQAT; PLLCSRAVSKQATN; LLCSRAVSKQATNI; LCSRAVSKQATNIS; CSRAVSKQATNISS; NIQAISFTKRPHTL; IQAISFTKRPHTLF; QAISFTKRPHTLFI; QHCGSCVGHMKYWG; HCGSCVGHMKYWGN; CGSCVGHMKYWGNI; GSCVGHMKYWGNIF; SCVGHMKYWGNIFP; CVGHMKYWGNIFPS; VGHMKYWGNIFPSC; GHMKYWGNIFPSCE; HMKYWGNIFPSCES; MKYWGNIFPSCESP; KYWGNIFPSCESPK; YWGNIFPSCESPKI; WGNIFPSCESPKIP; GNIFPSCESPKIPS; NIFPSCESPKIPSI; IFPSCESPKIPSIF; FPSCESPKIPSIFI; PSCESPKIPSIFIS; SCESPKIPSIFIST; CESPKIPSIFISTG; ESPKIPSIFISTGI; SPKIPSIFISTGIR; PKIPSIFISTGIRY; KIPSIFISTGIRYP; IPSIFISTGIRYPA; PSIFISTGIRYPAL; SIFISTGIRYPALN; IFISTGIRYPALNW; FISTGIRYPALNWI; ISTGIRYPALNWIS; STGIRYPALNWISI; TGIRYPALNWISIV; GIRYPALNWISIVF; IRYPALNWISIVFV; RYPALNWISIVFVQ; YPALNWISIVFVQI; PALNWISIVFVQIG; ALNWISIVFVQIGL; LNWISIVFVQIGLM; NWISIVFVQIGLMV; WISIVFVQIGLMVS; ISIVFVQIGLMVSI; SIVFVQIGLMVSIH; IVFVQIGLMVSIHY; VFVQIGLMVSIHYL; FVQIGLMVSIHYLG; VQIGLMVSIHYLGL; QIGLMVSIHYLGLG; IGLMVSIHYLGLGC; GLMVSIHYLGLGCW; LMVSIHYLGLGCWV; MVSIHYLGLGCWVF; VSIHYLGLGCWVFR; SIHYLGLGCWVFRG; IHYLGLGCWVFRGY; HYLGLGCWVFRGYS; YLGLGCWVFRGYST; LGLGCWVFRGYSTI; GLGCWVFRGYSTIR; LGCWVFRGYSTIRV; GCWVFRGYSTIRVL; HSLHFQGFSTYSKE; SLHFQGFSTYSKEV; LHFQGFSTYSKEVE; HFQGFSTYSKEVEI; FQGFSTYSKEVEIT; QGFSTYSKEVEITA; GFSTYSKEVEITAL; FSTYSKEVEITALN; STYSKEVEITALNR; TYSKEVEITALNRF; YSKEVEITALNRFS; SKEVEITALNRFSS; KEVEITALNRFSST; EVEITALNRFSSTM; VEITALNRFSSTML; EITALNRFSSTMLM; ITALNRFSSTMLMH; TALNRFSSTMLMHF; ALNRFSSTMLMHFL; PCMKVKHASYSNNL; CMKVKHASYSNNLC; MKVKHASYSNNLCL; KVKHASYSNNLCLY; VKHASYSNNLCLYS; KHASYSNNLCLYSY; HASYSNNLCLYSYS; ASYSNNLCLYSYSL; SYSNNLCLYSYSLP; YSNNLCLYSYSLPH; SNNLCLYSYSLPHQ; IGEGNSCCAVTGKH; GEGNSCCAVTGKHF; EGNSCCAVTGKHFS; GNSCCAVTGKHFSL; NSCCAVTGKHFSLW; SCCAVTGKHFSLWA; CCAVTGKHFSLWAI; CAVTGKHFSLWAIT; AVTGKHFSLWAITA; VTGKHFSLWAITAK; TGKHFSLWAITAKV; GKHFSLWAITAKVI; KHFSLWAITAKVIF; HFSLWAITAKVIFS; FSLWAITAKVIFST; TKAPKVFIWIPHFW; KAPKVFIWIPHFWV; EAFYLCNSIYPSFN; AFYLCNSIYPSFNF; FWHLHGFLWLFGSC; WHLHGFLWLFGSCP; HLHGFLWLFGSCPW; LHGFLWLFGSCPWT; HGFLWLFGSCPWTL; GFLWLFGSCPWTLS; FLWLFGSCPWTLSF; LWLFGSCPWTLSFS; WLFGSCPWTLSFSF; LFGSCPWTLSFSFG; FGSCPWTLSFSFGW; GSCPWTLSFSFGWG; SCPWTLSFSFGWGH; CPWTLSFSFGWGHL; PWTLSFSFGWGHLH; WTLSFSFGWGHLHM; TLSFSFGWGHLHML; LSFSFGWGHLHMLQ; SFSFGWGHLHMLQE; FSFGWGHLHMLQEQ; SFGWGHLHMLQEQV; FGWGHLHMLQEQVL; GWGHLHMLQEQVLQ; WGHLHMLQEQVLQS; GHLHMLQEQVLQSR; HLHMLQEQVLQSRT; LHMLQEQVLQSRTG; HMLQEQVLQSRTGL; MLQEQVLQSRTGLE; LQEQVLQSRTGLEV; QEQVLQSRTGLEVK; EQVLQSRTGLEVKA; QVLQSRTGLEVKAT; VLQSRTGLEVKATS; LQSRTGLEVKATSI; QSRTGLEVKATSIE; SRTGLEVKATSIEE; RTGLEVKATSIEEQ; TGLEVKATSIEEQF; GLEVKATSIEEQFF; LEVKATSIEEQFFD; TLLNVHFVDFLSPF; LLNVHFVDFLSPFF; LNVHFVDFLSPFFV; LLLYCQHHLYYKYG; LLYCQHHLYYKYGQ; LYCQHHLYYKYGQN; YCQHHLYYKYGQNV; CQHHLYYKYGQNVH; QHHLYYKYGQNVHG; HHLYYKYGQNVHGY; HLYYKYGQNVHGYL; LYYKYGQNVHGYLP; YYKYGQNVHGYLPF; YKYGQNVHGYLPFQ; KYGQNVHGYLPFQL; YGQNVHGYLPFQLL; GQNVHGYLPFQLLV; GKDQNNIVEYNYKS; KDQNNIVEYNYKSL; QKYLHQETEYHSTH; KYLHQETEYHSTHL; YLHQETEYHSTHLG; TIPKPCLIADRGLQ; IPKPCLIADRGLQW; PKPCLIADRGLQWK; KPCLIADRGLQWKL; PCLIADRGLQWKLC; CLIADRGLQWKLCD; LIADRGLQWKLCDP; IADRGLQWKLCDPN; ADRGLQWKLCDPNH; DRGLQWKLCDPNHQ; RGLQWKLCDPNHQR; GLQWKLCDPNHQRT; LQWKLCDPNHQRTY; QWKLCDPNHQRTYT; WKLCDPNHQRTYTL; KLCDPNHQRTYTLL; LCDPNHQRTYTLLE; CDPNHQRTYTLLEL; DPNHQRTYTLLELR; PNHQRTYTLLELRN; PQEHQQLQHMFEEL; QEHQQLQHMFEELG; EHQQLQHMFEELGL; QQQPPQQQFQPLKI; QQPPQQQFQPLKIL; QPPQQQFQPLKILW; PPQQQFQPLKILWQ; PQQQFQPLKILWQQ; QQQFQPLKILWQQQ; QQFQPLKILWQQQP; QFQPLKILWQQQPQ; FQPLKILWQQQPQI; QPLKILWQQQPQIH; PLKILWQQQPQIHW; LKILWQQQPQIHWQ; KILWQQQPQIHWQL; ILWQQQPQIHWQLG; LWQQQPQIHWQLGP; WQQQPQIHWQLGPP; QQQPQIHWQLGPPK; QQPQIHWQLGPPKV; QPQIHWQLGPPKVL; PQIHWQLGPPKVLE; QIHWQLGPPKVLEQ; IHWQLGPPKVLEQH; HWQLGPPKVLEQHP; TWKYKKKGITYLGV; WKYKKKGITYLGVF; KYKKKGITYLGVFY; YKKKGITYLGVFYR; KKKGITYLGVFYRV; KKGITYLGVFYRVF; KGITYLGVFYRVFY; GITYLGVFYRVFYS; ITYLGVFYRVFYSR; SSGTFVFPVYTVFT; SGTFVFPVYTVFTS; GTFVFPVYTVFTST; TFVFPVYTVFTSTK; FVFPVYTVFTSTKF; VFPVYTVFTSTKFQ; FPVYTVFTSTKFQQ; PVYTVFTSTKFQQK; VYTVFTSTKFQQKL; NKNKNPLSSFFCSS; KNKNPLSSFFCSSP; NKNPLSSFFCSSPG; KNPLSSFFCSSPGF; NPLSSFFCSSPGFT; PLSSFFCSSPGFTN; LSSFFCSSPGFTNF; SSFFCSSPGFTNFH; LGTRPRFLGSQNMS; GTRPRFLGSQNMSV; TRPRFLGSQNMSVM; RPRFLGSQNMSVMH; PRFLGSQNMSVMHF; RFLGSQNMSVMHFP; FLGSQNMSVMHFPS; AAPPCESCTFLPEV; APPCESCTFLPEVM; PPCESCTFLPEVMV; PCESCTFLPEVMVW; CESCTFLPEVMVWL; ESCTFLPEVMVWLH; SCTFLPEVMVWLHS; CTFLPEVMVWLHSP; TFLPEVMVWLHSPV; FLPEVMVWLHSPVS; LPEVMVWLHSPVSH; PEVMVWLHSPVSHA; EVMVWLHSPVSHAL; VMVWLHSPVSHALS; MVWLHSPVSHALSF; VWLHSPVSHALSFL; WLHSPVSHALSFLR; LHSPVSHALSFLRS; HSPVSHALSFLRSW; SPVSHALSFLRSWF; PVSHALSFLRSWFG; VSHALSFLRSWFGC; SHALSFLRSWFGCI; HALSFLRSWFGCIP; ALSFLRSWFGCIPW; LSFLRSWFGCIPWV; SFLRSWFGCIPWVS; FLRSWFGCIPWVSS; LRSWFGCIPWVSSS; RSWFGCIPWVSSSS; SWFGCIPWVSSSSL; WFGCIPWVSSSSLW; FGCIPWVSSSSLWP; GCIPWVSSSSLWPF; CIPWVSSSSLWPFF; IPWVSSSSLWPFFL; YIRGRGRLCLHPFS; IRGRGRLCLHPFSQ; RGRGRLCLHPFSQV; GRGRLCLHPFSQVV; RGRLCLHPFSQVVR; GRLCLHPFSQVVRV; RLCLHPFSQVVRVW; LCLHPFSQVVRVWR; CLHPFSQVVRVWRL; LHPFSQVVRVWRLF; HPFSQVVRVWRLFL; PFSQVVRVWRLFLR; FSQVVRVWRLFLRP; SQVVRVWRLFLRPS; QVVRVWRLFLRPSK; VVRVWRLFLRPSKT; VRVWRLFLRPSKTI; RVWRLFLRPSKTIW; VWRLFLRPSKTIWG; WRLFLRPSKTIWGN; RLFLRPSKTIWGNP; LFLRPSKTIWGNPY; FLRPSKTIWGNPYS; LRPSKTIWGNPYSF; RPSKTIWGNPYSFA; PSKTIWGNPYSFAI; SKTIWGNPYSFAIF; KTIWGNPYSFAIFA; TIWGNPYSFAIFAK 15 mers: KSCLGKSSLNEKSLF; SCLGKSSLNEKSLFK; CLGKSSLNEKSLFKE; LGKSSLNEKSLFKEV; FSSLPRYPVLQGMAY; SSLPRYPVLQGMAYL; SLPRYPVLQGMAYLF; LPRYPVLQGMAYLFQ; PRYPVLQGMAYLFQK; RYPVLQGMAYLFQKA; YPVLQGMAYLFQKAF; PVLQGMAYLFQKAFC; VLQGMAYLFQKAFCA; LQGMAYLFQKAFCAL; QGMAYLFQKAFCALP; GMAYLFQKAFCALPL; MAYLFQKAFCALPLH; AYLFQKAFCALPLHA; YLFQKAFCALPLHAM; LFQKAFCALPLHAMS; FQKAFCALPLHAMSA; KIFKKRALGLDRLLL; IFKKRALGLDRLLLH; RNSAMVGPNNWRNSL; NSAMVGPNNWRNSLQ; SAMVGPNNWRNSLQR; AMVGPNNWRNSLQRS; MVGPNNWRNSLQRSK; VGPNNWRNSLQRSKA; GPNNWRNSLQRSKAL; PNNWRNSLQRSKALR; VPTYGTEEWESWWSS; PTYGTEEWESWWSSF; TYGTEEWESWWSSFN; YGTEEWESWWSSFNE; GTEEWESWWSSFNEK; TEEWESWWSSFNEKW; EEWESWWSSFNEKWD; EWESWWSSFNEKWDE; WESWWSSFNEKWDED; ESWWSSFNEKWDEDL; SWWSSFNEKWDEDLF; WWSSFNEKWDEDLFC; WSSFNEKWDEDLFCH; SSFNEKWDEDLFCHE; SFNEKWDEDLFCHED; FNEKWDEDLFCHEDM; NEKWDEDLFCHEDMF; EKWDEDLFCHEDMFA; KWDEDLFCHEDMFAS; WDEDLFCHEDMFASD; DEDLFCHEDMFASDE; EDLFCHEDMFASDEE; DLFCHEDMFASDEEA; LFCHEDMFASDEEAT; FCHEDMFASDEEATA; CHEDMFASDEEATAD; HEDMFASDEEATADS; EDMFASDEEATADSQ; DMFASDEEATADSQH; MFASDEEATADSQHS; FASDEEATADSQHST; ASDEEATADSQHSTP; SDEEATADSQHSTPP; DEEATADSQHSTPPK; EEATADSQHSTPPKK; EATADSQHSTPPKKK; ATADSQHSTPPKKKR; TADSQHSTPPKKKRK; ADSQHSTPPKKKRKV; DSQHSTPPKKKRKVE; SQHSTPPKKKRKVED; QHSTPPKKKRKVEDP; HSTPPKKKRKVEDPK; STPPKKKRKVEDPKD; TPPKKKRKVEDPKDF; PPKKKRKVEDPKDFP; PKKKRKVEDPKDFPS; KKKRKVEDPKDFPSD; KKRKVEDPKDFPSDL; KRKVEDPKDFPSDLH; RKVEDPKDFPSDLHQ; KVEDPKDFPSDLHQF; VEDPKDFPSDLHQFL; EDPKDFPSDLHQFLS; DPKDFPSDLHQFLSQ; PKDFPSDLHQFLSQA; KDFPSDLHQFLSQAV; DFPSDLHQFLSQAVF; FPSDLHQFLSQAVFS; PSDLHQFLSQAVFSN; SDLHQFLSQAVFSNR; DLHQFLSQAVFSNRT; LHQFLSQAVFSNRTL; HQFLSQAVFSNRTLA; QFLSQAVFSNRTLAC; FLSQAVFSNRTLACF; LSQAVFSNRTLACFA; SQAVFSNRTLACFAV; QAVFSNRTLACFAVY; AVFSNRTLACFAVYT; VFSNRTLACFAVYTT; FSNRTLACFAVYTTK; SNRTLACFAVYTTKE; NRTLACFAVYTTKEK; RTLACFAVYTTKEKA; TLACFAVYTTKEKAQ; LACFAVYTTKEKAQI; ACFAVYTTKEKAQIL; CFAVYTTKEKAQILY; FAVYTTKEKAQILYK; AVYTTKEKAQILYKK; VYTTKEKAQILYKKL; YTTKEKAQILYKKLM; TTKEKAQILYKKLME; TKEKAQILYKKLMEK; KEKAQILYKKLMEKY; EKAQILYKKLMEKYS; KAQILYKKLMEKYSV; AQILYKKLMEKYSVT; QILYKKLMEKYSVTF; ILYKKLMEKYSVTFI; LYKKLMEKYSVTFIS; YKKLMEKYSVTFISR; KKLMEKYSVTFISRH; KLMEKYSVTFISRHM; LMEKYSVTFISRHMC; MEKYSVTFISRHMCA; EKYSVTFISRHMCAG; KYSVTFISRHMCAGH; YSVTFISRHMCAGHN; SVTFISRHMCAGHNI; VTFISRHMCAGHNII; TFISRHMCAGHNIIF; FISRHMCAGHNIIFF; ISRHMCAGHNIIFFL; SRHMCAGHNIIFFLT; RHMCAGHNIIFFLTP; HMCAGHNIIFFLTPH; MCAGHNIIFFLTPHR; CAGHNIIFFLTPHRH; AGHNIIFFLTPHRHR; GHNIIFFLTPHRHRV; HNIIFFLTPHRHRVS; NIIFFLTPHRHRVSA; IIFFLTPHRHRVSAI; IFFLTPHRHRVSAIN; FFLTPHRHRVSAINN; FLTPHRHRVSAINNF; LTPHRHRVSAINNFC; TPHRHRVSAINNFCQ; PHRHRVSAINNFCQK; HRHRVSAINNFCQKL; RHRVSAINNFCQKLC; HRVSAINNFCQKLCT; RVSAINNFCQKLCTF; VSAINNFCQKLCTFS; SAINNFCQKLCTFSF; AINNFCQKLCTFSFL; INNFCQKLCTFSFLI; NNFCQKLCTFSFLIC; NFCQKLCTFSFLICK; FCQKLCTFSFLICKG; CQKLCTFSFLICKGV; QKLCTFSFLICKGVN; KLCTFSFLICKGVNK; LCTFSFLICKGVNKE; CTFSFLICKGVNKEY; TFSFLICKGVNKEYL; FSFLICKGVNKEYLL; SFLICKGVNKEYLLY; FLICKGVNKEYLLYS; LICKGVNKEYLLYSA; ICKGVNKEYLLYSAL; CKGVNKEYLLYSALT; KGVNKEYLLYSALTR; GVNKEYLLYSALTRD; VNKEYLLYSALTRDP; NKEYLLYSALTRDPY; KEYLLYSALTRDPYH; EYLLYSALTRDPYHT; YLLYSALTRDPYHTI; LLYSALTRDPYHTIE; LYSALTRDPYHTIEE; YSALTRDPYHTIEES; SALTRDPYHTIEESI; ALTRDPYHTIEESIQ; LTRDPYHTIEESIQG; TRDPYHTIEESIQGG; RDPYHTIEESIQGGL; DPYHTIEESIQGGLK; PYHTIEESIQGGLKE; YHTIEESIQGGLKEH; HTIEESIQGGLKEHD; TIEESIQGGLKEHDF; IEESIQGGLKEHDFS; EESIQGGLKEHDFSP; ESIQGGLKEHDFSPE; SIQGGLKEHDFSPEE; IQGGLKEHDFSPEEP; QGGLKEHDFSPEEPE; GGLKEHDFSPEEPEE; GLKEHDFSPEEPEET; LKEHDFSPEEPEETK; KEHDFSPEEPEETKQ; EHDFSPEEPEETKQV; HDFSPEEPEETKQVS; DFSPEEPEETKQVSW; FSPEEPEETKQVSWK; SPEEPEETKQVSWKL; PEEPEETKQVSWKLI; EEPEETKQVSWKLIT; EPEETKQVSWKLITE; PEETKQVSWKLITEY; EETKQVSWKLITEYA; ETKQVSWKLITEYAV; TKQVSWKLITEYAVE; KQVSWKLITEYAVET; QVSWKLITEYAVETK; VSWKLITEYAVETKC; SWKLITEYAVETKCE; WKLITEYAVETKCED; KLITEYAVETKCEDV; LITEYAVETKCEDVF; ITEYAVETKCEDVFL; TEYAVETKCEDVFLL; EYAVETKCEDVFLLL; YAVETKCEDVFLLLG; AVETKCEDVFLLLGM; VETKCEDVFLLLGMY; ETKCEDVFLLLGMYL; TKCEDVFLLLGMYLE; KCEDVFLLLGMYLEF; CEDVFLLLGMYLEFQ; EDVFLLLGMYLEFQY; DVFLLLGMYLEFQYN; VFLLLGMYLEFQYNV; FLLLGMYLEFQYNVE; LLLGMYLEFQYNVEE; LLGMYLEFQYNVEEC; LGMYLEFQYNVEECK; GMYLEFQYNVEECKK; MYLEFQYNVEECKKC; YLEFQYNVEECKKCQ; LEFQYNVEECKKCQK; EFQYNVEECKKCQKK; FQYNVEECKKCQKKD; QYNVEECKKCQKKDQ; YNVEECKKCQKKDQP; NVEECKKCQKKDQPY; VEECKKCQKKDQPYH; EECKKCQKKDQPYHF; ECKKCQKKDQPYHFK; CKKCQKKDQPYHFKY; KKCQKKDQPYHFKYH; KCQKKDQPYHFKYHE; CQKKDQPYHFKYHEK; QKKDQPYHFKYHEKH; KKDQPYHFKYHEKHF; KDQPYHFKYHEKHFA; DQPYHFKYHEKHFAN; QPYHFKYHEKHFANA; PYHFKYHEKHFANAI; YHFKYHEKHFANAII; HFKYHEKHFANAIIF; FKYHEKHFANAIIFA; KYHEKHFANAIIFAE; YHEKHFANAIIFAES; HEKHFANAIIFAESK; EKHFANAIIFAESKN; KHFANAIIFAESKNQ; HFANAIIFAESKNQK; FANAIIFAESKNQKS; ANAIIFAESKNQKSI; NAIIFAESKNQKSIC; AIIFAESKNQKSICQ; IIFAESKNQKSICQQ; IFAESKNQKSICQQA; FAESKNQKSICQQAV; AESKNQKSICQQAVD; ESKNQKSICQQAVDT; SKNQKSICQQAVDTV; KNQKSICQQAVDTVL; NQKSICQQAVDTVLA; QKSICQQAVDTVLAK; KSICQQAVDTVLAKK; SICQQAVDTVLAKKR; ICQQAVDTVLAKKRV; CQQAVDTVLAKKRVD; QQAVDTVLAKKRVDT; QAVDTVLAKKRVDTL; AVDTVLAKKRVDTLH; VDTVLAKKRVDTLHM; DTVLAKKRVDTLHMT; TVLAKKRVDTLHMTR; VLAKKRVDTLHMTRE; LAKKRVDTLHMTREE; AKKRVDTLHMTREEM; KKRVDTLHMTREEML; KRVDTLHMTREEMLT; RVDTLHMTREEMLTE; VDTLHMTREEMLTER; DTLHMTREEMLTERF; TLHMTREEMLTERFN; LHMTREEMLTERFNH; HMTREEMLTERFNHI; MTREEMLTERFNHIL; TREEMLTERFNHILD; REEMLTERFNHILDK; EEMLTERFNHILDKM; EMLTERFNHILDKMD; MLTERFNHILDKMDL; LTERFNHILDKMDLI; TERFNHILDKMDLIF; ERFNHILDKMDLIFG; RFNHILDKMDLIFGA; FNHILDKMDLIFGAH; NHILDKMDLIFGAHG; HILDKMDLIFGAHGN; ILDKMDLIFGAHGNA; LDKMDLIFGAHGNAV; DKMDLIFGAHGNAVL; KMDLIFGAHGNAVLE; MDLIFGAHGNAVLEQ; DLIFGAHGNAVLEQY; LIFGAHGNAVLEQYM; IFGAHGNAVLEQYMA; FGAHGNAVLEQYMAG; GAHGNAVLEQYMAGV; AHGNAVLEQYMAGVA; HGNAVLEQYMAGVAW; GNAVLEQYMAGVAWL; NAVLEQYMAGVAWLH; AVLEQYMAGVAWLHC; VLEQYMAGVAWLHCL; LEQYMAGVAWLHCLL; EQYMAGVAWLHCLLP; QYMAGVAWLHCLLPK; YMAGVAWLHCLLPKM; MAGVAWLHCLLPKMD; AGVAWLHCLLPKMDS; GVAWLHCLLPKMDSV; VAWLHCLLPKMDSVI; AWLHCLLPKMDSVIF; WLHCLLPKMDSVIFD; LHCLLPKMDSVIFDF; HCLLPKMDSVIFDFL; CLLPKMDSVIFDFLH; LLPKMDSVIFDFLHC; LPKMDSVIFDFLHCI; PKMDSVIFDFLHCIV; KMDSVIFDFLHCIVF; MDSVIFDFLHCIVFN; DSVIFDFLHCIVFNV; SVIFDFLHCIVFNVP; VIFDFLHCIVFNVPK; IFDFLHCIVFNVPKR; FDFLHCIVFNVPKRR; DFLHCIVFNVPKRRY; FLHCIVFNVPKRRYW; LHCIVFNVPKRRYWL; HCIVFNVPKRRYWLF; CIVFNVPKRRYWLFK; IVFNVPKRRYWLFKG; VFNVPKRRYWLFKGP; FNVPKRRYWLFKGPI; NVPKRRYWLFKGPID; VPKRRYWLFKGPIDS; PKRRYWLFKGPIDSG; KRRYWLFKGPIDSGK; RRYWLFKGPIDSGKT; RYWLFKGPIDSGKTT; YWLFKGPIDSGKTTL; WLFKGPIDSGKTTLA; LFKGPIDSGKTTLAA; FKGPIDSGKTTLAAG; KGPIDSGKTTLAAGL; GPIDSGKTTLAAGLL; PIDSGKTTLAAGLLD; IDSGKTTLAAGLLDL; DSGKTTLAAGLLDLC; SGKTTLAAGLLDLCG; GKTTLAAGLLDLCGG; KTTLAAGLLDLCGGK; TTLAAGLLDLCGGKA; TLAAGLLDLCGGKAL; LAAGLLDLCGGKALN; AAGLLDLCGGKALNV; AGLLDLCGGKALNVN; GLLDLCGGKALNVNL; LLDLCGGKALNVNLP; LDLCGGKALNVNLPM; DLCGGKALNVNLPME; LCGGKALNVNLPMER; CGGKALNVNLPMERL; GGKALNVNLPMERLT; GKALNVNLPMERLTF; KALNVNLPMERLTFE; ALNVNLPMERLTFEL; LNVNLPMERLTFELG; NVNLPMERLTFELGV; VNLPMERLTFELGVA; NLPMERLTFELGVAI; LPMERLTFELGVAID; PMERLTFELGVAIDQ; MERLTFELGVAIDQY; ERLTFELGVAIDQYM; RLTFELGVAIDQYMV; LTFELGVAIDQYMVV; TFELGVAIDQYMVVF; FELGVAIDQYMVVFE; ELGVAIDQYMVVFED; LGVAIDQYMVVFEDV; GVAIDQYMVVFEDVK; VAIDQYMVVFEDVKG; AIDQYMVVFEDVKGT; IDQYMVVFEDVKGTG; DQYMVVFEDVKGTGA; QYMVVFEDVKGTGAE; YMVVFEDVKGTGAES; MVVFEDVKGTGAESK; VVFEDVKGTGAESKD; VFEDVKGTGAESKDL; FEDVKGTGAESKDLP; EDVKGTGAESKDLPS; DVKGTGAESKDLPSG; VKGTGAESKDLPSGH; KGTGAESKDLPSGHG; GTGAESKDLPSGHGI; TGAESKDLPSGHGIN; GAESKDLPSGHGINN; AESKDLPSGHGINNL; ESKDLPSGHGINNLD; SKDLPSGHGINNLDS; KDLPSGHGINNLDSL; DLPSGHGINNLDSLR; LPSGHGINNLDSLRD; PSGHGINNLDSLRDY; SGHGINNLDSLRDYL; GHGINNLDSLRDYLD; HGINNLDSLRDYLDG; GINNLDSLRDYLDGS; INNLDSLRDYLDGSV; NNLDSLRDYLDGSVK; NLDSLRDYLDGSVKV; LDSLRDYLDGSVKVN; DSLRDYLDGSVKVNL; SLRDYLDGSVKVNLE; LRDYLDGSVKVNLEK; RDYLDGSVKVNLEKK; DYLDGSVKVNLEKKH; YLDGSVKVNLEKKHL; LDGSVKVNLEKKHLN; DGSVKVNLEKKHLNK; GSVKVNLEKKHLNKR; SVKVNLEKKHLNKRT; VKVNLEKKHLNKRTQ; KVNLEKKHLNKRTQI; VNLEKKHLNKRTQIF; NLEKKHLNKRTQIFP; LEKKHLNKRTQIFPP; EKKHLNKRTQIFPPG; KKHLNKRTQIFPPGL; KHLNKRTQIFPPGLV; HLNKRTQIFPPGLVT; LNKRTQIFPPGLVTM; NKRTQIFPPGLVTMN; KRTQIFPPGLVTMNE; RTQIFPPGLVTMNEY; TQIFPPGLVTMNEYP; QIFPPGLVTMNEYPV; IFPPGLVTMNEYPVP; FPPGLVTMNEYPVPK; PPGLVTMNEYPVPKT; PGLVTMNEYPVPKTL; GLVTMNEYPVPKTLQ; LVTMNEYPVPKTLQA; VTMNEYPVPKTLQAR; TMNEYPVPKTLQARF; MNEYPVPKTLQARFV; NEYPVPKTLQARFVR; EYPVPKTLQARFVRQ; YPVPKTLQARFVRQI; PVPKTLQARFVRQID; VPKTLQARFVRQIDF; PKTLQARFVRQIDFR; KTLQARFVRQIDFRP; TLQARFVRQIDFRPK; LQARFVRQIDFRPKI; QARFVRQIDFRPKIY; ARFVRQIDFRPKIYL; RFVRQIDFRPKIYLR; FVRQIDFRPKIYLRK; VRQIDFRPKIYLRKS; RQIDFRPKIYLRKSL; QIDFRPKIYLRKSLQ; IDFRPKIYLRKSLQN; DFRPKIYLRKSLQNS; FRPKIYLRKSLQNSE; RPKIYLRKSLQNSEF; PKIYLRKSLQNSEFL; KIYLRKSLQNSEFLL; IYLRKSLQNSEFLLE; YLRKSLQNSEFLLEK; LRKSLQNSEFLLEKR; RKSLQNSEFLLEKRI; KSLQNSEFLLEKRIL; SLQNSEFLLEKRILQ; LQNSEFLLEKRILQS; QNSEFLLEKRILQSG; NSEFLLEKRILQSGM; SEFLLEKRILQSGMT; EFLLEKRILQSGMTL; FLLEKRILQSGMTLL; LLEKRILQSGMTLLL; LEKRILQSGMTLLLL; EKRILQSGMTLLLLL; KRILQSGMTLLLLLI; RILQSGMTLLLLLIW; ILQSGMTLLLLLIWF; LQSGMTLLLLLIWFR; QSGMTLLLLLIWFRP; SGMTLLLLLIWFRPV; GMTLLLLLIWFRPVA; MTLLLLLIWFRPVAD; TLLLLLIWFRPVADF; LLLLLIWFRPVADFA; LLLLIWFRPVADFAT; LLLIWFRPVADFATD; LLIWFRPVADFATDI; LIWFRPVADFATDIQ; IWFRPVADFATDIQS; WFRPVADFATDIQSR; FRPVADFATDIQSRI; RPVADFATDIQSRIV; PVADFATDIQSRIVE; VADFATDIQSRIVEW; ADFATDIQSRIVEWK; DFATDIQSRIVEWKE; FATDIQSRIVEWKER; ATDIQSRIVEWKERL; TDIQSRIVEWKERLD; DIQSRIVEWKERLDS; IQSRIVEWKERLDSE; QSRIVEWKERLDSEI; SRIVEWKERLDSEIS; RIVEWKERLDSEISM; IVEWKERLDSEISMY; VEWKERLDSEISMYT; EWKERLDSEISMYTF; WKERLDSEISMYTFS; KERLDSEISMYTFSR; ERLDSEISMYTFSRM; RLDSEISMYTFSRMK; LDSEISMYTFSRMKY; DSEISMYTFSRMKYN; SEISMYTFSRMKYNI; EISMYTFSRMKYNIC; ISMYTFSRMKYNICM; SMYTFSRMKYNICMG; MYTFSRMKYNICMGK; YTFSRMKYNICMGKC; TFSRMKYNICMGKCI; FSRMKYNICMGKCIL; SRMKYNICMGKCILD; RMKYNICMGKCILDI; MKYNICMGKCILDIT; KYNICMGKCILDITR; YNICMGKCILDITRE; NICMGKCILDITREE; ICMGKCILDITREED; CMGKCILDITREEDS; MGKCILDITREEDSE; GKCILDITREEDSET; KCILDITREEDSETE; CILDITREEDSETED; ILDITREEDSETEDS; LDITREEDSETEDSG; DITREEDSETEDSGH; ITREEDSETEDSGHG; TREEDSETEDSGHGS; REEDSETEDSGHGSS; EEDSETEDSGHGSST; EDSETEDSGHGSSTE; DSETEDSGHGSSTES; SETEDSGHGSSTESQ; ETEDSGHGSSTESQS; TEDSGHGSSTESQSQ; EDSGHGSSTESQSQC; DSGHGSSTESQSQCS; SGHGSSTESQSQCSS; GHGSSTESQSQCSSQ; HGSSTESQSQCSSQV; GSSTESQSQCSSQVS; SSTESQSQCSSQVSD; STESQSQCSSQVSDT; TESQSQCSSQVSDTS; ESQSQCSSQVSDTSA; SQSQCSSQVSDTSAP; QSQCSSQVSDTSAPA; SQCSSQVSDTSAPAE; QCSSQVSDTSAPAED; CSSQVSDTSAPAEDS; SSQVSDTSAPAEDSQ; SQVSDTSAPAEDSQR; QVSDTSAPAEDSQRS; VSDTSAPAEDSQRSD; SDTSAPAEDSQRSDP; DTSAPAEDSQRSDPH; TSAPAEDSQRSDPHS; SAPAEDSQRSDPHSQ; APAEDSQRSDPHSQE; PAEDSQRSDPHSQEL; AEDSQRSDPHSQELH; EDSQRSDPHSQELHL; DSQRSDPHSQELHLC; SQRSDPHSQELHLCK; QRSDPHSQELHLCKG; RSDPHSQELHLCKGF; SDPHSQELHLCKGFQ; DPHSQELHLCKGFQC; PHSQELHLCKGFQCF; HSQELHLCKGFQCFK; SQELHLCKGFQCFKR; QELHLCKGFQCFKRP; ELHLCKGFQCFKRPK; LHLCKGFQCFKRPKT; HLCKGFQCFKRPKTP; LCKGFQCFKRPKTPP; CKGFQCFKRPKTPPP; KGFQCFKRPKTPPPK; MYMYNKSTCLKHFGL; YMYNKSTCLKHFGLQ; MYNKSTCLKHFGLQL; YNKSTCLKHFGLQLS; NKSTCLKHFGLQLSL; KSTCLKHFGLQLSLF; STCLKHFGLQLSLFV; TCLKHFGLQLSLFVN; CLKHFGLQLSLFVNI; LKHFGLQLSLFVNIS; KHFGLQLSLFVNISY; HFGLQLSLFVNISYH; FGLQLSLFVNISYHI; GLQLSLFVNISYHIW; LQLSLFVNISYHIWV; QLSLFVNISYHIWVP; LSLFVNISYHIWVPW; SLFVNISYHIWVPWK; LFVNISYHIWVPWKS; FVNISYHIWVPWKSF; VNISYHIWVPWKSFC; NISYHIWVPWKSFCA; ISYHIWVPWKSFCAI; SYHIWVPWKSFCAIK; YHIWVPWKSFCAIKH; HIWVPWKSFCAIKHP; IWVPWKSFCAIKHPN; WVPWKSFCAIKHPNL; VPWKSFCAIKHPNLF; PWKSFCAIKHPNLFY; WKSFCAIKHPNLFYL; KSFCAIKHPNLFYLG; SFCAIKHPNLFYLGF; FCAIKHPNLFYLGFH; CAIKHPNLFYLGFHT; AIKHPNLFYLGFHTI; IKHPNLFYLGFHTIH; KHPNLFYLGFHTIHR; HPNLFYLGFHTIHRL; PNLFYLGFHTIHRLP; NLFYLGFHTIHRLPI; LFYLGFHTIHRLPIH; FYLGFHTIHRLPIHS; YLGFHTIHRLPIHSL; LGFHTIHRLPIHSLG; GFHTIHRLPIHSLGS; FHTIHRLPIHSLGSP; HTIHRLPIHSLGSPV; TIHRLPIHSLGSPVY; IHRLPIHSLGSPVYK; HRLPIHSLGSPVYKV; RLPIHSLGSPVYKVT; QKGNWVRILYRSFSQ; KGNWVRILYRSFSQA; GNWVRILYRSFSQAD; NWVRILYRSFSQADL; WVRILYRSFSQADLK; VRILYRSFSQADLKI; RILYRSFSQADLKIS; ILYRSFSQADLKISC; LYRSFSQADLKISCK; YRSFSQADLKISCKA; RSFSQADLKISCKAS; SFSQADLKISCKASP; FSQADLKISCKASPL; SQADLKISCKASPLL; QADLKISCKASPLLC; ADLKISCKASPLLCS; DLKISCKASPLLCSR; LKISCKASPLLCSRA; KISCKASPLLCSRAV; ISCKASPLLCSRAVS; SCKASPLLCSRAVSK; CKASPLLCSRAVSKQ; KASPLLCSRAVSKQA; ASPLLCSRAVSKQAT; SPLLCSRAVSKQATN; PLLCSRAVSKQATNI; LLCSRAVSKQATNIS; LCSRAVSKQATNISS; NIQAISFTKRPHTLF; IQAISFTKRPHTLFI; QHCGSCVGHMKYWGN; HCGSCVGHMKYWGNI; CGSCVGHMKYWGNIF; GSCVGHMKYWGNIFP; SCVGHMKYWGNIFPS; CVGHMKYWGNIFPSC; VGHMKYWGNIFPSCE; GHMKYWGNIFPSCES; HMKYWGNIFPSCESP; MKYWGNIFPSCESPK; KYWGNIFPSCESPKI; YWGNIFPSCESPKIP; WGNIFPSCESPKIPS; GNIFPSCESPKIPSI; NIFPSCESPKIPSIF; IFPSCESPKIPSIFI; FPSCESPKIPSIFIS; PSCESPKIPSIFIST; SCESPKIPSIFISTG; CESPKIPSIFISTGI; ESPKIPSIFISTGIR; SPKIPSIFISTGIRY; PKIPSIFISTGIRYP; KIPSIFISTGIRYPA; IPSIFISTGIRYPAL; PSIFISTGIRYPALN; SIFISTGIRYPALNW; IFISTGIRYPALNWI; FISTGIRYPALNWIS; ISTGIRYPALNWISI; STGIRYPALNWISIV; TGIRYPALNWISIVF; GIRYPALNWISIVFV; IRYPALNWISIVFVQ; RYPALNWISIVFVQI; YPALNWISIVFVQIG; PALNWISIVFVQIGL; ALNWISIVFVQIGLM; LNWISIVFVQIGLMV; NWISIVFVQIGLMVS; WISIVFVQIGLMVSI; ISIVFVQIGLMVSIH; SIVFVQIGLMVSIHY; IVFVQIGLMVSIHYL; VFVQIGLMVSIHYLG; FVQIGLMVSIHYLGL; VQIGLMVSIHYLGLG; QIGLMVSIHYLGLGC; IGLMVSIHYLGLGCW; GLMVSIHYLGLGCWV; LMVSIHYLGLGCWVF; MVSIHYLGLGCWVFR; VSIHYLGLGCWVFRG; SIHYLGLGCWVFRGY; IHYLGLGCWVFRGYS; HYLGLGCWVFRGYST; YLGLGCWVFRGYSTI; LGLGCWVFRGYSTIR; GLGCWVFRGYSTIRV; LGCWVFRGYSTIRVL; HSLHFQGFSTYSKEV; SLHFQGFSTYSKEVE; LHFQGFSTYSKEVEI; HFQGFSTYSKEVEIT; FQGFSTYSKEVEITA; QGFSTYSKEVEITAL; GFSTYSKEVEITALN; FSTYSKEVEITALNR; STYSKEVEITALNRF; TYSKEVEITALNRFS; YSKEVEITALNRFSS; SKEVEITALNRFSST; KEVEITALNRFSSTM; EVEITALNRFSSTML; VEITALNRFSSTMLM; EITALNRFSSTMLMH; ITALNRFSSTMLMHF; TALNRFSSTMLMHFL; PCMKVKHASYSNNLC; CMKVKHASYSNNLCL; MKVKHASYSNNLCLY; KVKHASYSNNLCLYS; VKHASYSNNLCLYSY; KHASYSNNLCLYSYS; HASYSNNLCLYSYSL; ASYSNNLCLYSYSLP; SYSNNLCLYSYSLPH; YSNNLCLYSYSLPHQ; IGEGNSCCAVTGKHF; GEGNSCCAVTGKHFS; EGNSCCAVTGKHFSL; GNSCCAVTGKHFSLW; NSCCAVTGKHFSLWA; SCCAVTGKHFSLWAI; CCAVTGKHFSLWAIT; CAVTGKHFSLWAITA; AVTGKHFSLWAITAK; VTGKHFSLWAITAKV; TGKHFSLWAITAKVI; GKHFSLWAITAKVIF; KHFSLWAITAKVIFS; HFSLWAITAKVIFST; TKAPKVFIWIPHFWV; EAFYLCNSIYPSFNF; FWHLHGFLWLFGSCP; WHLHGFLWLFGSCPW; HLHGFLWLFGSCPWT; LHGFLWLFGSCPWTL; HGFLWLFGSCPWTLS; GFLWLFGSCPWTLSF; FLWLFGSCPWTLSFS; LWLFGSCPWTLSFSF; WLFGSCPWTLSFSFG; LFGSCPWTLSFSFGW; FGSCPWTLSFSFGWG; GSCPWTLSFSFGWGH; SCPWTLSFSFGWGHL; CPWTLSFSFGWGHLH; PWTLSFSFGWGHLHM; WTLSFSFGWGHLHML; TLSFSFGWGHLHMLQ; LSFSFGWGHLHMLQE; SFSFGWGHLHMLQEQ; FSFGWGHLHMLQEQV; SFGWGHLHMLQEQVL; FGWGHLHMLQEQVLQ; GWGHLHMLQEQVLQS; WGHLHMLQEQVLQSR; GHLHMLQEQVLQSRT; HLHMLQEQVLQSRTG; LHMLQEQVLQSRTGL; HMLQEQVLQSRTGLE; MLQEQVLQSRTGLEV; LQEQVLQSRTGLEVK; QEQVLQSRTGLEVKA; EQVLQSRTGLEVKAT; QVLQSRTGLEVKATS; VLQSRTGLEVKATSI; LQSRTGLEVKATSIE; QSRTGLEVKATSIEE; SRTGLEVKATSIEEQ; RTGLEVKATSIEEQF; TGLEVKATSIEEQFF; GLEVKATSIEEQFFD; TLLNVHFVDFLSPFF; LLNVHFVDFLSPFFV; LLLYCQHHLYYKYGQ; LLYCQHHLYYKYGQN; LYCQHHLYYKYGQNV; YCQHHLYYKYGQNVH; CQHHLYYKYGQNVHG; QHHLYYKYGQNVHGY; HHLYYKYGQNVHGYL; HLYYKYGQNVHGYLP; LYYKYGQNVHGYLPF; YYKYGQNVHGYLPFQ; YKYGQNVHGYLPFQL; KYGQNVHGYLPFQLL; YGQNVHGYLPFQLLV; GKDQNNIVEYNYKSL; QKYLHQETEYHSTHL; KYLHQETEYHSTHLG; TIPKPCLIADRGLQW; IPKPCLIADRGLQWK; PKPCLIADRGLQWKL; KPCLIADRGLQWKLC; PCLIADRGLQWKLCD; CLIADRGLQWKLCDP; LIADRGLQWKLCDPN; IADRGLQWKLCDPNH; ADRGLQWKLCDPNHQ; DRGLQWKLCDPNHQR; RGLQWKLCDPNHQRT; GLQWKLCDPNHQRTY; LQWKLCDPNHQRTYT; QWKLCDPNHQRTYTL; WKLCDPNHQRTYTLL; KLCDPNHQRTYTLLE; LCDPNHQRTYTLLEL; CDPNHQRTYTLLELR; DPNHQRTYTLLELRN; PQEHQQLQHMFEELG; QEHQQLQHMFEELGL; QQQPPQQQFQPLKIL; QQPPQQQFQPLKILW; QPPQQQFQPLKILWQ; PPQQQFQPLKILWQQ; PQQQFQPLKILWQQQ; QQQFQPLKILWQQQP; QQFQPLKILWQQQPQ; QFQPLKILWQQQPQI; FQPLKILWQQQPQIH; QPLKILWQQQPQIHW; PLKILWQQQPQIHWQ; LKILWQQQPQIHWQL; KILWQQQPQIHWQLG; ILWQQQPQIHWQLGP; LWQQQPQIHWQLGPP; WQQQPQIHWQLGPPK; QQQPQIHWQLGPPKV; QQPQIHWQLGPPKVL; QPQIHWQLGPPKVLE; PQIHWQLGPPKVLEQ; QIHWQLGPPKVLEQH; IHWQLGPPKVLEQHP; TWKYKKKGITYLGVF; WKYKKKGITYLGVFY; KYKKKGITYLGVFYR; YKKKGITYLGVFYRV; KKKGITYLGVFYRVF; KKGITYLGVFYRVFY; KGITYLGVFYRVFYS; GITYLGVFYRVFYSR; SSGTFVFPVYTVFTS; SGTFVFPVYTVFTST; GTFVFPVYTVFTSTK; TFVFPVYTVFTSTKF; FVFPVYTVFTSTKFQ; VFPVYTVFTSTKFQQ; FPVYTVFTSTKFQQK; PVYTVFTSTKFQQKL; NKNKNPLSSFFCSSP; KNKNPLSSFFCSSPG; NKNPLSSFFCSSPGF; KNPLSSFFCSSPGFT; NPLSSFFCSSPGFTN; PLSSFFCSSPGFTNF; LSSFFCSSPGFTNFH; LGTRPRFLGSQNMSV; GTRPRFLGSQNMSVM; TRPRFLGSQNMSVMH; RPRFLGSQNMSVMHF; PRFLGSQNMSVMHFP; RFLGSQNMSVMHFPS; AAPPCESCTFLPEVM; APPCESCTFLPEVMV; PPCESCTFLPEVMVW; PCESCTFLPEVMVWL; CESCTFLPEVMVWLH; ESCTFLPEVMVWLHS; SCTFLPEVMVWLHSP; CTFLPEVMVWLHSPV; TFLPEVMVWLHSPVS; FLPEVMVWLHSPVSH; LPEVMVWLHSPVSHA; PEVMVWLHSPVSHAL; EVMVWLHSPVSHALS; VMVWLHSPVSHALSF; MVWLHSPVSHALSFL; VWLHSPVSHALSFLR; WLHSPVSHALSFLRS; LHSPVSHALSFLRSW; HSPVSHALSFLRSWF; SPVSHALSFLRSWFG; PVSHALSFLRSWFGC; VSHALSFLRSWFGCI; SHALSFLRSWFGCIP; HALSFLRSWFGCIPW; ALSFLRSWFGCIPWV; LSFLRSWFGCIPWVS; SFLRSWFGCIPWVSS; FLRSWFGCIPWVSSS; LRSWFGCIPWVSSSS; RSWFGCIPWVSSSSL; SWFGCIPWVSSSSLW; WFGCIPWVSSSSLWP; FGCIPWVSSSSLWPF; GCIPWVSSSSLWPFF; CIPWVSSSSLWPFFL; YIRGRGRLCLHPFSQ; IRGRGRLCLHPFSQV; RGRGRLCLHPFSQVV; GRGRLCLHPFSQVVR; RGRLCLHPFSQVVRV; GRLCLHPFSQVVRVW; RLCLHPFSQVVRVWR; LCLHPFSQVVRVWRL; CLHPFSQVVRVWRLF; LHPFSQVVRVWRLFL; HPFSQVVRVWRLFLR; PFSQVVRVWRLFLRP; FSQVVRVWRLFLRPS; SQVVRVWRLFLRPSK; QVVRVWRLFLRPSKT; VVRVWRLFLRPSKTI; VRVWRLFLRPSKTIW; RVWRLFLRPSKTIWG; VWRLFLRPSKTIWGN; WRLFLRPSKTIWGNP; RLFLRPSKTIWGNPY; LFLRPSKTIWGNPYS; FLRPSKTIWGNPYSF; LRPSKTIWGNPYSFA; RPSKTIWGNPYSFAI; PSKTIWGNPYSFAIF; SKTIWGNPYSFAIFA; KTIWGNPYSFAIFAK 16 mers: KSCLGKSSLNEKSLFK; SCLGKSSLNEKSLFKE; CLGKSSLNEKSLFKEV; FSSLPRYPVLQGMAYL; SSLPRYPVLQGMAYLF; SLPRYPVLQGMAYLFQ; LPRYPVLQGMAYLFQK; PRYPVLQGMAYLFQKA; RYPVLQGMAYLFQKAF; YPVLQGMAYLFQKAFC; PVLQGMAYLFQKAFCA; VLQGMAYLFQKAFCAL; LQGMAYLFQKAFCALP; QGMAYLFQKAFCALPL; GMAYLFQKAFCALPLH; MAYLFQKAFCALPLHA; AYLFQKAFCALPLHAM; YLFQKAFCALPLHAMS; LFQKAFCALPLHAMSA; KIFKKRALGLDRLLLH; RNSAMVGPNNWRNSLQ; NSAMVGPNNWRNSLQR; SAMVGPNNWRNSLQRS; AMVGPNNWRNSLQRSK; MVGPNNWRNSLQRSKA; VGPNNWRNSLQRSKAL; GPNNWRNSLQRSKALR; VPTYGTEEWESWWSSF; PTYGTEEWESWWSSFN; TYGTEEWESWWSSFNE; YGTEEWESWWSSFNEK; GTEEWESWWSSFNEKW; TEEWESWWSSFNEKWD; EEWESWWSSFNEKWDE; EWESWWSSFNEKWDED; WESWWSSFNEKWDEDL; ESWWSSFNEKWDEDLF; SWWSSFNEKWDEDLFC; WWSSFNEKWDEDLFCH; WSSFNEKWDEDLFCHE; SSFNEKWDEDLFCHED; SFNEKWDEDLFCHEDM; FNEKWDEDLFCHEDMF; NEKWDEDLFCHEDMFA; EKWDEDLFCHEDMFAS; KWDEDLFCHEDMFASD; WDEDLFCHEDMFASDE; DEDLFCHEDMFASDEE; EDLFCHEDMFASDEEA; DLFCHEDMFASDEEAT; LFCHEDMFASDEEATA; FCHEDMFASDEEATAD; CHEDMFASDEEATADS; HEDMFASDEEATADSQ; EDMFASDEEATADSQH; DMFASDEEATADSQHS; MFASDEEATADSQHST; FASDEEATADSQHSTP; ASDEEATADSQHSTPP; SDEEATADSQHSTPPK; DEEATADSQHSTPPKK; EEATADSQHSTPPKKK; EATADSQHSTPPKKKR; ATADSQHSTPPKKKRK; TADSQHSTPPKKKRKV; ADSQHSTPPKKKRKVE; DSQHSTPPKKKRKVED; SQHSTPPKKKRKVEDP; QHSTPPKKKRKVEDPK; HSTPPKKKRKVEDPKD; STPPKKKRKVEDPKDF; TPPKKKRKVEDPKDFP; PPKKKRKVEDPKDFPS; PKKKRKVEDPKDFPSD; KKKRKVEDPKDFPSDL; KKRKVEDPKDFPSDLH; KRKVEDPKDFPSDLHQ; RKVEDPKDFPSDLHQF; KVEDPKDFPSDLHQFL; VEDPKDFPSDLHQFLS; EDPKDFPSDLHQFLSQ; DPKDFPSDLHQFLSQA; PKDFPSDLHQFLSQAV; KDFPSDLHQFLSQAVF; DFPSDLHQFLSQAVFS; FPSDLHQFLSQAVFSN; PSDLHQFLSQAVFSNR; SDLHQFLSQAVFSNRT; DLHQFLSQAVFSNRTL; LHQFLSQAVFSNRTLA; HQFLSQAVFSNRTLAC; QFLSQAVFSNRTLACF; FLSQAVFSNRTLACFA; LSQAVFSNRTLACFAV; SQAVFSNRTLACFAVY; QAVFSNRTLACFAVYT; AVFSNRTLACFAVYTT; VFSNRTLACFAVYTTK; FSNRTLACFAVYTTKE; SNRTLACFAVYTTKEK; NRTLACFAVYTTKEKA; RTLACFAVYTTKEKAQ; TLACFAVYTTKEKAQI; LACFAVYTTKEKAQIL; ACFAVYTTKEKAQILY; CFAVYTTKEKAQILYK; FAVYTTKEKAQILYKK; AVYTTKEKAQILYKKL; VYTTKEKAQILYKKLM; YTTKEKAQILYKKLME; TTKEKAQILYKKLMEK; TKEKAQILYKKLMEKY; KEKAQILYKKLMEKYS; EKAQILYKKLMEKYSV; KAQILYKKLMEKYSVT; AQILYKKLMEKYSVTF; QILYKKLMEKYSVTFI; ILYKKLMEKYSVTFIS; LYKKLMEKYSVTFISR; YKKLMEKYSVTFISRH; KKLMEKYSVTFISRHM; KLMEKYSVTFISRHMC; LMEKYSVTFISRHMCA; MEKYSVTFISRHMCAG; EKYSVTFISRHMCAGH; KYSVTFISRHMCAGHN; YSVTFISRHMCAGHNI; SVTFISRHMCAGHNII; VTFISRHMCAGHNIIF; TFISRHMCAGHNIIFF; FISRHMCAGHNIIFFL; ISRHMCAGHNIIFFLT; SRHMCAGHNIIFFLTP; RHMCAGHNIIFFLTPH; HMCAGHNIIFFLTPHR; MCAGHNIIFFLTPHRH; CAGHNIIFFLTPHRHR; AGHNIIFFLTPHRHRV; GHNIIFFLTPHRHRVS; HNIIFFLTPHRHRVSA; NIIFFLTPHRHRVSAI; IIFFLTPHRHRVSAIN; IFFLTPHRHRVSAINN; FFLTPHRHRVSAINNF; FLTPHRHRVSAINNFC; LTPHRHRVSAINNFCQ; TPHRHRVSAINNFCQK; PHRHRVSAINNFCQKL; HRHRVSAINNFCQKLC; RHRVSAINNFCQKLCT; HRVSAINNFCQKLCTF; RVSAINNFCQKLCTFS; VSAINNFCQKLCTFSF; SAINNFCQKLCTFSFL; AINNFCQKLCTFSFLI; INNFCQKLCTFSFLIC; NNFCQKLCTFSFLICK; NFCQKLCTFSFLICKG; FCQKLCTFSFLICKGV; CQKLCTFSFLICKGVN; QKLCTFSFLICKGVNK; KLCTFSFLICKGVNKE; LCTFSFLICKGVNKEY; CTFSFLICKGVNKEYL; TFSFLICKGVNKEYLL; FSFLICKGVNKEYLLY; SFLICKGVNKEYLLYS; FLICKGVNKEYLLYSA; LICKGVNKEYLLYSAL; ICKGVNKEYLLYSALT; CKGVNKEYLLYSALTR; KGVNKEYLLYSALTRD; GVNKEYLLYSALTRDP; VNKEYLLYSALTRDPY; NKEYLLYSALTRDPYH; KEYLLYSALTRDPYHT; EYLLYSALTRDPYHTI; YLLYSALTRDPYHTIE; LLYSALTRDPYHTIEE; LYSALTRDPYHTIEES; YSALTRDPYHTIEESI; SALTRDPYHTIEESIQ; ALTRDPYHTIEESIQG; LTRDPYHTIEESIQGG; TRDPYHTIEESIQGGL; RDPYHTIEESIQGGLK; DPYHTIEESIQGGLKE; PYHTIEESIQGGLKEH; YHTIEESIQGGLKEHD; HTIEESIQGGLKEHDF; TIEESIQGGLKEHDFS; IEESIQGGLKEHDFSP; EESIQGGLKEHDFSPE; ESIQGGLKEHDFSPEE; SIQGGLKEHDFSPEEP; IQGGLKEHDFSPEEPE; QGGLKEHDFSPEEPEE; GGLKEHDFSPEEPEET; GLKEHDFSPEEPEETK; LKEHDFSPEEPEETKQ; KEHDFSPEEPEETKQV; EHDFSPEEPEETKQVS; HDFSPEEPEETKQVSW; DFSPEEPEETKQVSWK; FSPEEPEETKQVSWKL; SPEEPEETKQVSWKLI; PEEPEETKQVSWKLIT; EEPEETKQVSWKLITE; EPEETKQVSWKLITEY; PEETKQVSWKLITEYA; EETKQVSWKLITEYAV; ETKQVSWKLITEYAVE; TKQVSWKLITEYAVET; KQVSWKLITEYAVETK; QVSWKLITEYAVETKC; VSWKLITEYAVETKCE; SWKLITEYAVETKCED; WKLITEYAVETKCEDV; KLITEYAVETKCEDVF; LITEYAVETKCEDVFL; ITEYAVETKCEDVFLL; TEYAVETKCEDVFLLL; EYAVETKCEDVFLLLG; YAVETKCEDVFLLLGM; AVETKCEDVFLLLGMY; VETKCEDVFLLLGMYL; ETKCEDVFLLLGMYLE; TKCEDVFLLLGMYLEF; KCEDVFLLLGMYLEFQ; CEDVFLLLGMYLEFQY; EDVFLLLGMYLEFQYN; DVFLLLGMYLEFQYNV; VFLLLGMYLEFQYNVE; FLLLGMYLEFQYNVEE; LLLGMYLEFQYNVEEC; LLGMYLEFQYNVEECK; LGMYLEFQYNVEECKK; GMYLEFQYNVEECKKC; MYLEFQYNVEECKKCQ; YLEFQYNVEECKKCQK; LEFQYNVEECKKCQKK; EFQYNVEECKKCQKKD; FQYNVEECKKCQKKDQ; QYNVEECKKCQKKDQP; YNVEECKKCQKKDQPY; NVEECKKCQKKDQPYH; VEECKKCQKKDQPYHF; EECKKCQKKDQPYHFK; ECKKCQKKDQPYHFKY; CKKCQKKDQPYHFKYH; KKCQKKDQPYHFKYHE; KCQKKDQPYHFKYHEK; CQKKDQPYHFKYHEKH; QKKDQPYHFKYHEKHF; KKDQPYHFKYHEKHFA; KDQPYHFKYHEKHFAN; DQPYHFKYHEKHFANA; QPYHFKYHEKHFANAI; PYHFKYHEKHFANAII; YHFKYHEKHFANAIIF; HFKYHEKHFANAIIFA; FKYHEKHFANAIIFAE; KYHEKHFANAIIFAES; YHEKHFANAIIFAESK; HEKHFANAIIFAESKN; EKHFANAIIFAESKNQ; KHFANAIIFAESKNQK; HFANAIIFAESKNQKS; FANAIIFAESKNQKSI; ANAIIFAESKNQKSIC; NAIIFAESKNQKSICQ; AIIFAESKNQKSICQQ; IIFAESKNQKSICQQA; IFAESKNQKSICQQAV; FAESKNQKSICQQAVD; AESKNQKSICQQAVDT; ESKNQKSICQQAVDTV; SKNQKSICQQAVDTVL; KNQKSICQQAVDTVLA; NQKSICQQAVDTVLAK; QKSICQQAVDTVLAKK; KSICQQAVDTVLAKKR; SICQQAVDTVLAKKRV; ICQQAVDTVLAKKRVD; CQQAVDTVLAKKRVDT; QQAVDTVLAKKRVDTL; QAVDTVLAKKRVDTLH; AVDTVLAKKRVDTLHM; VDTVLAKKRVDTLHMT; DTVLAKKRVDTLHMTR; TVLAKKRVDTLHMTRE; VLAKKRVDTLHMTREE; LAKKRVDTLHMTREEM; AKKRVDTLHMTREEML; KKRVDTLHMTREEMLT; KRVDTLHMTREEMLTE; RVDTLHMTREEMLTER; VDTLHMTREEMLTERF; DTLHMTREEMLTERFN; TLHMTREEMLTERFNH; LHMTREEMLTERFNHI; HMTREEMLTERFNHIL; MTREEMLTERFNHILD; TREEMLTERFNHILDK; REEMLTERFNHILDKM; EEMLTERFNHILDKMD; EMLTERFNHILDKMDL; MLTERFNHILDKMDLI; LTERFNHILDKMDLIF; TERFNHILDKMDLIFG; ERFNHILDKMDLIFGA; RFNHILDKMDLIFGAH; FNHILDKMDLIFGAHG; NHILDKMDLIFGAHGN; HILDKMDLIFGAHGNA; ILDKMDLIFGAHGNAV; LDKMDLIFGAHGNAVL; DKMDLIFGAHGNAVLE; KMDLIFGAHGNAVLEQ; MDLIFGAHGNAVLEQY; DLIFGAHGNAVLEQYM; LIFGAHGNAVLEQYMA; IFGAHGNAVLEQYMAG; FGAHGNAVLEQYMAGV; GAHGNAVLEQYMAGVA; AHGNAVLEQYMAGVAW; HGNAVLEQYMAGVAWL; GNAVLEQYMAGVAWLH; NAVLEQYMAGVAWLHC; AVLEQYMAGVAWLHCL; VLEQYMAGVAWLHCLL; LEQYMAGVAWLHCLLP; EQYMAGVAWLHCLLPK; QYMAGVAWLHCLLPKM; YMAGVAWLHCLLPKMD; MAGVAWLHCLLPKMDS; AGVAWLHCLLPKMDSV; GVAWLHCLLPKMDSVI; VAWLHCLLPKMDSVIF; AWLHCLLPKMDSVIFD; WLHCLLPKMDSVIFDF; LHCLLPKMDSVIFDFL; HCLLPKMDSVIFDFLH; CLLPKMDSVIFDFLHC; LLPKMDSVIFDFLHCI; LPKMDSVIFDFLHCIV; PKMDSVIFDFLHCIVF; KMDSVIFDFLHCIVFN; MDSVIFDFLHCIVFNV; DSVIFDFLHCIVFNVP; SVIFDFLHCIVFNVPK; VIFDFLHCIVFNVPKR; IFDFLHCIVFNVPKRR; FDFLHCIVFNVPKRRY; DFLHCIVFNVPKRRYW; FLHCIVFNVPKRRYWL; LHCIVFNVPKRRYWLF; HCIVFNVPKRRYWLFK; CIVFNVPKRRYWLFKG; IVFNVPKRRYWLFKGP; VFNVPKRRYWLFKGPI; FNVPKRRYWLFKGPID; NVPKRRYWLFKGPIDS; VPKRRYWLFKGPIDSG; PKRRYWLFKGPIDSGK; KRRYWLFKGPIDSGKT; RRYWLFKGPIDSGKTT; RYWLFKGPIDSGKTTL; YWLFKGPIDSGKTTLA; WLFKGPIDSGKTTLAA; LFKGPIDSGKTTLAAG; FKGPIDSGKTTLAAGL; KGPIDSGKTTLAAGLL; GPIDSGKTTLAAGLLD; PIDSGKTTLAAGLLDL; IDSGKTTLAAGLLDLC; DSGKTTLAAGLLDLCG; SGKTTLAAGLLDLCGG; GKTTLAAGLLDLCGGK; KTTLAAGLLDLCGGKA; TTLAAGLLDLCGGKAL; TLAAGLLDLCGGKALN; LAAGLLDLCGGKALNV; AAGLLDLCGGKALNVN; AGLLDLCGGKALNVNL; GLLDLCGGKALNVNLP; LLDLCGGKALNVNLPM; LDLCGGKALNVNLPME; DLCGGKALNVNLPMER; LCGGKALNVNLPMERL; CGGKALNVNLPMERLT; GGKALNVNLPMERLTF; GKALNVNLPMERLTFE; KALNVNLPMERLTFEL; ALNVNLPMERLTFELG; LNVNLPMERLTFELGV; NVNLPMERLTFELGVA; VNLPMERLTFELGVAI; NLPMERLTFELGVAID; LPMERLTFELGVAIDQ; PMERLTFELGVAIDQY; MERLTFELGVAIDQYM; ERLTFELGVAIDQYMV; RLTFELGVAIDQYMVV; LTFELGVAIDQYMVVF; TFELGVAIDQYMVVFE; FELGVAIDQYMVVFED; ELGVAIDQYMVVFEDV; LGVAIDQYMVVFEDVK; GVAIDQYMVVFEDVKG; VAIDQYMVVFEDVKGT; AIDQYMVVFEDVKGTG; IDQYMVVFEDVKGTGA; DQYMVVFEDVKGTGAE; QYMVVFEDVKGTGAES; YMVVFEDVKGTGAESK; MVVFEDVKGTGAESKD; VVFEDVKGTGAESKDL; VFEDVKGTGAESKDLP; FEDVKGTGAESKDLPS; EDVKGTGAESKDLPSG; DVKGTGAESKDLPSGH; VKGTGAESKDLPSGHG; KGTGAESKDLPSGHGI; GTGAESKDLPSGHGIN; TGAESKDLPSGHGINN; GAESKDLPSGHGINNL; AESKDLPSGHGINNLD; ESKDLPSGHGINNLDS; SKDLPSGHGINNLDSL; KDLPSGHGINNLDSLR; DLPSGHGINNLDSLRD; LPSGHGINNLDSLRDY; PSGHGINNLDSLRDYL; SGHGINNLDSLRDYLD; GHGINNLDSLRDYLDG; HGINNLDSLRDYLDGS; GINNLDSLRDYLDGSV; INNLDSLRDYLDGSVK; NNLDSLRDYLDGSVKV; NLDSLRDYLDGSVKVN; LDSLRDYLDGSVKVNL; DSLRDYLDGSVKVNLE; SLRDYLDGSVKVNLEK; LRDYLDGSVKVNLEKK; RDYLDGSVKVNLEKKH; DYLDGSVKVNLEKKHL; YLDGSVKVNLEKKHLN; LDGSVKVNLEKKHLNK; DGSVKVNLEKKHLNKR; GSVKVNLEKKHLNKRT; SVKVNLEKKHLNKRTQ; VKVNLEKKHLNKRTQI; KVNLEKKHLNKRTQIF; VNLEKKHLNKRTQIFP; NLEKKHLNKRTQIFPP; LEKKHLNKRTQIFPPG; EKKHLNKRTQIFPPGL; KKHLNKRTQIFPPGLV; KHLNKRTQIFPPGLVT; HLNKRTQIFPPGLVTM; LNKRTQIFPPGLVTMN; NKRTQIFPPGLVTMNE; KRTQIFPPGLVTMNEY; RTQIFPPGLVTMNEYP; TQIFPPGLVTMNEYPV; QIFPPGLVTMNEYPVP; IFPPGLVTMNEYPVPK; FPPGLVTMNEYPVPKT; PPGLVTMNEYPVPKTL; PGLVTMNEYPVPKTLQ; GLVTMNEYPVPKTLQA; LVTMNEYPVPKTLQAR; VTMNEYPVPKTLQARF; TMNEYPVPKTLQARFV; MNEYPVPKTLQARFVR; NEYPVPKTLQARFVRQ; EYPVPKTLQARFVRQI; YPVPKTLQARFVRQID; PVPKTLQARFVRQIDF; VPKTLQARFVRQIDFR; PKTLQARFVRQIDFRP; KTLQARFVRQIDFRPK; TLQARFVRQIDFRPKI; LQARFVRQIDFRPKIY; QARFVRQIDFRPKIYL; ARFVRQIDFRPKIYLR; RFVRQIDFRPKIYLRK; FVRQIDFRPKIYLRKS; VRQIDFRPKIYLRKSL; RQIDFRPKIYLRKSLQ; QIDFRPKIYLRKSLQN; IDFRPKIYLRKSLQNS; DFRPKIYLRKSLQNSE; FRPKIYLRKSLQNSEF; RPKIYLRKSLQNSEFL; PKIYLRKSLQNSEFLL; KIYLRKSLQNSEFLLE; IYLRKSLQNSEFLLEK; YLRKSLQNSEFLLEKR; LRKSLQNSEFLLEKRI; RKSLQNSEFLLEKRIL; KSLQNSEFLLEKRILQ; SLQNSEFLLEKRILQS; LQNSEFLLEKRILQSG; QNSEFLLEKRILQSGM; NSEFLLEKRILQSGMT; SEFLLEKRILQSGMTL; EFLLEKRILQSGMTLL; FLLEKRILQSGMTLLL; LLEKRILQSGMTLLLL; LEKRILQSGMTLLLLL; EKRILQSGMTLLLLLI; KRILQSGMTLLLLLIW; RILQSGMTLLLLLIWF; ILQSGMTLLLLLIWFR; LQSGMTLLLLLIWFRP; QSGMTLLLLLIWFRPV; SGMTLLLLLIWFRPVA; GMTLLLLLIWFRPVAD; MTLLLLLIWFRPVADF; TLLLLLIWFRPVADFA; LLLLLIWFRPVADFAT; LLLLIWFRPVADFATD; LLLIWFRPVADFATDI; LLIWFRPVADFATDIQ; LIWFRPVADFATDIQS; IWFRPVADFATDIQSR; WFRPVADFATDIQSRI; FRPVADFATDIQSRIV; RPVADFATDIQSRIVE; PVADFATDIQSRIVEW; VADFATDIQSRIVEWK; ADFATDIQSRIVEWKE; DFATDIQSRIVEWKER; FATDIQSRIVEWKERL; ATDIQSRIVEWKERLD; TDIQSRIVEWKERLDS; DIQSRIVEWKERLDSE; IQSRIVEWKERLDSEI; QSRIVEWKERLDSEIS; SRIVEWKERLDSEISM; RIVEWKERLDSEISMY; IVEWKERLDSEISMYT; VEWKERLDSEISMYTF; EWKERLDSEISMYTFS; WKERLDSEISMYTFSR; KERLDSEISMYTFSRM; ERLDSEISMYTFSRMK; RLDSEISMYTFSRMKY; LDSEISMYTFSRMKYN; DSEISMYTFSRMKYNI; SEISMYTFSRMKYNIC; EISMYTFSRMKYNICM; ISMYTFSRMKYNICMG; SMYTFSRMKYNICMGK; MYTFSRMKYNICMGKC; YTFSRMKYNICMGKCI; TFSRMKYNICMGKCIL; FSRMKYNICMGKCILD; SRMKYNICMGKCILDI; RMKYNICMGKCILDIT; MKYNICMGKCILDITR; KYNICMGKCILDITRE; YNICMGKCILDITREE; NICMGKCILDITREED; ICMGKCILDITREEDS; CMGKCILDITREEDSE; MGKCILDITREEDSET; GKCILDITREEDSETE; KCILDITREEDSETED; CILDITREEDSETEDS; ILDITREEDSETEDSG; LDITREEDSETEDSGH; DITREEDSETEDSGHG; ITREEDSETEDSGHGS; TREEDSETEDSGHGSS; REEDSETEDSGHGSST; EEDSETEDSGHGSSTE; EDSETEDSGHGSSTES; DSETEDSGHGSSTESQ; SETEDSGHGSSTESQS; ETEDSGHGSSTESQSQ; TEDSGHGSSTESQSQC; EDSGHGSSTESQSQCS; DSGHGSSTESQSQCSS; SGHGSSTESQSQCSSQ; GHGSSTESQSQCSSQV; HGSSTESQSQCSSQVS; GSSTESQSQCSSQVSD; SSTESQSQCSSQVSDT; STESQSQCSSQVSDTS; TESQSQCSSQVSDTSA; ESQSQCSSQVSDTSAP; SQSQCSSQVSDTSAPA; QSQCSSQVSDTSAPAE; SQCSSQVSDTSAPAED; QCSSQVSDTSAPAEDS; CSSQVSDTSAPAEDSQ; SSQVSDTSAPAEDSQR; SQVSDTSAPAEDSQRS; QVSDTSAPAEDSQRSD; VSDTSAPAEDSQRSDP; SDTSAPAEDSQRSDPH; DTSAPAEDSQRSDPHS; TSAPAEDSQRSDPHSQ; SAPAEDSQRSDPHSQE; APAEDSQRSDPHSQEL; PAEDSQRSDPHSQELH; AEDSQRSDPHSQELHL; EDSQRSDPHSQELHLC; DSQRSDPHSQELHLCK; SQRSDPHSQELHLCKG; QRSDPHSQELHLCKGF; RSDPHSQELHLCKGFQ; SDPHSQELHLCKGFQC; DPHSQELHLCKGFQCF; PHSQELHLCKGFQCFK; HSQELHLCKGFQCFKR; SQELHLCKGFQCFKRP; QELHLCKGFQCFKRPK; ELHLCKGFQCFKRPKT; LHLCKGFQCFKRPKTP; HLCKGFQCFKRPKTPP; LCKGFQCFKRPKTPPP; CKGFQCFKRPKTPPPK; MYMYNKSTCLKHFGLQ; YMYNKSTCLKHFGLQL; MYNKSTCLKHFGLQLS; YNKSTCLKHFGLQLSL; NKSTCLKHFGLQLSLF; KSTCLKHFGLQLSLFV; STCLKHFGLQLSLFVN; TCLKHFGLQLSLFVNI; CLKHFGLQLSLFVNIS; LKHFGLQLSLFVNISY; KHFGLQLSLFVNISYH; HFGLQLSLFVNISYHI; FGLQLSLFVNISYHIW; GLQLSLFVNISYHIWV; LQLSLFVNISYHIWVP; QLSLFVNISYHIWVPW; LSLFVNISYHIWVPWK; SLFVNISYHIWVPWKS; LFVNISYHIWVPWKSF; FVNISYHIWVPWKSFC; VNISYHIWVPWKSFCA; NISYHIWVPWKSFCAI; ISYHIWVPWKSFCAIK; SYHIWVPWKSFCAIKH; YHIWVPWKSFCAIKHP; HIWVPWKSFCAIKHPN; IWVPWKSFCAIKHPNL; WVPWKSFCAIKHPNLF; VPWKSFCAIKHPNLFY; PWKSFCAIKHPNLFYL; WKSFCAIKHPNLFYLG; KSFCAIKHPNLFYLGF; SFCAIKHPNLFYLGFH; FCAIKHPNLFYLGFHT; CAIKHPNLFYLGFHTI; AIKHPNLFYLGFHTIH; IKHPNLFYLGFHTIHR; KHPNLFYLGFHTIHRL; HPNLFYLGFHTIHRLP; PNLFYLGFHTIHRLPI; NLFYLGFHTIHRLPIH; LFYLGFHTIHRLPIHS; FYLGFHTIHRLPIHSL; YLGFHTIHRLPIHSLG; LGFHTIHRLPIHSLGS; GFHTIHRLPIHSLGSP; FHTIHRLPIHSLGSPV; HTIHRLPIHSLGSPVY; TIHRLPIHSLGSPVYK; IHRLPIHSLGSPVYKV; HRLPIHSLGSPVYKVT; QKGNWVRILYRSFSQA; KGNWVRILYRSFSQAD; GNWVRILYRSFSQADL; NWVRILYRSFSQADLK; WVRILYRSFSQADLKI; VRILYRSFSQADLKIS; RILYRSFSQADLKISC; ILYRSFSQADLKISCK; LYRSFSQADLKISCKA; YRSFSQADLKISCKAS; RSFSQADLKISCKASP; SFSQADLKISCKASPL; FSQADLKISCKASPLL; SQADLKISCKASPLLC; QADLKISCKASPLLCS; ADLKISCKASPLLCSR; DLKISCKASPLLCSRA; LKISCKASPLLCSRAV; KISCKASPLLCSRAVS; ISCKASPLLCSRAVSK; SCKASPLLCSRAVSKQ; CKASPLLCSRAVSKQA; KASPLLCSRAVSKQAT; ASPLLCSRAVSKQATN; SPLLCSRAVSKQATNI; PLLCSRAVSKQATNIS; LLCSRAVSKQATNISS; NIQAISFTKRPHTLFI; QHCGSCVGHMKYWGNI; HCGSCVGHMKYWGNIF; CGSCVGHMKYWGNIFP; GSCVGHMKYWGNIFPS; SCVGHMKYWGNIFPSC; CVGHMKYWGNIFPSCE; VGHMKYWGNIFPSCES; GHMKYWGNIFPSCESP; HMKYWGNIFPSCESPK; MKYWGNIFPSCESPKI; KYWGNIFPSCESPKIP; YWGNIFPSCESPKIPS; WGNIFPSCESPKIPSI; GNIFPSCESPKIPSIF; NIFPSCESPKIPSIFI; IFPSCESPKIPSIFIS; FPSCESPKIPSIFIST; PSCESPKIPSIFISTG; SCESPKIPSIFISTGI; CESPKIPSIFISTGIR; ESPKIPSIFISTGIRY; SPKIPSIFISTGIRYP; PKIPSIFISTGIRYPA; KIPSIFISTGIRYPAL; IPSIFISTGIRYPALN; PSIFISTGIRYPALNW; SIFISTGIRYPALNWI; IFISTGIRYPALNWIS; FISTGIRYPALNWISI; ISTGIRYPALNWISIV; STGIRYPALNWISIVF; TGIRYPALNWISIVFV; GIRYPALNWISIVFVQ; IRYPALNWISIVFVQI; RYPALNWISIVFVQIG; YPALNWISIVFVQIGL; PALNWISIVFVQIGLM; ALNWISIVFVQIGLMV; LNWISIVFVQIGLMVS; NWISIVFVQIGLMVSI; WISIVFVQIGLMVSIH; ISIVFVQIGLMVSIHY; SIVFVQIGLMVSIHYL; IVFVQIGLMVSIHYLG; VFVQIGLMVSIHYLGL; FVQIGLMVSIHYLGLG; VQIGLMVSIHYLGLGC; QIGLMVSIHYLGLGCW; IGLMVSIHYLGLGCWV; GLMVSIHYLGLGCWVF; LMVSIHYLGLGCWVFR; MVSIHYLGLGCWVFRG; VSIHYLGLGCWVFRGY; SIHYLGLGCWVFRGYS; IHYLGLGCWVFRGYST; HYLGLGCWVFRGYSTI; YLGLGCWVFRGYSTIR; LGLGCWVFRGYSTIRV; GLGCWVFRGYSTIRVL; HSLHFQGFSTYSKEVE; SLHFQGFSTYSKEVEI; LHFQGFSTYSKEVEIT; HFQGFSTYSKEVEITA; FQGFSTYSKEVEITAL; QGFSTYSKEVEITALN; GFSTYSKEVEITALNR; FSTYSKEVEITALNRF; STYSKEVEITALNRFS; TYSKEVEITALNRFSS; YSKEVEITALNRFSST; SKEVEITALNRFSSTM; KEVEITALNRFSSTML; EVEITALNRFSSTMLM; VEITALNRFSSTMLMH; EITALNRFSSTMLMHF; ITALNRFSSTMLMHFL; PCMKVKHASYSNNLCL; CMKVKHASYSNNLCLY; MKVKHASYSNNLCLYS; KVKHASYSNNLCLYSY; VKHASYSNNLCLYSYS; KHASYSNNLCLYSYSL; HASYSNNLCLYSYSLP; ASYSNNLCLYSYSLPH; SYSNNLCLYSYSLPHQ; IGEGNSCCAVTGKHFS; GEGNSCCAVTGKHFSL; EGNSCCAVTGKHFSLW; GNSCCAVTGKHFSLWA; NSCCAVTGKHFSLWAI; SCCAVTGKHFSLWAIT; CCAVTGKHFSLWAITA; CAVTGKHFSLWAITAK; AVTGKHFSLWAITAKV; VTGKHFSLWAITAKVI; TGKHFSLWAITAKVIF; GKHFSLWAITAKVIFS; KHFSLWAITAKVIFST; FWHLHGFLWLFGSCPW; WHLHGFLWLFGSCPWT; HLHGFLWLFGSCPWTL; LHGFLWLFGSCPWTLS; HGFLWLFGSCPWTLSF; GFLWLFGSCPWTLSFS; FLWLFGSCPWTLSFSF; LWLFGSCPWTLSFSFG; WLFGSCPWTLSFSFGW; LFGSCPWTLSFSFGWG; FGSCPWTLSFSFGWGH; GSCPWTLSFSFGWGHL; SCPWTLSFSFGWGHLH; CPWTLSFSFGWGHLHM; PWTLSFSFGWGHLHML; WTLSFSFGWGHLHMLQ; TLSFSFGWGHLHMLQE; LSFSFGWGHLHMLQEQ; SFSFGWGHLHMLQEQV; FSFGWGHLHMLQEQVL; SFGWGHLHMLQEQVLQ; FGWGHLHMLQEQVLQS; GWGHLHMLQEQVLQSR; WGHLHMLQEQVLQSRT; GHLHMLQEQVLQSRTG; HLHMLQEQVLQSRTGL; LHMLQEQVLQSRTGLE; HMLQEQVLQSRTGLEV; MLQEQVLQSRTGLEVK; LQEQVLQSRTGLEVKA; QEQVLQSRTGLEVKAT; EQVLQSRTGLEVKATS; QVLQSRTGLEVKATSI; VLQSRTGLEVKATSIE; LQSRTGLEVKATSIEE; QSRTGLEVKATSIEEQ; SRTGLEVKATSIEEQF; RTGLEVKATSIEEQFF; TGLEVKATSIEEQFFD; TLLNVHFVDFLSPFFV; LLLYCQHHLYYKYGQN; LLYCQHHLYYKYGQNV; LYCQHHLYYKYGQNVH; YCQHHLYYKYGQNVHG; CQHHLYYKYGQNVHGY; QHHLYYKYGQNVHGYL; HHLYYKYGQNVHGYLP; HLYYKYGQNVHGYLPF; LYYKYGQNVHGYLPFQ; YYKYGQNVHGYLPFQL; YKYGQNVHGYLPFQLL; KYGQNVHGYLPFQLLV; QKYLHQETEYHSTHLG; TIPKPCLIADRGLQWK; IPKPCLIADRGLQWKL; PKPCLIADRGLQWKLC; KPCLIADRGLQWKLCD; PCLIADRGLQWKLCDP; CLIADRGLQWKLCDPN; LIADRGLQWKLCDPNH; IADRGLQWKLCDPNHQ; ADRGLQWKLCDPNHQR; DRGLQWKLCDPNHQRT; RGLQWKLCDPNHQRTY; GLQWKLCDPNHQRTYT; LQWKLCDPNHQRTYTL; QWKLCDPNHQRTYTLL; WKLCDPNHQRTYTLLE; KLCDPNHQRTYTLLEL; LCDPNHQRTYTLLELR; CDPNHQRTYTLLELRN; PQEHQQLQHMFEELGL; QQQPPQQQFQPLKILW; QQPPQQQFQPLKILWQ; QPPQQQFQPLKILWQQ; PPQQQFQPLKILWQQQ; PQQQFQPLKILWQQQP; QQQFQPLKILWQQQPQ; QQFQPLKILWQQQPQI; QFQPLKILWQQQPQIH; FQPLKILWQQQPQIHW; QPLKILWQQQPQIHWQ; PLKILWQQQPQIHWQL; LKILWQQQPQIHWQLG; KILWQQQPQIHWQLGP; ILWQQQPQIHWQLGPP; LWQQQPQIHWQLGPPK; WQQQPQIHWQLGPPKV; QQQPQIHWQLGPPKVL; QQPQIHWQLGPPKVLE; QPQIHWQLGPPKVLEQ; PQIHWQLGPPKVLEQH; QIHWQLGPPKVLEQHP; TWKYKKKGITYLGVFY; WKYKKKGITYLGVFYR; KYKKKGITYLGVFYRV; YKKKGITYLGVFYRVF; KKKGITYLGVFYRVFY; KKGITYLGVFYRVFYS; KGITYLGVFYRVFYSR; SSGTFVFPVYTVFTST; SGTFVFPVYTVFTSTK; GTFVFPVYTVFTSTKF; TFVFPVYTVFTSTKFQ; FVFPVYTVFTSTKFQQ; VFPVYTVFTSTKFQQK; FPVYTVFTSTKFQQKL; NKNKNPLSSFFCSSPG; KNKNPLSSFFCSSPGF; NKNPLSSFFCSSPGFT; KNPLSSFFCSSPGFTN; NPLSSFFCSSPGFTNF; PLSSFFCSSPGFTNFH; LGTRPRFLGSQNMSVM; GTRPRFLGSQNMSVMH; TRPRFLGSQNMSVMHF; RPRFLGSQNMSVMHFP; PRFLGSQNMSVMHFPS; AAPPCESCTFLPEVMV; APPCESCTFLPEVMVW; PPCESCTFLPEVMVWL; PCESCTFLPEVMVWLH; CESCTFLPEVMVWLHS; ESCTFLPEVMVWLHSP; SCTFLPEVMVWLHSPV; CTFLPEVMVWLHSPVS; TFLPEVMVWLHSPVSH; FLPEVMVWLHSPVSHA; LPEVMVWLHSPVSHAL; PEVMVWLHSPVSHALS; EVMVWLHSPVSHALSF; VMVWLHSPVSHALSFL; MVWLHSPVSHALSFLR; VWLHSPVSHALSFLRS; WLHSPVSHALSFLRSW; LHSPVSHALSFLRSWF; HSPVSHALSFLRSWFG; SPVSHALSFLRSWFGC; PVSHALSFLRSWFGCI; VSHALSFLRSWFGCIP; SHALSFLRSWFGCIPW; HALSFLRSWFGCIPWV; ALSFLRSWFGCIPWVS; LSFLRSWFGCIPWVSS; SFLRSWFGCIPWVSSS; FLRSWFGCIPWVSSSS; LRSWFGCIPWVSSSSL; RSWFGCIPWVSSSSLW; SWFGCIPWVSSSSLWP; WFGCIPWVSSSSLWPF; FGCIPWVSSSSLWPFF; GCIPWVSSSSLWPFFL; YIRGRGRLCLHPFSQV; IRGRGRLCLHPFSQVV; RGRGRLCLHPFSQVVR; GRGRLCLHPFSQVVRV; RGRLCLHPFSQVVRVW; GRLCLHPFSQVVRVWR; RLCLHPFSQVVRVWRL; LCLHPFSQVVRVWRLF; CLHPFSQVVRVWRLFL; LHPFSQVVRVWRLFLR; HPFSQVVRVWRLFLRP; PFSQVVRVWRLFLRPS; FSQVVRVWRLFLRPSK; SQVVRVWRLFLRPSKT; QVVRVWRLFLRPSKTI; VVRVWRLFLRPSKTIW; VRVWRLFLRPSKTIWG; RVWRLFLRPSKTIWGN; VWRLFLRPSKTIWGNP; WRLFLRPSKTIWGNPY; RLFLRPSKTIWGNPYS; LFLRPSKTIWGNPYSF; FLRPSKTIWGNPYSFA; LRPSKTIWGNPYSFAI; RPSKTIWGNPYSFAIF; PSKTIWGNPYSFAIFA; SKTIWGNPYSFAIFAK SEQ ID NOS.: 24957-44888

Preferred BK virus fragments of VP2-3 capable of interacting with one or more MHC class 2 molecules are listed in Table P.

TABLE P Prediction of BK virus VP2-3 protein specific MHC class 2, 15-mer peptide binders for 14 MHC class 2 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHCII/ database. The MHC class 2 molecules for which no binders were found are not listed. Allele pos peptide core 1-log50k(aff) aff(nM) B.L. Identity DRB1_0101 36 AAIEVQIASLATVEG  VQIASLATV 0.7655 13 SB BK VP2-3 DRB1_0101 37 AIEVQIASLATVEGI  IASLATVEG 0.7653 13 SB BK VP2-3 DRB1_0101 38 IEVQIASLATVEGIT  IASLATVEG 0.7535 14 SB BK VP2-3 DRB1_0101 39 EVQIASLATVEGITT  IASLATVEG 0.7419 16 SB BK VP2-3 DRB1_0101 216 QDYYSNLSPIRPSMV  YSNLSPIRP 0.7369 17 SB BK VP2-3 DRB1_0101 258 VTQRMDLRNKESVHS  VTQRMDLRN 0.7362 17 SB BK VP2-3 DRB1_0101 259 TQRMDLRNKESVHSG  LRNKESVHS 0.7390 17 SB BK VP2-3 DRB1_0101 260 QRMDLRNKESVHSGE  LRNKESVHS 0.7399 17 SB BK VP2-3 DRB1_0101 261 RMDLRNKESVHSGEF  LRNKESVHS 0.7383 17 SB BK VP2-3 DRB1_0101 262 MDLRNKESVHSGEFI  LRNKESVHS 0.7362 17 SB BK VP2-3 DRB1_0101 217 DYYSNLSPIRPSMVR  YSNLSPIRP 0.7308 18 SB BK VP2-3 DRB1_0101 82 AALIQTVTGISSLAQ  IQTVTGISS 0.7316 18 SB BK VP2-3 DRB1_0101 83 ALIQTVTGISSLAQV  VTGISSLAQ 0.7288 19 SB BK VP2-3 DRB1_0101 40 VQIASLATVEGITTT  IASLATVEG 0.7231 20 SB BK VP2-3 DRB1_0101 66 QTYAVIAGAPGAIAG  IAGAPGAIA 0.7250 20 SB BK VP2-3 DRB1_0101 65 PQTYAVIAGAPGAIA  VIAGAPGAI 0.7203 21 SB BK VP2-3 DRB1_0101 67 TYAVIAGAPGAIAGF  IAGAPGAIA 0.7196 21 SB BK VP2-3 DRB1_0101 68 YAVIAGAPGAIAGFA  IAGAPGAIA 0.7188 21 SB BK VP2-3 DRB1_0101 213 NYIQDYYSNLSPIRP  YYSNLSPIR 0.7087 23 SB BK VP2-3 DRB1_0101 214 YIQDYYSNLSPIRPS  YSNLSPIRP 0.7104 23 SB BK VP2-3 DRB1_0101 215 IQDYYSNLSPIRPSM  YSNLSPIRP 0.7116 23 SB BK VP2-3 DRB1_0101 219 YSNLSPIRPSMVRQV  YSNLSPIRP 0.7018 25 SB BK VP2-3 DRB1_0101 84 LIQTVTGISSLAQVG  VTGISSLAQ 0.7012 25 SB BK VP2-3 DRB1_0101 69 AVIAGAPGAIAGFAA  IAGAPGAIA 0.6972 26 SB BK VP2-3 DRB1_0101 85 IQTVTGISSLAQVGY  VTGISSLAQ 0.7004 26 SB BK VP2-3 DRB1_0101 24 FSVAEIAAGEAAAAI  IAAGEAAAA 0.6947 27 SB BK VP2-3 DRB1_0101 26 VAEIAAGEAAAAIEV  IAAGEAAAA 0.6967 27 SB BK VP2-3 DRB1_0101 27 AEIAAGEAAAAIEVQ  IAAGEAAAA 0.6963 27 SB BK VP2-3 DRB1_0101 25 SVAEIAAGEAAAAIE  IAAGEAAAA 0.6933 28 SB BK VP2-3 DRB1_0101 34 AAAAIEVQIASLATV  EVQIASLAT 0.6919 28 SB BK VP2-3 DRB1_0101 35 AAAIEVQIASLATVE  VQIASLATV 0.6928 28 SB BK VP2-3 DRB1_0101 23 GFSVAEIAAGEAAAA  VAEIAAGEA 0.6867 30 SB BK VP2-3 DRB1_0101 292 QWMLPLLLGLYGTVT  QWMLPLLLG 0.6800 32 SB BK VP2-3 DRB1_0101 1 MGAALALLGDLVASV  MGAALALLG 0.6779 33 SB BK VP2-3 DRB1_0101 296 PLLLGLYGTVTPALE  LLGLYGTVT 0.6771 33 SB BK VP2-3 DRB1_0101 289 TAPQWMLPLLLGLYG  PQWMLPLLL 0.6746 34 SB BK VP2-3 DRB1_0101 295 LPLLLGLYGTVTPAL  LLGLYGTVT 0.6709 35 SB BK VP2-3 DRB1_0101 218 YYSNLSPIRPSMVRQ  YSNLSPIRP 0.6689 36 SB BK VP2-3 DRB1_0101 293 WMLPLLLGLYGTVTP  LLGLYGTVT 0.6559 41 SB BK VP2-3 DRB1_0101 294 MLPLLLGLYGTVTPA  LLGLYGTVT 0.6545 42 SB BK VP2-3 DRB1_0101 220 SNLSPIRPSMVRQVA  IRPSMVRQV 0.6515 43 SB BK VP2-3 DRB1_0101 288 RTAPQWMLPLLLGLY  PQWMLPLLL 0.6514 43 SB BK VP2-3 DRB1_0101 86 QTVTGISSLAQVGYR  VTGISSLAQ 0.6515 43 SB BK VP2-3 DRB1_0101 9 GDLVASVSEAAAATG  LVASVSEAA 0.6476 45 SB BK VP2-3 DRB1_0101 287 QRTAPQWMLPLLLGL  PQWMLPLLL 0.6469 46 SB BK VP2-3 DRB1_0101 290 APQWMLPLLLGLYGT  QWMLPLLLG 0.6444 47 SB BK VP2-3 DRB1_0101 263 DLRNKESVHSGEFIE  LRNKESVHS 0.6362 51 WB BK VP2-3 DRB1_0101 264 LRNKESVHSGEFIEK  LRNKESVHS 0.6346 52 WB BK VP2-3 DRB1_0101 42 IASLATVEGITTTSE  IASLATVEG 0.6326 53 WB BK VP2-3 DRB1_0101 5 LALLGDLVASVSEAA  LGDLVASVS 0.6322 53 WB BK VP2-3 DRB1_0101 170 RDDIPAITSQELQRR  IPAITSQEL 0.6313 54 WB BK VP2-3 DRB1_0101 171 DDIPAITSQELQRRT  IPAITSQEL 0.6309 54 WB BK VP2-3 DRB1_0101 186 ERFFRDSLARFLEET  FRDSLARFL 0.6320 54 WB BK VP2-3 DRB1_0101 184 RTERFFRDSLARFLE  FRDSLARFL 0.6295 55 WB BK VP2-3 DRB1_0101 185 TERFFRDSLARFLEE  FRDSLARFL 0.6304 55 WB BK VP2-3 DRB1_0101 183 RRTERFFRDSLARFL  FFRDSLARF 0.6285 56 WB BK VP2-3 DRB1_0101 187 RFFRDSLARFLEETT  FRDSLARFL 0.6286 56 WB BK VP2-3 DRB1_0101 70 VIAGAPGAIAGFAAL  IAGAPGAIA 0.6277 56 WB BK VP2-3 DRB1_0101 75 PGAIAGFAALIQTVT  IAGFAALIQ 0.6288 56 WB BK VP2-3 DRB1_0101 76 GAIAGFAALIQTVTG  FAALIQTVT 0.6280 56 WB BK VP2-3 DRB1_0101 41 QIASLATVEGITTTS  IASLATVEG 0.6263 57 WB BK VP2-3 DRB1_0101 6 ALLGDLVASVSEAAA  LVASVSEAA 0.6253 58 WB BK VP2-3 DRB1_0101 221 NLSPIRPSMVRQVAE  IRPSMVRQV 0.6218 60 WB BK VP2-3 DRB1_0101 297 LLLGLYGTVTPALEA  LLGLYGTVT 0.6216 60 WB BK VP2-3 DRB1_0101 222 LSPIRPSMVRQVAER  IRPSMVRQV 0.6206 61 WB BK VP2-3 DRB1_0101 291 PQWMLPLLLGLYGTV  PQWMLPLLL 0.6197 61 WB BK VP2-3 DRB1_0101 298 LLGLYGTVTPALEAY  LLGLYGTVT 0.6201 61 WB BK VP2-3 DRB1_0101 79 AGFAALIQTVTGISS  FAALIQTVT 0.6202 61 WB BK VP2-3 DRB1_0101 8 LGDLVASVSEAAAAT  LVASVSEAA 0.6196 61 WB BK VP2-3 DRB1_0101 155 PSLFATISQALWHVI  LFATISQAL 0.6154 64 WB BK VP2-3 DRB1_0101 28 EIAAGEAAAAIEVQI  IAAGEAAAA 0.6146 65 WB BK VP2-3 DRB1_0101 286 NQRTAPQWMLPLLLG  PQWMLPLLL 0.6139 65 WB BK VP2-3 DRB1_0101 151 RHWGPSLFATISQAL  RHWGPSLFA 0.6126 66 WB BK VP2-3 DRB1_0101 275 FIEKTIAPGGANQRT  IAPGGANQR 0.6093 69 WB BK VP2-3 DRB1_0101 29 IAAGEAAAAIEVQIA  IAAGEAAAA 0.6093 69 WB BK VP2-3 DRB1_0101 7 LLGDLVASVSEAAAA  LVASVSEAA 0.6068 70 WB BK VP2-3 DRB1_0101 11 LVASVSEAAAATGFS  VSEAAAATG 0.6048 72 WB BK VP2-3 DRB1_0101 152 HWGPSLFATISQALW  LFATISQAL 0.6052 72 WB BK VP2-3 DRB1_0101 276 IEKTIAPGGANQRTA  IAPGGANQR 0.6053 72 WB BK VP2-3 DRB1_0101 154 GPSLFATISQALWHV  LFATISQAL 0.6040 73 WB BK VP2-3 DRB1_0101 111 TVGLYQQSGMALELF  LYQQSGMAL 0.6024 74 WB BK VP2-3 DRB1_0101 10 DLVASVSEAAAATGF  VSEAAAATG 0.6015 75 WB BK VP2-3 DRB1_0101 112 VGLYQQSGMALELFN  LYQQSGMAL 0.6010 75 WB BK VP2-3 DRB1_0101 277 EKTIAPGGANQRTAP  IAPGGANQR 0.6011 75 WB BK VP2-3 DRB1_0101 71 IAGAPGAIAGFAALI  IAGAPGAIA 0.6015 75 WB BK VP2-3 DRB1_0101 153 WGPSLFATISQALWH  LFATISQAL 0.5994 76 WB BK VP2-3 DRB1_0101 223 SPIRPSMVRQVAERE  IRPSMVRQV 0.6003 76 WB BK VP2-3 DRB1_0101 110 STVGLYQQSGMALEL  LYQQSGMAL 0.5977 78 WB BK VP2-3 DRB1_0101 78 IAGFAALIQTVTGIS  FAALIQTVT 0.5963 79 WB BK VP2-3 DRB1_0101 77 AIAGFAALIQTVTGI  FAALIQTVT 0.5949 80 WB BK VP2-3 DRB1_0101 278 KTIAPGGANQRTAPQ  IAPGGANQR 0.5943 81 WB BK VP2-3 DRB1_0101 2 GAALALLGDLVASVS  LALLGDLVA 0.5930 82 WB BK VP2-3 DRB1_0101 3 AALALLGDLVASVSE  LGDLVASVS 0.5912 83 WB BK VP2-3 DRB1_0101 81 FAALIQTVTGISSLA  IQTVTGISS 0.5912 83 WB BK VP2-3 DRB1_0101 173 IPAITSQELQRRTER  ITSQELQRR 0.5853 89 WB BK VP2-3 DRB1_0101 172 DIPAITSQELQRRTE  ITSQELQRR 0.5840 90 WB BK VP2-3 DRB1_0101 88 VTGISSLAQVGYRFF  VTGISSLAQ 0.5828 91 WB BK VP2-3 DRB1_0101 80 GFAALIQTVTGISSL  IQTVTGISS 0.5817 92 WB BK VP2-3 DRB1_0101 274 EFIEKTIAPGGANQR  IEKTIAPGG 0.5781 96 WB BK VP2-3 DRB1_0101 320 KRRVSRGSSQKAKGT  VSRGSSQKA 0.5786 96 WB BK VP2-3 DRB1_0101 167 HVIRDDIPAITSQEL  IRDDIPAIT 0.5761 98 WB BK VP2-3 DRB1_0101 109 VSTVGLYQQSGMALE  LYQQSGMAL 0.5756 99 WB BK VP2-3 DRB1_0101 64 TPQTYAVIAGAPGAI  YAVIAGAPG 0.5756 99 WB BK VP2-3 DRB1_0101 321 RRVSRGSSQKAKGTR  VSRGSSQKA 0.5746 100 WB BK VP2-3 DRB1_0101 323 VSRGSSQKAKGTRAS  VSRGSSQKA 0.5730 101 WB BK VP2-3 DRB1_0101 319 KKRRVSRGSSQKAKG  VSRGSSQKA 0.5712 104 WB BK VP2-3 DRB1_0101 318 QKKRRVSRGSSQKAK  VSRGSSQKA 0.5695 105 WB BK VP2-3 DRB1_0101 87 TVTGISSLAQVGYRF  VTGISSLAQ 0.5702 105 WB BK VP2-3 DRB1_0101 299 LGLYGTVTPALEAYE  LYGTVTPAL 0.5689 106 WB BK VP2-3 DRB1_0101 4 ALALLGDLVASVSEA  LGDLVASVS 0.5688 106 WB BK VP2-3 DRB1_0101 317 NQKKRRVSRGSSQKA  RVSRGSSQK 0.5685 107 WB BK VP2-3 DRB1_0101 12 VASVSEAAAATGFSV  VSEAAAATG 0.5666 109 WB BK VP2-3 DRB1_0101 169 IRDDIPAITSQELQR  IPAITSQEL 0.5628 113 WB BK VP2-3 DRB1_0101 285 ANQRTAPQWMLPLLL  RTAPQWMLP 0.5629 113 WB BK VP2-3 DRB1_0101 33 EAAAAIEVQIASLAT  IEVQIASLA 0.5628 113 WB BK VP2-3 DRB1_0101 74 APGAIAGFAALIQTV  IAGFAALIQ 0.5631 113 WB BK VP2-3 DRB1_0101 168 VIRDDIPAITSQELQ  IPAITSQEL 0.5596 117 WB BK VP2-3 DRB1_0101 212 YNYIQDYYSNLSPIR  IQDYYSNLS 0.5601 117 WB BK VP2-3 DRB1_0101 72 AGAPGAIAGFAALIQ  AIAGFAALI 0.5598 117 WB BK VP2-3 DRB1_0101 73 GAPGAIAGFAALIQT  IAGFAALIQ 0.5602 117 WB BK VP2-3 DRB1_0101 108 KVSTVGLYQQSGMAL  TVGLYQQSG 0.5550 123 WB BK VP2-3 DRB1_0101 156 SLFATISQALWHVIR  LFATISQAL 0.5526 127 WB BK VP2-3 DRB1_0101 13 ASVSEAAAATGFSVA  VSEAAAATG 0.5482 133 WB BK VP2-3 DRB1_0101 113 GLYQQSGMALELFNP  LYQQSGMAL 0.5426 141 WB BK VP2-3 DRB1_0101 157 LFATISQALWHVIRD  LFATISQAL 0.5415 143 WB BK VP2-3 DRB1_0101 188 FFRDSLARFLEETTW  FRDSLARFL 0.5345 154 WB BK VP2-3 DRB1_0101 43 ASLATVEGITTTSEA  LATVEGITT 0.5345 154 WB BK VP2-3 DRB1_0101 149 DPRHWGPSLFATISQ  RHWGPSLFA 0.5298 162 WB BK VP2-3 DRB1_0101 148 LDPRHWGPSLFATIS  RHWGPSLFA 0.5294 163 WB BK VP2-3 DRB1_0101 57 AIAAIGLTPQTYAVI  IAAIGLTPQ 0.5280 165 WB BK VP2-3 DRB1_0101 189 FRDSLARFLEETTWT  FRDSLARFL 0.5271 167 WB BK VP2-3 DRB1_0101 279 TIAPGGANQRTAPQW  IAPGGANQR 0.5252 170 WB BK VP2-3 DRB1_0101 174 PAITSQELQRRTERF  ITSQELQRR 0.5214 177 WB BK VP2-3 DRB1_0101 114 LYQQSGMALELFNPD  LYQQSGMAL 0.5213 178 WB BK VP2-3 DRB1_0101 199 ETTWTIVNAPINFYN  IVNAPINFY 0.5209 178 WB BK VP2-3 DRB1_0101 58 IAAIGLTPQTYAVIA  LTPQTYAVI 0.5203 180 WB BK VP2-3 DRB1_0101 147 YLDPRHWGPSLFATI  RHWGPSLFA 0.5192 182 WB BK VP2-3 DRB1_0101 56 EAIAAIGLTPQTYAV  IAAIGLTPQ 0.5190 182 WB BK VP2-3 DRB1_0101 200 TTWTIVNAPINFYNY  IVNAPINFY 0.5185 183 WB BK VP2-3 DRB1_0101 198 EETTWTIVNAPINFY  WTIVNAPIN 0.5179 184 WB BK VP2-3 DRB1_0101 224 PIRPSMVRQVAEREG  IRPSMVRQV 0.5170 186 WB BK VP2-3 DRB1_0101 63 LTPQTYAVIAGAPGA  YAVIAGAPG 0.5172 186 WB BK VP2-3 DRB1_0101 225 IRPSMVRQVAEREGT  IRPSMVRQV 0.5152 190 WB BK VP2-3 DRB1_0101 209 INFYNYIQDYYSNLS  YNYIQDYYS 0.5135 193 WB BK VP2-3 DRB1_0101 55 SEAIAAIGLTPQTYA  IAAIGLTPQ 0.5133 194 WB BK VP2-3 DRB1_0101 210 NFYNYIQDYYSNLSP  IQDYYSNLS 0.5129 195 WB BK VP2-3 DRB1_0101 145 IQYLDPRHWGPSLFA  IQYLDPRHW 0.5100 201 WB BK VP2-3 DRB1_0101 300 GLYGTVTPALEAYED  LYGTVTPAL 0.5097 201 WB BK VP2-3 DRB1_0101 322 RVSRGSSQKAKGTRA  VSRGSSQKA 0.5073 207 WB BK VP2-3 DRB1_0101 201 TWTIVNAPINFYNYI  IVNAPINFY 0.5050 212 WB BK VP2-3 DRB1_0101 202 WTIVNAPINFYNYIQ  IVNAPINFY 0.5004 223 WB BK VP2-3 DRB1_0101 140 TFVNNIQYLDPRHWG  IQYLDPRHW 0.4969 231 WB BK VP2-3 DRB1_0101 327 SSQKAKGTRASAKTT  QKAKGTRAS 0.4971 231 WB BK VP2-3 DRB1_0101 139 NTFVNNIQYLDPRHW  VNNIQYLDP 0.4965 232 WB BK VP2-3 DRB1_0101 45 LATVEGITTTSEAIA  VEGITTTSE 0.4966 232 WB BK VP2-3 DRB1_0101 62 GLTPQTYAVIAGAPG  TPQTYAVIA 0.4959 234 WB BK VP2-3 DRB1_0101 280 IAPGGANQRTAPQWM  IAPGGANQR 0.4948 237 WB BK VP2-3 DRB1_0101 54 TSEAIAAIGLTPQTY  IAAIGLTPQ 0.4931 241 WB BK VP2-3 DRB1_0101 142 VNNIQYLDPRHWGPS  IQYLDPRHW 0.4908 247 WB BK VP2-3 DRB1_0101 211 FYNYIQDYYSNLSPI  IQDYYSNLS 0.4889 252 WB BK VP2-3 DRB1_0101 53 TTSEAIAAIGLTPQT  IAAIGLTPQ 0.4889 252 WB BK VP2-3 DRB1_0101 141 FVNNIQYLDPRHWGP  IQYLDPRHW 0.4885 253 WB BK VP2-3 DRB1_0101 143 NNIQYLDPRHWGPSL  IQYLDPRHW 0.4867 258 WB BK VP2-3 DRB1_0101 44 SLATVEGITTTSEAI  VEGITTTSE 0.4868 258 WB BK VP2-3 DRB1_0101 59 AAIGLTPQTYAVIAG  LTPQTYAVI 0.4849 263 WB BK VP2-3 DRB1_0101 326 GSSQKAKGTRASAKT  QKAKGTRAS 0.4838 267 WB BK VP2-3 DRB1_0101 14 SVSEAAAATGFSVAE  VSEAAAATG 0.4826 270 WB BK VP2-3 DRB1_0101 150 PRHWGPSLFATISQA  WGPSLFATI 0.4823 271 WB BK VP2-3 DRB1_0101 301 LYGTVTPALEAYEDG  LYGTVTPAL 0.4803 277 WB BK VP2-3 DRB1_0101 129 EYYDILFPGVNTFVN  LFPGVNTFV 0.4778 284 WB BK VP2-3 DRB1_0101 60 AIGLTPQTYAVIAGA  LTPQTYAVI 0.4766 288 WB BK VP2-3 DRB1_0101 146 QYLDPRHWGPSLFAT  RHWGPSLFA 0.4756 291 WB BK VP2-3 DRB1_0101 52 TTTSEAIAAIGLTPQ  SEAIAAIGL 0.4719 303 WB BK VP2-3 DRB1_0101 130 YYDILFPGVNTFVNN  LFPGVNTFV 0.4703 308 WB BK VP2-3 DRB1_0101 128 DEYYDILFPGVNTFV  YYDILFPGV 0.4673 318 WB BK VP2-3 DRB1_0101 325 RGSSQKAKGTRASAK  QKAKGTRAS 0.4649 327 WB BK VP2-3 DRB1_0101 131 YDILFPGVNTFVNNI  LFPGVNTFV 0.4632 333 WB BK VP2-3 DRB1_0101 46 ATVEGITTTSEAIAA  VEGITTTSE 0.4606 342 WB BK VP2-3 DRB1_0101 15 VSEAAAATGFSVAEI  VSEAAAATG 0.4598 345 WB BK VP2-3 DRB1_0101 328 SQKAKGTRASAKTTN  QKAKGTRAS 0.4565 358 WB BK VP2-3 DRB1_0101 132 DILFPGVNTFVNNIQ  LFPGVNTFV 0.4558 361 WB BK VP2-3 DRB1_0101 61 IGLTPQTYAVIAGAP  LTPQTYAVI 0.4557 361 WB BK VP2-3 DRB1_0101 324 SRGSSQKAKGTRASA  QKAKGTRAS 0.4547 365 WB BK VP2-3 DRB1_0101 329 QKAKGTRASAKTTNK  QKAKGTRAS 0.4538 369 WB BK VP2-3 DRB1_0101 22 TGFSVAEIAAGEAAA  FSVAEIAAG 0.4532 371 WB BK VP2-3 DRB1_0101 32 GEAAAAIEVQIASLA  AAAIEVQIA 0.4528 372 WB BK VP2-3 DRB1_0101 21 ATGFSVAEIAAGEAA  FSVAEIAAG 0.4520 376 WB BK VP2-3 DRB1_0101 20 AATGFSVAEIAAGEA  FSVAEIAAG 0.4471 396 WB BK VP2-3 DRB1_0101 227 PSMVRQVAEREGTHV  MVRQVAERE 0.4426 416 WB BK VP2-3 DRB1_0101 101 FFSDWDHKVSTVGLY  WDHKVSTVG 0.4398 429 WB BK VP2-3 DRB1_0101 100 RFFSDWDHKVSTVGL  WDHKVSTVG 0.4393 431 WB BK VP2-3 DRB1_0101 103 SDWDHKVSTVGLYQQ  WDHKVSTVG 0.4367 443 WB BK VP2-3 DRB1_0101 158 FATISQALWHVIRDD  ISQALWHVI 0.4312 471 WB BK VP2-3 DRB1_0101 175 AITSQELQRRTERFF  ITSQELQRR 0.4287 483 WB BK VP2-3 DRB1_0101 49 EGITTTSEAIAAIGL  ITTTSEAIA 0.4284 485 WB BK VP2-3 DRB1_0101 102 FSDWDHKVSTVGLYQ  WDHKVSTVG 0.4283 486 WB BK VP2-3 DRB1_0301 182 QRRTERFFRDSLARF  RFFRDSLAR 0.4487 390 WB BK VP2-3 DRB1_0301 183 RRTERFFRDSLARFL  FFRDSLARF 0.4472 396 WB BK VP2-3 DRB1_0301 186 ERFFRDSLARFLEET  FFRDSLARF 0.4469 397 WB BK VP2-3 DRB1_0301 184 RTERFFRDSLARFLE  FFRDSLARF 0.4468 398 WB BK VP2-3 DRB1_0301 185 TERFFRDSLARFLEE  FFRDSLARF 0.4464 399 WB BK VP2-3 DRB1_0401 213 NYIQDYYSNLSPIRP  YYSNLSPIR 0.5927 82 WB BK VP2-3 DRB1_0401 212 YNYIQDYYSNLSPIR  IQDYYSNLS 0.5864 88 WB BK VP2-3 DRB1_0401 214 YIQDYYSNLSPIRPS  YYSNLSPIR 0.5789 95 WB BK VP2-3 DRB1_0401 215 IQDYYSNLSPIRPSM  YYSNLSPIR 0.5767 97 WB BK VP2-3 DRB1_0401 216 QDYYSNLSPIRPSMV  YYSNLSPIR 0.5674 108 WB BK VP2-3 DRB1_0401 258 VTQRMDLRNKESVHS  VTQRMDLRN 0.5284 164 WB BK VP2-3 DRB1_0401 259 TQRMDLRNKESVHSG  LRNKESVHS 0.5237 173 WB BK VP2-3 DRB1_0401 260 QRMDLRNKESVHSGE  LRNKESVHS 0.5240 173 WB BK VP2-3 DRB1_0401 261 RMDLRNKESVHSGEF  LRNKESVHS 0.5213 178 WB BK VP2-3 DRB1_0401 262 MDLRNKESVHSGEFI  LRNKESVHS 0.5168 187 WB BK VP2-3 DRB1_0401 5 LALLGDLVASVSEAA  LLGDLVASV 0.5166 187 WB BK VP2-3 DRB1_0401 6 ALLGDLVASVSEAAA  LVASVSEAA 0.5140 192 WB BK VP2-3 DRB1_0401 7 LLGDLVASVSEAAAA  LVASVSEAA 0.5130 194 WB BK VP2-3 DRB1_0401 8 LGDLVASVSEAAAAT  LVASVSEAA 0.5130 194 WB BK VP2-3 DRB1_0401 9 GDLVASVSEAAAATG  LVASVSEAA 0.5118 197 WB BK VP2-3 DRB1_0401 82 AALIQTVTGISSLAQ  LIQTVTGIS 0.5068 208 WB BK VP2-3 DRB1_0401 217 DYYSNLSPIRPSMVR  YYSNLSPIR 0.4779 284 WB BK VP2-3 DRB1_0401 83 ALIQTVTGISSLAQV  VTGISSLAQ 0.4763 289 WB BK VP2-3 DRB1_0401 84 LIQTVTGISSLAQVG  VTGISSLAQ 0.4711 306 WB BK VP2-3 DRB1_0401 218 YYSNLSPIRPSMVRQ  YYSNLSPIR 0.4694 312 WB BK VP2-3 DRB1_0401 198 EETTWTIVNAPINFY  WTIVNAPIN 0.4557 361 WB BK VP2-3 DRB1_0401 199 ETTWTIVNAPINFYN  IVNAPINFY 0.4556 362 WB BK VP2-3 DRB1_0401 200 TTWTIVNAPINFYNY  IVNAPINFY 0.4527 373 WB BK VP2-3 DRB1_0401 85 IQTVTGISSLAQVGY  VTGISSLAQ 0.4432 414 WB BK VP2-3 DRB1_0401 202 WTIVNAPINFYNYIQ  IVNAPINFY 0.4421 418 WB BK VP2-3 DRB1_0401 201 TWTIVNAPINFYNYI  IVNAPINFY 0.4401 427 WB BK VP2-3 DRB1_0401 81 FAALIQTVTGISSLA  LIQTVTGIS 0.4399 428 WB BK VP2-3 DRB1_0401 36 AAIEVQIASLATVEG  IEVQIASLA 0.4327 463 WB BK VP2-3 DRB1_0401 132 DILFPGVNTFVNNIQ  GVNTFVNNI 0.4289 483 WB BK VP2-3 DRB1_0404 213 NYIQDYYSNLSPIRP  IQDYYSNLS 0.5128 195 WB BK VP2-3 DRB1_0404 82 AALIQTVTGISSLAQ  LIQTVTGIS 0.4868 258 WB BK VP2-3 DRB1_0404 198 EETTWTIVNAPINFY  TTWTIVNAP 0.4822 271 WB BK VP2-3 DRB1_0404 215 IQDYYSNLSPIRPSM  IQDYYSNLS 0.4815 273 WB BK VP2-3 DRB1_0404 295 LPLLLGLYGTVTPAL  LLGLYGTVT 0.4754 292 WB BK VP2-3 DRB1_0404 214 YIQDYYSNLSPIRPS  IQDYYSNLS 0.4645 328 WB BK VP2-3 DRB1_0404 296 PLLLGLYGTVTPALE  LLGLYGTVT 0.4620 337 WB BK VP2-3 DRB1_0404 293 WMLPLLLGLYGTVTP  LLGLYGTVT 0.4571 356 WB BK VP2-3 DRB1_0404 294 MLPLLLGLYGTVTPA  LLGLYGTVT 0.4547 365 WB BK VP2-3 DRB1_0404 36 AAIEVQIASLATVEG  IEVQIASLA 0.4515 378 WB BK VP2-3 DRB1_0404 200 TTWTIVNAPINFYNY  IVNAPINFY 0.4472 396 WB BK VP2-3 DRB1_0404 194 ARFLEETTWTIVNAP  FLEETTWTI 0.4467 398 WB BK VP2-3 DRB1_0404 212 YNYIQDYYSNLSPIR  IQDYYSNLS 0.4449 406 WB BK VP2-3 DRB1_0404 199 ETTWTIVNAPINFYN  IVNAPINFY 0.4444 408 WB BK VP2-3 DRB1_0404 81 FAALIQTVTGISSLA  LIQTVTGIS 0.4428 415 WB BK VP2-3 DRB1_0404 292 QWMLPLLLGLYGTVT  MLPLLLGLY 0.4376 439 WB BK VP2-3 DRB1_0404 297 LLLGLYGTVTPALEA  LGLYGTVTP 0.4365 445 WB BK VP2-3 DRB1_0404 84 LIQTVTGISSLAQVG  LIQTVTGIS 0.4287 483 WB BK VP2-3 DRB1_0404 38 IEVQIASLATVEGIT  IASLATVEG 0.4281 487 WB BK VP2-3 DRB1_0404 78 IAGFAALIQTVTGIS  AALIQTVTG 0.4270 493 WB BK VP2-3 DRB1_0404 196 FLEETTWTIVNAPIN  TTWTIVNAP 0.4258 499 WB BK VP2-3 DRB1_0405 213 NYIQDYYSNLSPIRP  IQDYYSNLS 0.5630 113 WB BK VP2-3 DRB1_0405 212 YNYIQDYYSNLSPIR  IQDYYSNLS 0.5391 146 WB BK VP2-3 DRB1_0405 209 INFYNYIQDYYSNLS  YNYIQDYYS 0.5339 155 WB BK VP2-3 DRB1_0405 96 QVGYRFFSDWDHKVS  YRFFSDWDH 0.5285 164 WB BK VP2-3 DRB1_0405 210 NFYNYIQDYYSNLSP  IQDYYSNLS 0.5274 166 WB BK VP2-3 DRB1_0405 196 FLEETTWTIVNAPIN  EETTWTIVN 0.5259 169 WB BK VP2-3 DRB1_0405 214 YIQDYYSNLSPIRPS  IQDYYSNLS 0.5183 184 WB BK VP2-3 DRB1_0405 215 IQDYYSNLSPIRPSM  IQDYYSNLS 0.5155 189 WB BK VP2-3 DRB1_0405 135 FPGVNTFVNNIQYLD  VNTFVNNIQ 0.5129 194 WB BK VP2-3 DRB1_0405 211 FYNYIQDYYSNLSPI  IQDYYSNLS 0.5093 202 WB BK VP2-3 DRB1_0405 198 EETTWTIVNAPINFY  WTIVNAPIN 0.5089 203 WB BK VP2-3 DRB1_0405 136 PGVNTFVNNIQYLDP  VNTFVNNIQ 0.5073 207 WB BK VP2-3 DRB1_0405 95 AQVGYRFFSDWDHKV  YRFFSDWDH 0.5059 210 WB BK VP2-3 DRB1_0405 132 DILFPGVNTFVNNIQ  FPGVNTFVN 0.5008 222 WB BK VP2-3 DRB1_0405 133 ILFPGVNTFVNNIQY  VNTFVNNIQ 0.4983 228 WB BK VP2-3 DRB1_0405 97 VGYRFFSDWDHKVST  YRFFSDWDH 0.4930 241 WB BK VP2-3 DRB1_0405 194 ARFLEETTWTIVNAP  EETTWTIVN 0.4887 253 WB BK VP2-3 DRB1_0405 197 LEETTWTIVNAPINF  WTIVNAPIN 0.4832 268 WB BK VP2-3 DRB1_0405 199 ETTWTIVNAPINFYN  WTIVNAPIN 0.4813 274 WB BK VP2-3 DRB1_0405 195 RFLEETTWTIVNAPI  EETTWTIVN 0.4799 278 WB BK VP2-3 DRB1_0405 94 LAQVGYRFFSDWDHK  GYRFFSDWD 0.4772 286 WB BK VP2-3 DRB1_0405 93 SLAQVGYRFFSDWDH  GYRFFSDWD 0.4758 291 WB BK VP2-3 DRB1_0405 134 LFPGVNTFVNNIQYL  VNTFVNNIQ 0.4752 292 WB BK VP2-3 DRB1_0405 193 LARFLEETTWTIVNA  EETTWTIVN 0.4694 312 WB BK VP2-3 DRB1_0405 158 FATISQALWHVIRDD  QALWHVIRD 0.4626 335 WB BK VP2-3 DRB1_0405 157 LFATISQALWHVIRD  SQALWHVIR 0.4616 339 WB BK VP2-3 DRB1_0405 200 TTWTIVNAPINFYNY  IVNAPINFY 0.4599 345 WB BK VP2-3 DRB1_0405 98 GYRFFSDWDHKVSTV  YRFFSDWDH 0.4557 361 WB BK VP2-3 DRB1_0405 192 SLARFLEETTWTIVN  FLEETTWTI 0.4451 405 WB BK VP2-3 DRB1_0405 137 GVNTFVNNIQYLDPR  VNTFVNNIQ 0.4315 469 WB BK VP2-3 DRB1_0405 138 VNTFVNNIQYLDPRH  VNTFVNNIQ 0.4315 469 WB BK VP2-3 DRB1_0701 155 PSLFATISQALWHVI  LFATISQAL 0.6499 44 SB BK VP2-3 DRB1_0701 154 GPSLFATISQALWHV  LFATISQAL 0.6324 53 WB BK VP2-3 DRB1_0701 153 WGPSLFATISQALWH  LFATISQAL 0.6252 58 WB BK VP2-3 DRB1_0701 152 HWGPSLFATISQALW  LFATISQAL 0.6229 59 WB BK VP2-3 DRB1_0701 151 RHWGPSLFATISQAL  WGPSLFATI 0.6204 61 WB BK VP2-3 DRB1_0701 219 YSNLSPIRPSMVRQV  LSPIRPSMV 0.6186 62 WB BK VP2-3 DRB1_0701 220 SNLSPIRPSMVRQVA  LSPIRPSMV 0.6184 62 WB BK VP2-3 DRB1_0701 216 QDYYSNLSPIRPSMV  YYSNLSPIR 0.6145 65 WB BK VP2-3 DRB1_0701 217 DYYSNLSPIRPSMVR  LSPIRPSMV 0.6117 67 WB BK VP2-3 DRB1_0701 218 YYSNLSPIRPSMVRQ  LSPIRPSMV 0.6108 67 WB BK VP2-3 DRB1_0701 194 ARFLEETTWTIVNAP  FLEETTWTI 0.6047 72 WB BK VP2-3 DRB1_0701 191 DSLARFLEETTWTIV  FLEETTWTI 0.6040 73 WB BK VP2-3 DRB1_0701 193 LARFLEETTWTIVNA  FLEETTWTI 0.6028 73 WB BK VP2-3 DRB1_0701 192 SLARFLEETTWTIVN  FLEETTWTI 0.6024 74 WB BK VP2-3 DRB1_0701 156 SLFATISQALWHVIR  LFATISQAL 0.5732 101 WB BK VP2-3 DRB1_0701 157 LFATISQALWHVIRD  LFATISQAL 0.5709 104 WB BK VP2-3 DRB1_0701 195 RFLEETTWTIVNAPI  LEETTWTIV 0.5523 127 WB BK VP2-3 DRB1_0701 221 NLSPIRPSMVRQVAE  LSPIRPSMV 0.5258 169 WB BK VP2-3 DRB1_0701 222 LSPIRPSMVRQVAER  LSPIRPSMV 0.5249 171 WB BK VP2-3 DRB1_0701 196 FLEETTWTIVNAPIN  FLEETTWTI 0.5082 205 WB BK VP2-3 DRB1_0701 58 IAAIGLTPQTYAVIA  LTPQTYAVI 0.4999 224 WB BK VP2-3 DRB1_0701 57 AIAAIGLTPQTYAVI  AIGLTPQTY 0.4992 226 WB BK VP2-3 DRB1_0701 59 AAIGLTPQTYAVIAG  LTPQTYAVI 0.4959 234 WB BK VP2-3 DRB1_0701 60 AIGLTPQTYAVIAGA  LTPQTYAVI 0.4955 235 WB BK VP2-3 DRB1_0701 61 IGLTPQTYAVIAGAP  LTPQTYAVI 0.4924 243 WB BK VP2-3 DRB1_0701 190 RDSLARFLEETTWTI  RDSLARFLE 0.4903 248 WB BK VP2-3 DRB1_0701 167 HVIRDDIPAITSQEL  VIRDDIPAI 0.4747 294 WB BK VP2-3 DRB1_0701 131 YDILFPGVNTFVNNI  LFPGVNTFV 0.4730 299 WB BK VP2-3 DRB1_0701 168 VIRDDIPAITSQELQ  IPAITSQEL 0.4729 300 WB BK VP2-3 DRB1_0701 132 DILFPGVNTFVNNIQ  LFPGVNTFV 0.4725 301 WB BK VP2-3 DRB1_0701 169 IRDDIPAITSQELQR  IPAITSQEL 0.4681 316 WB BK VP2-3 DRB1_0701 170 RDDIPAITSQELQRR  IPAITSQEL 0.4671 319 WB BK VP2-3 DRB1_0701 171 DDIPAITSQELQRRT  IPAITSQEL 0.4635 332 WB BK VP2-3 DRB1_0701 129 EYYDILFPGVNTFVN  LFPGVNTFV 0.4503 383 WB BK VP2-3 DRB1_0701 130 YYDILFPGVNTFVNN  FPGVNTFVN 0.4488 389 WB BK VP2-3 DRB1_0701 133 ILFPGVNTFVNNIQY  FPGVNTFVN 0.4334 459 WB BK VP2-3 DRB1_0701 158 FATISQALWHVIRDD  ISQALWHVI 0.4279 488 WB BK VP2-3 DRB1_0802 214 YIQDYYSNLSPIRPS  YSNLSPIRP 0.4370 442 WB BK VP2-3 DRB1_0802 213 NYIQDYYSNLSPIRP  YYSNLSPIR 0.4360 447 WB BK VP2-3 DRB1_0802 215 IQDYYSNLSPIRPSM  YSNLSPIRP 0.4360 447 WB BK VP2-3 DRB1_0802 216 QDYYSNLSPIRPSMV  YSNLSPIRP 0.4358 448 WB BK VP2-3 DRB1_0901 110 STVGLYQQSGMALEL  YQQSGMALE 0.4827 270 WB BK VP2-3 DRB1_0901 111 TVGLYQQSGMALELF  YQQSGMALE 0.4750 293 WB BK VP2-3 DRB1_0901 112 VGLYQQSGMALELFN  YQQSGMALE 0.4750 293 WB BK VP2-3 DRB1_0901 109 VSTVGLYQQSGMALE  LYQQSGMAL 0.4737 297 WB BK VP2-3 DRB1_0901 36 AAIEVQIASLATVEG  VQIASLATV 0.4709 306 WB BK VP2-3 DRB1_0901 35 AAAIEVQIASLATVE  VQIASLATV 0.4664 322 WB BK VP2-3 DRB1_0901 198 EETTWTIVNAPINFY  WTIVNAPIN 0.4656 324 WB BK VP2-3 DRB1_0901 199 ETTWTIVNAPINFYN  WTIVNAPIN 0.4657 324 WB BK VP2-3 DRB1_0901 37 AIEVQIASLATVEGI  VQIASLATV 0.4650 326 WB BK VP2-3 DRB1_0901 34 AAAAIEVQIASLATV  IEVQIASLA 0.4647 328 WB BK VP2-3 DRB1_0901 38 IEVQIASLATVEGIT  VQIASLATV 0.4639 331 WB BK VP2-3 DRB1_0901 297 LLLGLYGTVTPALEA  LYGTVTPAL 0.4627 335 WB BK VP2-3 DRB1_0901 200 TTWTIVNAPINFYNY  WTIVNAPIN 0.4612 340 WB BK VP2-3 DRB1_0901 296 PLLLGLYGTVTPALE  LYGTVTPAL 0.4611 341 WB BK VP2-3 DRB1_0901 299 LGLYGTVTPALEAYE  LYGTVTPAL 0.4598 346 WB BK VP2-3 DRB1_0901 298 LLGLYGTVTPALEAY  LYGTVTPAL 0.4531 372 WB BK VP2-3 DRB1_0901 113 GLYQQSGMALELFNP  YQQSGMALE 0.4451 405 WB BK VP2-3 DRB1_0901 183 RRTERFFRDSLARFL  FFRDSLARF 0.4413 422 WB BK VP2-3 DRB1_0901 184 RTERFFRDSLARFLE  FRDSLARFL 0.4404 426 WB BK VP2-3 DRB1_0901 186 ERFFRDSLARFLEET  FRDSLARFL 0.4393 431 WB BK VP2-3 DRB1_0901 185 TERFFRDSLARFLEE  FRDSLARFL 0.4382 436 WB BK VP2-3 DRB1_0901 187 RFFRDSLARFLEETT  FRDSLARFL 0.4306 474 WB BK VP2-3 DRB1_0901 295 LPLLLGLYGTVTPAL  LGLYGTVTP 0.4290 482 WB BK VP2-3 DRB1_0901 65 PQTYAVIAGAPGAIA  VIAGAPGAI 0.4281 487 WB BK VP2-3 DRB1_0901 66 QTYAVIAGAPGAIAG  VIAGAPGAI 0.4279 488 WB BK VP2-3 DRB1_0901 67 TYAVIAGAPGAIAGF  VIAGAPGAI 0.4259 499 WB BK VP2-3 DRB1_1302 135 FPGVNTFVNNIQYLD  VNTFVNNIQ 0.7008 25 SB BK VP2-3 DRB1_1302 136 PGVNTFVNNIQYLDP  FVNNIQYLD 0.6940 27 SB BK VP2-3 DRB1_1302 137 GVNTFVNNIQYLDPR  FVNNIQYLD 0.6861 30 SB BK VP2-3 DRB1_1302 138 VNTFVNNIQYLDPRH  FVNNIQYLD 0.6825 31 SB BK VP2-3 DRB1_1302 139 NTFVNNIQYLDPRHW  FVNNIQYLD 0.6608 39 SB BK VP2-3 DRB1_1302 213 NYIQDYYSNLSPIRP  IQDYYSNLS 0.6338 53 WB BK VP2-3 DRB1_1302 216 QDYYSNLSPIRPSMV  YSNLSPIRP 0.6265 57 WB BK VP2-3 DRB1_1302 215 IQDYYSNLSPIRPSM  YSNLSPIRP 0.6245 58 WB BK VP2-3 DRB1_1302 214 YIQDYYSNLSPIRPS  YSNLSPIRP 0.6230 59 WB BK VP2-3 DRB1_1302 217 DYYSNLSPIRPSMVR  YSNLSPIRP 0.6216 60 WB BK VP2-3 DRB1_1302 293 WMLPLLLGLYGTVTP  LLGLYGTVT 0.6200 61 WB BK VP2-3 DRB1_1302 296 PLLLGLYGTVTPALE  LGLYGTVTP 0.6167 63 WB BK VP2-3 DRB1_1302 294 MLPLLLGLYGTVTPA  LGLYGTVTP 0.6126 66 WB BK VP2-3 DRB1_1302 295 LPLLLGLYGTVTPAL  LGLYGTVTP 0.6083 69 WB BK VP2-3 DRB1_1302 297 LLLGLYGTVTPALEA  LGLYGTVTP 0.6067 70 WB BK VP2-3 DRB1_1302 140 TFVNNIQYLDPRHWG  FVNNIQYLD 0.5962 79 WB BK VP2-3 DRB1_1302 36 AAIEVQIASLATVEG  VQIASLATV 0.5884 86 WB BK VP2-3 DRB1_1302 141 FVNNIQYLDPRHWGP  FVNNIQYLD 0.5710 104 WB BK VP2-3 DRB1_1302 37 AIEVQIASLATVEGI  VQIASLATV 0.5647 111 WB BK VP2-3 DRB1_1302 38 IEVQIASLATVEGIT  VQIASLATV 0.5646 111 WB BK VP2-3 DRB1_1302 218 YYSNLSPIRPSMVRQ  YSNLSPIRP 0.5481 133 WB BK VP2-3 DRB1_1302 199 ETTWTIVNAPINFYN  IVNAPINFY 0.5463 135 WB BK VP2-3 DRB1_1302 200 TTWTIVNAPINFYNY  IVNAPINFY 0.5452 137 WB BK VP2-3 DRB1_1302 198 EETTWTIVNAPINFY  WTIVNAPIN 0.5445 138 WB BK VP2-3 DRB1_1302 298 LLGLYGTVTPALEAY  LGLYGTVTP 0.5383 148 WB BK VP2-3 DRB1_1302 219 YSNLSPIRPSMVRQV  YSNLSPIRP 0.5366 150 WB BK VP2-3 DRB1_1302 201 TWTIVNAPINFYNYI  IVNAPINFY 0.5349 153 WB BK VP2-3 DRB1_1302 79 AGFAALIQTVTGISS  FAALIQTVT 0.5306 161 WB BK VP2-3 DRB1_1302 34 AAAAIEVQIASLATV  IEVQIASLA 0.5257 169 WB BK VP2-3 DRB1_1302 202 WTIVNAPINFYNYIQ  IVNAPINFY 0.5240 172 WB BK VP2-3 DRB1_1302 35 AAAIEVQIASLATVE  VQIASLATV 0.5233 174 WB BK VP2-3 DRB1_1302 299 LGLYGTVTPALEAYE  LGLYGTVTP 0.5095 202 WB BK VP2-3 DRB1_1302 40 VQIASLATVEGITTT  IASLATVEG 0.5094 202 WB BK VP2-3 DRB1_1302 80 GFAALIQTVTGISSL  IQTVTGISS 0.5080 205 WB BK VP2-3 DRB1_1302 39 EVQIASLATVEGITT  IASLATVEG 0.5076 206 WB BK VP2-3 DRB1_1302 81 FAALIQTVTGISSLA  IQTVTGISS 0.5054 211 WB BK VP2-3 DRB1_1302 78 IAGFAALIQTVTGIS  FAALIQTVT 0.4783 283 WB BK VP2-3 DRB1_1302 82 AALIQTVTGISSLAQ  IQTVTGISS 0.4693 312 WB BK VP2-3 DRB1_1302 83 ALIQTVTGISSLAQV  IQTVTGISS 0.4437 411 WB BK VP2-3 DRB1_1302 109 VSTVGLYQQSGMALE  VGLYQQSGM 0.4417 420 WB BK VP2-3 DRB1_1302 132 DILFPGVNTFVNNIQ  FPGVNTFVN 0.4394 431 WB BK VP2-3 DRB1_1302 133 ILFPGVNTFVNNIQY  VNTFVNNIQ 0.4339 457 WB BK VP2-3 DRB1_1302 203 TIVNAPINFYNYIQD  IVNAPINFY 0.4317 468 WB BK VP2-3 DRB1_1302 110 STVGLYQQSGMALEL  VGLYQQSGM 0.4274 490 WB BK VP2-3 DRB1_1501 259 TQRMDLRNKESVHSG  LRNKESVHS 0.5055 211 WB BK VP2-3 DRB1_1501 258 VTQRMDLRNKESVHS  TQRMDLRNK 0.4963 233 WB BK VP2-3 DRB1_1501 260 QRMDLRNKESVHSGE  LRNKESVHS 0.4888 252 WB BK VP2-3 DRB1_1501 261 RMDLRNKESVHSGEF  LRNKESVHS 0.4818 272 WB BK VP2-3 DRB1_1501 292 QWMLPLLLGLYGTVT  MLPLLLGLY 0.4818 272 WB BK VP2-3 DRB1_1501 293 WMLPLLLGLYGTVTP  LLGLYGTVT 0.4703 308 WB BK VP2-3 DRB1_1501 262 MDLRNKESVHSGEFI  LRNKESVHS 0.4652 326 WB BK VP2-3 DRB1_1501 294 MLPLLLGLYGTVTPA  LLGLYGTVT 0.4567 357 WB BK VP2-3 DRB1_1501 295 LPLLLGLYGTVTPAL  LLGLYGTVT 0.4514 378 WB BK VP2-3 DRB1_1501 296 PLLLGLYGTVTPALE  LLGLYGTVT 0.4387 434 WB BK VP2-3 DRB4_0101 213 NYIQDYYSNLSPIRP  IQDYYSNLS 0.4336 458 WB BK VP2-3 DRB5_0101 216 QDYYSNLSPIRPSMV  YYSNLSPIR 0.5417 142 WB BK VP2-3 DRB5_0101 214 YIQDYYSNLSPIRPS  YSNLSPIRP 0.5315 159 WB BK VP2-3 DRB5_0101 215 IQDYYSNLSPIRPSM  YSNLSPIRP 0.5316 159 WB BK VP2-3 DRB5_0101 213 NYIQDYYSNLSPIRP  YYSNLSPIR 0.5308 160 WB BK VP2-3 DRB5_0101 217 DYYSNLSPIRPSMVR  YSNLSPIRP 0.5081 205 WB BK VP2-3 DRB5_0101 218 YYSNLSPIRPSMVRQ  YYSNLSPIR 0.4623 336 WB BK VP2-3 DRB5_0101 174 PAITSQELQRRTERF  ITSQELQRR 0.4449 406 WB BK VP2-3 DRB5_0101 173 IPAITSQELQRRTER  ITSQELQRR 0.4422 418 WB BK VP2-3 SEQ ID NOS.: 58312-59135

Preferred BK virus fragments of VP1 capable of interacting with one or more MHC class 2 molecules are listed in Table Q.

TABLE Q Prediction of BK virus VP1 protein specific MHC class 2, 15-mer peptide binders for 14 MHC class 2 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHCII/ database. The MHC class 2 molecules for which no binders were found are not listed. Bind Identity Allel pos peptide  core 1-log50k(aff) aff(nM) level DRB1_0101 164 QGVLMNYRTKYPQGT  LMNYRTKYP 0.7782 11 SB VP1 DRB1_0101 165 GVLMNYRTKYPQGTI  YRTKYPQGT 0.7768 11 SB VP1 DRB1_0101 166 VLMNYRTKYPQGTIT  YRTKYPQGT 0.7796 11 SB VP1 DRB1_0101 167 LMNYRTKYPQGTITP  YRTKYPQGT 0.7798 11 SB VP1 DRB1_0101 168 MNYRTKYPQGTITPK  YRTKYPQGT 0.7778 11 SB VP1 DRB1_0101 118 KTEVIGITSMLNLHA  VIGITSMLN 0.7623 13 SB VP1 DRB1_0101 119 TEVIGITSMLNLHAG  VIGITSMLN 0.7621 13 SB VP1 DRB1_0101 233 PPVLHVTNTATTVLL  VTNTATTVL 0.7280 19 SB VP1 DRB1_0101 234 PVLHVTNTATTVLLD  VTNTATTVL 0.7252 20 SB VP1 DRB1_0101 235 VLHVTNTATTVLLDE  VTNTATTVL 0.7244 20 SB VP1 DRB1_0101 232 VPPVLHVTNTATTVL  VLHVTNTAT 0.7197 21 SB VP1 DRB1_0101 236 LHVTNTATTVLLDEQ  VTNTATTVL 0.7207 21 SB VP1 DRB1_0101 121 VIGITSMLNLHAGSQ  VIGITSMLN 0.7107 23 SB VP1 DRB1_0101 120 EVIGITSMLNLHAGS  VIGITSMLN 0.7035 25 SB VP1 DRB1_0101 266 ADICGLFTNSSGTQQ  ICGLFTNSS 0.7009 25 SB VP1 DRB1_0101 262 YVSAADICGLFTNSS  YVSAADICG 0.6956 27 SB VP1 DRB1_0101 117 VKTEVIGITSMLNLH  VIGITSMLN 0.6913 28 SB VP1 DRB1_0101 116 TVKTEVIGITSMLNL  VIGITSMLN 0.6903 29 SB VP1 DRB1_0101 115 VTVKTEVIGITSMLN  EVIGITSML 0.6842 30 SB VP1 DRB1_0101 169 NYRTKYPQGTITPKN  YRTKYPQGT 0.6853 30 SB VP1 DRB1_0101 265 AADICGLFTNSSGTQ  ICGLFTNSS 0.6859 30 SB VP1 DRB1_0101 170 YRTKYPQGTITPKNP  YRTKYPQGT 0.6835 31 SB VP1 DRB1_0101 264 SAADICGLFTNSSGT  ICGLFTNSS 0.6829 31 SB VP1 DRB1_0101 263 VSAADICGLFTNSSG  ICGLFTNSS 0.6809 32 SB VP1 DRB1_0101 305 FLLSDLINRRTQKVD  LINRRTQKV 0.6730 34 SB VP1 DRB1_0101 304 SFLLSDLINRRTQKV  LSDLINRRT 0.6723 35 SB VP1 DRB1_0101 105 TCGNLLMWEAVTVKT  LLMWEAVTV 0.6651 37 SB VP1 DRB1_0101 106 CGNLLMWEAVTVKTE  LLMWEAVTV 0.6660 37 SB VP1 DRB1_0101 107 GNLLMWEAVTVKTEV  LLMWEAVTV 0.6675 37 SB VP1 DRB1_0101 306 LLSDLINRRTQKVDG  LINRRTQKV 0.6610 39 SB VP1 DRB1_0101 307 LSDLINRRTQKVDGQ  LINRRTQKV 0.6620 39 SB VP1 DRB1_0101 308 SDLINRRTQKVDGQP  LINRRTQKV 0.6493 44 SB VP1 DRB1_0101 122 IGITSMLNLHAGSQK  ITSMLNLHA 0.6472 45 SB VP1 DRB1_0101 108 NLLMWEAVTVKTEVI  MWEAVTVKT 0.6381 50 WB VP1 DRB1_0101 237 HVTNTATTVLLDEQG  VTNTATTVL 0.6362 51 WB VP1 DRB1_0101 267 DICGLFTNSSGTQQW  ICGLFTNSS 0.6283 56 WB VP1 DRB1_0101 268 ICGLFTNSSGTQQWR  ICGLFTNSS 0.6286 56 WB VP1 DRB1_0101 104 LTCGNLLMWEAVTVK  LLMWEAVTV 0.6269 57 WB VP1 DRB1_0101 317 KVDGQPMYGMESQVE  VDGQPMYGM 0.6232 59 WB VP1 DRB1_0101 318 VDGQPMYGMESQVEE  MYGMESQVE 0.6230 59 WB VP1 DRB1_0101 238 VTNTATTVLLDEQGV  VTNTATTVL 0.6202 61 WB VP1 DRB1_0101 252 VGPLCKADSLYVSAA  LCKADSLYV 0.6161 64 WB VP1 DRB1_0101 253 GPLCKADSLYVSAAD  LCKADSLYV 0.6146 65 WB VP1 DRB1_0101 250 QGVGPLCKADSLYVS  LCKADSLYV 0.6129 66 WB VP1 DRB1_0101 251 GVGPLCKADSLYVSA  LCKADSLYV 0.6115 67 WB VP1 DRB1_0101 109 LLMWEAVTVKTEVIG  MWEAVTVKT 0.6104 68 WB VP1 DRB1_0101 249 EQGVGPLCKADSLYV  VGPLCKADS 0.6000 76 WB VP1 DRB1_0101 123 GITSMLNLHAGSQKV  ITSMLNLHA 0.5940 81 WB VP1 DRB1_0101 124 ITSMLNLHAGSQKVH  ITSMLNLHA 0.5895 85 WB VP1 DRB1_0101 320 GQPMYGMESQVEEVR  MYGMESQVE 0.5805 94 WB VP1 DRB1_0101 103 DLTCGNLLMWEAVTV  LTCGNLLMW 0.5786 96 WB VP1 DRB1_0101 319 DGQPMYGMESQVEEV  MYGMESQVE 0.5779 96 WB VP1 DRB1_0101 315 TQKVDGQPMYGMESQ  VDGQPMYGM 0.5631 113 WB VP1 DRB1_0101 309 DLINRRTQKVDGQPM  LINRRTQKV 0.5612 115 WB VP1 DRB1_0101 314 RTQKVDGQPMYGMES  VDGQPMYGM 0.5605 116 WB VP1 DRB1_0101 316 QKVDGQPMYGMESQV  VDGQPMYGM 0.5604 116 WB VP1 DRB1_0101 321 QPMYGMESQVEEVRV  MYGMESQVE 0.5604 116 WB VP1 DRB1_0101 310 LINRRTQKVDGQPMY  LINRRTQKV 0.5595 117 WB VP1 DRB1_0101 161 LEMQGVLMNYRTKYP  MQGVLMNYR 0.5570 121 WB VP1 DRB1_0101 158 GDPLEMQGVLMNYRT  MQGVLMNYR 0.5484 132 WB VP1 DRB1_0101 256 CKADSLYVSAADICG  ADSLYVSAA 0.5470 135 WB VP1 DRB1_0101 257 KADSLYVSAADICGL  YVSAADICG 0.5462 136 WB VP1 DRB1_0101 84 RKMLPCYSTARIPLP  RKMLPCYST 0.5450 137 WB VP1 DRB1_0101 258 ADSLYVSAADICGLF  YVSAADICG 0.5446 138 WB VP1 DRB1_0101 259 DSLYVSAADICGLFT  YVSAADICG 0.5443 138 WB VP1 DRB1_0101 159 DPLEMQGVLMNYRTK  MQGVLMNYR 0.5441 139 WB VP1 DRB1_0101 260 SLYVSAADICGLFTN  YVSAADICG 0.5396 146 WB VP1 DRB1_0101 81 SPDRKMLPCYSTARI  RKMLPCYST 0.5323 158 WB VP1 DRB1_0101 110 LMWEAVTVKTEVIGI  MWEAVTVKT 0.5308 160 WB VP1 DRB1_0101 231 NVPPVLHVTNTATTV  LHVTNTATT 0.5288 164 WB VP1 DRB1_0101 177 GTITPKNPTAQSQVM  ITPKNPTAQ 0.5283 165 WB VP1 DRB1_0101 82 PDRKMLPCYSTARIP  RKMLPCYST 0.5256 170 WB VP1 DRB1_0101 254 PLCKADSLYVSAADI  LCKADSLYV 0.5231 174 WB VP1 DRB1_0101 162 EMQGVLMNYRTKYPQ  LMNYRTKYP 0.5203 179 WB VP1 DRB1_0101 80 DSPDRKMLPCYSTAR  RKMLPCYST 0.5206 179 WB VP1 DRB1_0101 255 LCKADSLYVSAADIC  LCKADSLYV 0.5180 184 WB VP1 DRB1_0101 294 KRSVKNPYPISFLLS  VKNPYPISF 0.5180 184 WB VP1 DRB1_0101 313 RRTQKVDGQPMYGME  VDGQPMYGM 0.5170 186 WB VP1 DRB1_0101 157 GGDPLEMQGVLMNYR  LEMQGVLMN 0.5164 187 WB VP1 DRB1_0101 295 RSVKNPYPISFLLSD  VKNPYPISF 0.5161 188 WB VP1 DRB1_0101 312 NRRTQKVDGQPMYGM  KVDGQPMYG 0.5163 188 WB VP1 DRB1_0101 160 PLEMQGVLMNYRTKY  MQGVLMNYR 0.5148 190 WB VP1 DRB1_0101 269 CGLFTNSSGTQQWRG  FTNSSGTQQ 0.5138 193 WB VP1 DRB1_0101 292 LRKRSVKNPYPISFL  VKNPYPISF 0.5094 202 WB VP1 DRB1_0101 163 MQGVLMNYRTKYPQG  LMNYRTKYP 0.5072 207 WB VP1 DRB1_0101 230 ENVPPVLHVTNTATT  VLHVTNTAT 0.5053 211 WB VP1 DRB1_0101 293 RKRSVKNPYPISFLL  VKNPYPISF 0.5053 211 WB VP1 DRB1_0101 270 GLFTNSSGTQQWRGL  FTNSSGTQQ 0.5035 215 WB VP1 DRB1_0101 175 PQGTITPKNPTAQSQ  ITPKNPTAQ 0.5026 217 WB VP1 DRB1_0101 176 QGTITPKNPTAQSQV  ITPKNPTAQ 0.5007 222 WB VP1 DRB1_0101 291 RLRKRSVKNPYPISF  LRKRSVKNP 0.5005 222 WB VP1 DRB1_0101 125 TSMLNLHAGSQKVHE  MLNLHAGSQ 0.4968 231 WB VP1 DRB1_0101 62 DNLRGYSQHLSAENA  LRGYSQHLS 0.4929 241 WB VP1 DRB1_0101 83 DRKMLPCYSTARIPL  MLPCYSTAR 0.4902 249 WB VP1 DRB1_0101 87 LPCYSTARIPLPNLN  YSTARIPLP 0.4891 252 WB VP1 DRB1_0101 85 KMLPCYSTARIPLPN  YSTARIPLP 0.4865 259 WB VP1 DRB1_0101 349 IRYIDRQGQLQTKMV  YIDRQGQLQ 0.4856 261 WB VP1 DRB1_0101 111 MWEAVTVKTEVIGIT  MWEAVTVKT 0.4847 264 WB VP1 DRB1_0101 88 PCYSTARIPLPNLNE  YSTARIPLP 0.4819 272 WB VP1 DRB1_0101 86 MLPCYSTARIPLPNL  YSTARIPLP 0.4817 273 WB VP1 DRB1_0101 23 VQVPKLLIKGGVEVL  LLIKGGVEV 0.4803 277 WB VP1 DRB1_0101 61 DDNLRGYSQHLSAEN  LRGYSQHLS 0.4800 278 WB VP1 DRB1_0101 179 ITPKNPTAQSQVMNT  ITPKNPTAQ 0.4786 282 WB VP1 DRB1_0101 285 ARYFKIRLRKRSVKN  FKIRLRKRS 0.4787 282 WB VP1 DRB1_0101 155 AVGGDPLEMQGVLMN  GDPLEMQGV 0.4780 284 WB VP1 DRB1_0101 284 LARYFKIRLRKRSVK  FKIRLRKRS 0.4764 289 WB VP1 DRB1_0101 178 TITPKNPTAQSQVMN  ITPKNPTAQ 0.4755 291 WB VP1 DRB1_0101 282 RGLARYFKIRLRKRS  YFKIRLRKR 0.4754 292 WB VP1 DRB1_0101 283 GLARYFKIRLRKRSV  FKIRLRKRS 0.4744 295 WB VP1 DRB1_0101 173 KYPQGTITPKNPTAQ  PQGTITPKN 0.4716 304 WB VP1 DRB1_0101 174 YPQGTITPKNPTAQS  ITPKNPTAQ 0.4716 304 WB VP1 DRB1_0101 224 GTYTGGENVPPVLHV  YTGGENVPP 0.4697 310 WB VP1 DRB1_0101 322 PMYGMESQVEEVRVF  MYGMESQVE 0.4691 312 WB VP1 DRB1_0101 156 VGGDPLEMQGVLMNY  LEMQGVLMN 0.4685 314 WB VP1 DRB1_0101 25 VPKLLIKGGVEVLEV  LLIKGGVEV 0.4678 317 WB VP1 DRB1_0101 24 QVPKLLIKGGVEVLE  LLIKGGVEV 0.4674 318 WB VP1 DRB1_0101 22 PVQVPKLLIKGGVEV  VPKLLIKGG 0.4668 320 WB VP1 DRB1_0101 261 LYVSAADICGLFTNS  YVSAADICG 0.4665 321 WB VP1 DRB1_0101 26 PKLLIKGGVEVLEVK  LLIKGGVEV 0.4633 332 WB VP1 DRB1_0101 151 FHFFAVGGDPLEMQG  VGGDPLEMQ 0.4633 333 WB VP1 DRB1_0101 323 MYGMESQVEEVRVFD  MYGMESQVE 0.4626 335 WB VP1 DRB1_0101 150 NFHFFAVGGDPLEMQ  AVGGDPLEM 0.4611 340 WB VP1 DRB1_0101 223 FGTYTGGENVPPVLH  YTGGENVPP 0.4596 346 WB VP1 DRB1_0101 297 VKNPYPISFLLSDLI  VKNPYPISF 0.4588 349 WB VP1 DRB1_0101 63 NLRGYSQHLSAENAF  YSQHLSAEN 0.4583 351 WB VP1 DRB1_0101 152 HFFAVGGDPLEMQGV  VGGDPLEMQ 0.4576 354 WB VP1 DRB1_0101 286 RYFKIRLRKRSVKNP  FKIRLRKRS 0.4564 358 WB VP1 DRB1_0101 64 LRGYSQHLSAENAFE  YSQHLSAEN 0.4559 360 WB VP1 DRB1_0101 220 TRYFGTYTGGENVPP  YFGTYTGGE 0.4546 365 WB VP1 DRB1_0101 301 YPISFLLSDLINRRT  ISFLLSDLI 0.4540 368 WB VP1 DRB1_0101 126 SMLNLHAGSQKVHEN  MLNLHAGSQ 0.4520 376 WB VP1 DRB1_0101 34 VEVLEVKTGVDAITE  VKTGVDAIT 0.4507 381 WB VP1 DRB1_0101 33 GVEVLEVKTGVDAIT  VEVLEVKTG 0.4499 385 WB VP1 DRB1_0101 226 YTGGENVPPVLHVTN  YTGGENVPP 0.4471 397 WB VP1 DRB1_0101 303 ISFLLSDLINRRTQK  LSDLINRRT 0.4468 397 WB VP1 DRB1_0101 153 FFAVGGDPLEMQGVL  VGGDPLEMQ 0.4446 407 WB VP1 DRB1_0101 225 TYTGGENVPPVLHVT  YTGGENVPP 0.4439 410 WB VP1 DRB1_0101 302 PISFLLSDLINRRTQ  LSDLINRRT 0.4439 411 WB VP1 DRB1_0101 36 VLEVKTGVDAITEVE  VKTGVDAIT 0.4399 429 WB VP1 DRB1_0101 35 EVLEVKTGVDAITEV  VKTGVDAIT 0.4395 430 WB VP1 DRB1_0101 37 LEVKTGVDAITEVEC  VKTGVDAIT 0.4381 437 WB VP1 DRB1_0101 127 MLNLHAGSQKVHENG  MLNLHAGSQ 0.4375 440 WB VP1 DRB1_0101 229 GENVPPVLHVTNTAT  NVPPVLHVT 0.4368 443 WB VP1 DRB1_0101 60 PDDNLRGYSQHLSAE  LRGYSQHLS 0.4346 454 WB VP1 DRB1_0101 59 DPDDNLRGYSQHLSA  LRGYSQHLS 0.4337 458 WB VP1 DRB1_0101 65 RGYSQHLSAENAFES  YSQHLSAEN 0.4335 459 WB VP1 DRB1_0101 27 KLLIKGGVEVLEVKT  LIKGGVEVL 0.4331 461 WB VP1 DRB1_0101 221 RYFGTYTGGENVPPV  YTGGENVPP 0.4318 468 WB VP1 DRB1_0101 296 SVKNPYPISFLLSDL  VKNPYPISF 0.4317 468 WB VP1 DRB1_0101 222 YFGTYTGGENVPPVL  YTGGENVPP 0.4313 470 WB VP1 DRB1_0101 271 LFTNSSGTQQWRGLA  FTNSSGTQQ 0.4313 470 WB VP1 DRB1_0101 58 GDPDDNLRGYSQHLS  NLRGYSQHL 0.4305 474 WB VP1 DRB1_0101 281 WRGLARYFKIRLRKR  WRGLARYFK 0.4285 485 WB VP1 DRB1_0101 276 SGTQQWRGLARYFKI  WRGLARYFK 0.4263 496 WB VP1 DRB1_0101 154 FAVGGDPLEMQGVLM  VGGDPLEMQ 0.4261 498 WB VP1 DRB1_0101 277 GTQQWRGLARYFKIR  WRGLARYFK 0.4259 498 WB VP1 DRB1_0101 275 SSGTQQWRGLARYFK  QQWRGLARY 0.4258 499 WB VP1 DRB1_0401 118 KTEVIGITSMLNLHA  VIGITSMLN 0.5278 165 WB VP1 DRB1_0401 119 TEVIGITSMLNLHAG  ITSMLNLHA 0.5243 172 WB VP1 DRB1_0401 266 ADICGLFTNSSGTQQ  ICGLFTNSS 0.5078 206 WB VP1 DRB1_0401 265 AADICGLFTNSSGTQ  ICGLFTNSS 0.5038 215 WB VP1 DRB1_0401 120 EVIGITSMLNLHAGS  ITSMLNLHA 0.4938 239 WB VP1 DRB1_0401 121 VIGITSMLNLHAGSQ  ITSMLNLHA 0.4931 241 WB VP1 DRB1_0401 262 YVSAADICGLFTNSS  YVSAADICG 0.4874 256 WB VP1 DRB1_0401 264 SAADICGLFTNSSGT  ICGLFTNSS 0.4849 263 WB VP1 DRB1_0401 263 VSAADICGLFTNSSG  ICGLFTNSS 0.4805 276 WB VP1 DRB1_0401 287 YFKIRLRKRSVKNPY  RLRKRSVKN 0.4585 350 WB VP1 DRB1_0401 304 SFLLSDLINRRTQKV  LLSDLINRR 0.4554 362 WB VP1 DRB1_0401 288 FKIRLRKRSVKNPYP  RKRSVKNPY 0.4485 390 WB VP1 DRB1_0401 122 IGITSMLNLHAGSQK  ITSMLNLHA 0.4473 395 WB VP1 DRB1_0401 291 RLRKRSVKNPYPISF  RKRSVKNPY 0.4444 408 WB VP1 DRB1_0401 232 VPPVLHVTNTATTVL  PVLHVTNTA 0.4431 414 WB VP1 DRB1_0401 115 VTVKTEVIGITSMLN  VKTEVIGIT 0.4422 418 WB VP1 DRB1_0401 289 KIRLRKRSVKNPYPI  RKRSVKNPY 0.4410 424 WB VP1 DRB1_0401 117 VKTEVIGITSMLNLH  VIGITSMLN 0.4404 426 WB VP1 DRB1_0401 268 ICGLFTNSSGTQQWR  ICGLFTNSS 0.4395 430 WB VP1 DRB1_0401 267 DICGLFTNSSGTQQW  ICGLFTNSS 0.4385 435 WB VP1 DRB1_0401 230 ENVPPVLHVTNTATT  PVLHVTNTA 0.4370 442 WB VP1 DRB1_0401 290 IRLRKRSVKNPYPIS  RKRSVKNPY 0.4334 460 WB VP1 DRB1_0401 231 NVPPVLHVTNTATTV  PVLHVTNTA 0.4332 461 WB VP1 DRB1_0401 301 YPISFLLSDLINRRT  LLSDLINRR 0.4287 483 WB VP1 DRB1_0401 116 TVKTEVIGITSMLNL  VIGITSMLN 0.4285 485 WB VP1 DRB1_0401 300 PYPISFLLSDLINRR  ISFLLSDLI 0.4265 495 WB VP1 DRB1_0404 121 VIGITSMLNLHAGSQ  ITSMLNLHA 0.6731 34 SB VP1 DRB1_0404 122 IGITSMLNLHAGSQK  MLNLHAGSQ 0.6665 37 SB VP1 DRB1_0404 124 ITSMLNLHAGSQKVH  MLNLHAGSQ 0.6499 44 SB VP1 DRB1_0404 123 GITSMLNLHAGSQKV  MLNLHAGSQ 0.6491 45 SB VP1 DRB1_0404 163 MQGVLMNYRTKYPQG  LMNYRTKYP 0.6123 66 WB VP1 DRB1_0404 125 TSMLNLHAGSQKVHE  MLNLHAGSQ 0.6117 67 WB VP1 DRB1_0404 161 LEMQGVLMNYRTKYP  MQGVLMNYR 0.6109 67 WB VP1 DRB1_0404 164 QGVLMNYRTKYPQGT  LMNYRTKYP 0.6092 69 WB VP1 DRB1_0404 162 EMQGVLMNYRTKYPQ  LMNYRTKYP 0.6059 71 WB VP1 DRB1_0404 165 GVLMNYRTKYPQGTI  LMNYRTKYP 0.6046 72 WB VP1 DRB1_0404 126 SMLNLHAGSQKVHEN  MLNLHAGSQ 0.5148 190 WB VP1 DRB1_0404 127 MLNLHAGSQKVHENG  MLNLHAGSQ 0.5132 194 WB VP1 DRB1_0404 166 VLMNYRTKYPQGTIT  LMNYRTKYP 0.5108 199 WB VP1 DRB1_0404 266 ADICGLFTNSSGTQQ  ICGLFTNSS 0.5092 202 WB VP1 DRB1_0404 265 AADICGLFTNSSGTQ  ICGLFTNSS 0.5081 205 WB VP1 DRB1_0404 167 LMNYRTKYPQGTITP  LMNYRTKYP 0.5069 208 WB VP1 DRB1_0404 304 SFLLSDLINRRTQKV  LLSDLINRR 0.4931 241 WB VP1 DRB1_0404 301 YPISFLLSDLINRRT  LLSDLINRR 0.4876 256 WB VP1 DRB1_0404 119 TEVIGITSMLNLHAG  ITSMLNLHA 0.4851 263 WB VP1 DRB1_0404 302 PISFLLSDLINRRTQ  LLSDLINRR 0.4821 271 WB VP1 DRB1_0404 303 ISFLLSDLINRRTQK  LLSDLINRR 0.4816 273 WB VP1 DRB1_0404 118 KTEVIGITSMLNLHA  VIGITSMLN 0.4807 275 WB VP1 DRB1_0404 46 ITEVECFLNPEMGDP  TEVECFLNP 0.4807 275 WB VP1 DRB1_0404 47 TEVECFLNPEMGDPD  FLNPEMGDP 0.4801 277 WB VP1 DRB1_0404 48 EVECFLNPEMGDPDD  FLNPEMGDP 0.4754 292 WB VP1 DRB1_0404 50 ECFLNPEMGDPDDNL  FLNPEMGDP 0.4751 293 WB VP1 DRB1_0404 49 VECFLNPEMGDPDDN  FLNPEMGDP 0.4745 295 WB VP1 DRB1_0404 267 DICGLFTNSSGTQQW  LFTNSSGTQ 0.4682 315 WB VP1 DRB1_0404 268 ICGLFTNSSGTQQWR  LFTNSSGTQ 0.4665 321 WB VP1 DRB1_0404 84 RKMLPCYSTARIPLP  MLPCYSTAR 0.4629 334 WB VP1 DRB1_0404 105 TCGNLLMWEAVTVKT  LMWEAVTVK 0.4618 338 WB VP1 DRB1_0404 106 CGNLLMWEAVTVKTE  LMWEAVTVK 0.4597 346 WB VP1 DRB1_0404 232 VPPVLHVTNTATTVL  LHVTNTATT 0.4584 351 WB VP1 DRB1_0404 300 PYPISFLLSDLINRR  FLLSDLINR 0.4582 351 WB VP1 DRB1_0404 120 EVIGITSMLNLHAGS  ITSMLNLHA 0.4575 354 WB VP1 DRB1_0404 107 GNLLMWEAVTVKTEV  LMWEAVTVK 0.4552 363 WB VP1 DRB1_0404 233 PPVLHVTNTATTVLL  LHVTNTATT 0.4466 398 WB VP1 DRB1_0404 230 ENVPPVLHVTNTATT  VLHVTNTAT 0.4465 399 WB VP1 DRB1_0404 108 NLLMWEAVTVKTEVI  LMWEAVTVK 0.4456 403 WB VP1 DRB1_0404 305 FLLSDLINRRTQKVD  LLSDLINRR 0.4431 414 WB VP1 DRB1_0404 192 NTDHKAYLDKNNAYP  KAYLDKNNA 0.4422 418 WB VP1 DRB1_0404 193 TDHKAYLDKNNAYPV  YLDKNNAYP 0.4402 427 WB VP1 DRB1_0404 231 NVPPVLHVTNTATTV  LHVTNTATT 0.4401 428 WB VP1 DRB1_0404 194 DHKAYLDKNNAYPVE  YLDKNNAYP 0.4393 431 WB VP1 DRB1_0404 85 KMLPCYSTARIPLPN  YSTARIPLP 0.4335 459 WB VP1 DRB1_0404 234 PVLHVTNTATTVLLD  LHVTNTATT 0.4328 463 WB VP1 DRB1_0404 195 HKAYLDKNNAYPVEC  YLDKNNAYP 0.4303 476 WB VP1 DRB1_0404 196 KAYLDKNNAYPVECW  YLDKNNAYP 0.4288 483 WB VP1 DRB1_0404 104 LTCGNLLMWEAVTVK  LLMWEAVTV 0.4272 492 WB VP1 DRB1_0405 205 YPVECWIPDPSRNEN  WIPDPSRNE 0.4758 291 WB VP1 DRB1_0405 204 AYPVECWIPDPSRNE  ECWIPDPSR 0.4737 297 WB VP1 DRB1_0405 118 KTEVIGITSMLNLHA  VIGITSMLN 0.4649 327 WB VP1 DRB1_0405 119 TEVIGITSMLNLHAG  VIGITSMLN 0.4617 338 WB VP1 DRB1_0405 88 PCYSTARIPLPNLNE  YSTARIPLP 0.4515 378 WB VP1 DRB1_0405 206 PVECWIPDPSRNENT  WIPDPSRNE 0.4387 434 WB VP1 DRB1_0405 115 VTVKTEVIGITSMLN  TVKTEVIGI 0.4272 492 WB VP1 DRB1_0701 232 VPPVLHVTNTATTVL  VLHVTNTAT 0.7832 10 SB VP1 DRB1_0701 233 PPVLHVTNTATTVLL  VTNTATTVL 0.7867 10 SB VP1 DRB1_0701 234 PVLHVTNTATTVLLD  VTNTATTVL 0.7821 11 SB VP1 DRB1_0701 235 VLHVTNTATTVLLDE  VTNTATTVL 0.7792 11 SB VP1 DRB1_0701 236 LHVTNTATTVLLDEQ  VTNTATTVL 0.7807 11 SB VP1 DRB1_0701 237 HVTNTATTVLLDEQG  VTNTATTVL 0.6865 30 SB VP1 DRB1_0701 238 VTNTATTVLLDEQGV  VTNTATTVL 0.6833 31 SB VP1 DRB1_0701 304 SFLLSDLINRRTQKV  LSDLINRRT 0.5382 148 WB VP1 DRB1_0701 308 SDLINRRTQKVDGQP  LINRRTQKV 0.5370 150 WB VP1 DRB1_0701 305 FLLSDLINRRTQKVD  LINRRTQKV 0.5365 151 WB VP1 DRB1_0701 306 LLSDLINRRTQKVDG  LINRRTQKV 0.5340 155 WB VP1 DRB1_0701 307 LSDLINRRTQKVDGQ  LINRRTQKV 0.5332 156 WB VP1 DRB1_0701 231 NVPPVLHVTNTATTV  VLHVTNTAT 0.4751 293 WB VP1 DRB1_0701 107 GNLLMWEAVTVKTEV  LLMWEAVTV 0.4593 347 WB VP1 DRB1_0701 105 TCGNLLMWEAVTVKT  LLMWEAVTV 0.4539 368 WB VP1 DRB1_0701 106 CGNLLMWEAVTVKTE  LLMWEAVTV 0.4530 372 WB VP1 DRB1_0701 104 LTCGNLLMWEAVTVK  LLMWEAVTV 0.4517 377 WB VP1 DRB1_0701 103 DLTCGNLLMWEAVTV  LTCGNLLMW 0.4475 395 WB VP1 DRB1_0701 230 ENVPPVLHVTNTATT  VLHVTNTAT 0.4461 401 WB VP1 DRB1_0701 309 DLINRRTQKVDGQPM  LINRRTQKV 0.4383 436 WB VP1 DRB1_0701 310 LINRRTQKVDGQPMY  LINRRTQKV 0.4370 442 WB VP1 DRB1_0701 285 ARYFKIRLRKRSVKN  YFKIRLRKR 0.4289 483 WB VP1 DRB1_0701 249 EQGVGPLCKADSLYV  PLCKADSLY 0.4260 498 WB VP1 DRB1_0802 282 RGLARYFKIRLRKRS  RGLARYFKI 0.5826 91 WB VP1 DRB1_0802 283 GLARYFKIRLRKRSV  FKIRLRKRS 0.5827 91 WB VP1 DRB1_0802 284 LARYFKIRLRKRSVK  FKIRLRKRS 0.5824 92 WB VP1 DRB1_0802 285 ARYFKIRLRKRSVKN  FKIRLRKRS 0.5816 92 WB VP1 DRB1_0802 286 RYFKIRLRKRSVKNP  FKIRLRKRS 0.5825 92 WB VP1 DRB1_0802 287 YFKIRLRKRSVKNPY  FKIRLRKRS 0.4907 247 WB VP1 DRB1_0802 288 FKIRLRKRSVKNPYP  FKIRLRKRS 0.4905 248 WB VP1 DRB1_0901 84 RKMLPCYSTARIPLP  LPCYSTARI 0.5150 190 WB VP1 DRB1_0901 85 KMLPCYSTARIPLPN  YSTARIPLP 0.5124 195 WB VP1 DRB1_0901 86 MLPCYSTARIPLPNL  YSTARIPLP 0.4991 226 WB VP1 DRB1_0901 87 LPCYSTARIPLPNLN  YSTARIPLP 0.4968 231 WB VP1 DRB1_0901 88 PCYSTARIPLPNLNE  YSTARIPLP 0.4598 345 WB VP1 DRB1_1101 276 SGTQQWRGLARYFKI  WRGLARYFK 0.5202 180 WB VP1 DRB1_1101 277 GTQQWRGLARYFKIR  WRGLARYFK 0.5200 180 WB VP1 DRB1_1101 278 TQQWRGLARYFKIRL  WRGLARYFK 0.5165 187 WB VP1 DRB1_1101 275 SSGTQQWRGLARYFK  QQWRGLARY 0.5148 191 WB VP1 DRB1_1101 279 QQWRGLARYFKIRLR  WRGLARYFK 0.5146 191 WB VP1 DRB1_1101 281 WRGLARYFKIRLRKR  WRGLARYFK 0.4569 357 WB VP1 DRB1_1101 280 QWRGLARYFKIRLRK  WRGLARYFK 0.4404 426 WB VP1 DRB1_1302 161 LEMQGVLMNYRTKYP  VLMNYRTKY 0.6366 51 WB VP1 DRB1_1302 162 EMQGVLMNYRTKYPQ  VLMNYRTKY 0.6357 51 WB VP1 DRB1_1302 163 MQGVLMNYRTKYPQG  VLMNYRTKY 0.6190 62 WB VP1 DRB1_1302 164 QGVLMNYRTKYPQGT  VLMNYRTKY 0.6178 63 WB VP1 DRB1_1302 160 PLEMQGVLMNYRTKY  QGVLMNYRT 0.6118 67 WB VP1 DRB1_1302 233 PPVLHVTNTATTVLL  VTNTATTVL 0.6016 75 WB VP1 DRB1_1302 234 PVLHVTNTATTVLLD  VTNTATTVL 0.5831 91 WB VP1 DRB1_1302 232 VPPVLHVTNTATTVL  VLHVTNTAT 0.5808 93 WB VP1 DRB1_1302 235 VLHVTNTATTVLLDE  VTNTATTVL 0.5658 110 WB VP1 DRB1_1302 284 LARYFKIRLRKRSVK  FKIRLRKRS 0.5521 127 WB VP1 DRB1_1302 165 GVLMNYRTKYPQGTI  VLMNYRTKY 0.5482 133 WB VP1 DRB1_1302 285 ARYFKIRLRKRSVKN  FKIRLRKRS 0.5453 137 WB VP1 DRB1_1302 286 RYFKIRLRKRSVKNP  FKIRLRKRS 0.5448 138 WB VP1 DRB1_1302 287 YFKIRLRKRSVKNPY  IRLRKRSVK 0.5427 141 WB VP1 DRB1_1302 236 LHVTNTATTVLLDEQ  VTNTATTVL 0.5416 143 WB VP1 DRB1_1302 288 FKIRLRKRSVKNPYP  IRLRKRSVK 0.5351 153 WB VP1 DRB1_1302 117 VKTEVIGITSMLNLH  IGITSMLNL 0.5226 175 WB VP1 DRB1_1302 166 VLMNYRTKYPQGTIT  VLMNYRTKY 0.5220 176 WB VP1 DRB1_1302 116 TVKTEVIGITSMLNL  EVIGITSML 0.5120 196 WB VP1 DRB1_1302 282 RGLARYFKIRLRKRS  LARYFKIRL 0.4951 236 WB VP1 DRB1_1302 118 KTEVIGITSMLNLHA  IGITSMLNL 0.4947 237 WB VP1 DRB1_1302 283 GLARYFKIRLRKRSV  FKIRLRKRS 0.4916 245 WB VP1 DRB1_1302 304 SFLLSDLINRRTQKV  LLSDLINRR 0.4893 251 WB VP1 DRB1_1302 305 FLLSDLINRRTQKVD  LINRRTQKV 0.4877 255 WB VP1 DRB1_1302 119 TEVIGITSMLNLHAG  IGITSMLNL 0.4792 280 WB VP1 DRB1_1302 120 EVIGITSMLNLHAGS  IGITSMLNL 0.4786 282 WB VP1 DRB1_1302 91 STARIPLPNLNEDLT  ARIPLPNLN 0.4726 301 WB VP1 DRB1_1302 237 HVTNTATTVLLDEQG  VTNTATTVL 0.4703 308 WB VP1 DRB1_1302 95 IPLPNLNEDLTCGNL  LPNLNEDLT 0.4680 316 WB VP1 DRB1_1302 93 ARIPLPNLNEDLTCG  LPNLNEDLT 0.4675 318 WB VP1 DRB1_1302 94 RIPLPNLNEDLTCGN  LPNLNEDLT 0.4673 318 WB VP1 DRB1_1302 159 DPLEMQGVLMNYRTK  QGVLMNYRT 0.4669 320 WB VP1 DRB1_1302 92 TARIPLPNLNEDLTC  LPNLNEDLT 0.4645 328 WB VP1 DRB1_1302 158 GDPLEMQGVLMNYRT  LEMQGVLMN 0.4643 329 WB VP1 DRB1_1302 289 KIRLRKRSVKNPYPI  RKRSVKNPY 0.4576 354 WB VP1 DRB1_1302 290 IRLRKRSVKNPYPIS  RKRSVKNPY 0.4565 358 WB VP1 DRB1_1302 306 LLSDLINRRTQKVDG  LINRRTQKV 0.4527 373 WB VP1 DRB1_1302 122 IGITSMLNLHAGSQK  IGITSMLNL 0.4502 383 WB VP1 DRB1_1302 115 VTVKTEVIGITSMLN  VKTEVIGIT 0.4481 392 WB VP1 DRB1_1302 114 AVTVKTEVIGITSML  VKTEVIGIT 0.4425 417 WB VP1 DRB1_1302 238 VTNTATTVLLDEQGV  VTNTATTVL 0.4366 444 WB VP1 DRB1_1302 307 LSDLINRRTQKVDGQ  LINRRTQKV 0.4354 450 WB VP1 DRB1_1302 23 VQVPKLLIKGGVEVL  LLIKGGVEV 0.4322 466 WB VP1 DRB1_1302 266 ADICGLFTNSSGTQQ  LFTNSSGTQ 0.4320 466 WB VP1 DRB1_1302 267 DICGLFTNSSGTQQW  FTNSSGTQQ 0.4291 481 WB VP1 DRB1_1501 283 GLARYFKIRLRKRSV  YFKIRLRKR 0.6573 41 SB VP1 DRB1_1501 282 RGLARYFKIRLRKRS  YFKIRLRKR 0.6478 45 SB VP1 DRB1_1501 284 LARYFKIRLRKRSVK  YFKIRLRKR 0.6478 45 SB VP1 DRB1_1501 285 ARYFKIRLRKRSVKN  YFKIRLRKR 0.6480 45 SB VP1 DRB1_1501 281 WRGLARYFKIRLRKR  ARYFKIRLR 0.6307 54 WB VP1 DRB1_1501 286 RYFKIRLRKRSVKNP  YFKIRLRKR 0.5738 101 WB VP1 DRB1_1501 279 QQWRGLARYFKIRLR  WRGLARYFK 0.5664 109 WB VP1 DRB1_1501 287 YFKIRLRKRSVKNPY  YFKIRLRKR 0.5644 111 WB VP1 DRB1_1501 301 YPISFLLSDLINRRT  FLLSDLINR 0.5442 139 WB VP1 DRB1_1501 280 QWRGLARYFKIRLRK  ARYFKIRLR 0.5432 140 WB VP1 DRB1_1501 302 PISFLLSDLINRRTQ  FLLSDLINR 0.5326 157 WB VP1 DRB1_1501 303 ISFLLSDLINRRTQK  FLLSDLINR 0.5312 160 WB VP1 DRB1_1501 304 SFLLSDLINRRTQKV  LLSDLINRR 0.5284 165 WB VP1 DRB1_1501 300 PYPISFLLSDLINRR  FLLSDLINR 0.5247 171 WB VP1 DRB1_1501 305 FLLSDLINRRTQKVD  FLLSDLINR 0.5067 208 WB VP1 DRB1_1501 104 LTCGNLLMWEAVTVK  LLMWEAVTV 0.5050 212 WB VP1 DRB1_1501 105 TCGNLLMWEAVTVKT  LLMWEAVTV 0.5048 212 WB VP1 DRB1_1501 107 GNLLMWEAVTVKTEV  LLMWEAVTV 0.5033 216 WB VP1 DRB1_1501 106 CGNLLMWEAVTVKTE  LLMWEAVTV 0.5029 217 WB VP1 DRB1_1501 161 LEMQGVLMNYRTKYP  MQGVLMNYR 0.4970 231 WB VP1 DRB1_1501 278 TQQWRGLARYFKIRL  WRGLARYFK 0.4915 245 WB VP1 DRB1_1501 275 SSGTQQWRGLARYFK  TQQWRGLAR 0.4823 271 WB VP1 DRB1_1501 276 SGTQQWRGLARYFKI  TQQWRGLAR 0.4818 272 WB VP1 DRB1_1501 163 MQGVLMNYRTKYPQG  MQGVLMNYR 0.4769 287 WB VP1 DRB1_1501 299 NPYPISFLLSDLINR  ISFLLSDLI 0.4742 296 WB VP1 DRB1_1501 162 EMQGVLMNYRTKYPQ  MQGVLMNYR 0.4707 307 WB VP1 DRB1_1501 288 FKIRLRKRSVKNPYP  IRLRKRSVK 0.4578 353 WB VP1 DRB1_1501 277 GTQQWRGLARYFKIR  WRGLARYFK 0.4564 358 WB VP1 DRB1_1501 108 NLLMWEAVTVKTEVI  LLMWEAVTV 0.4524 374 WB VP1 DRB1_1501 160 PLEMQGVLMNYRTKY  MQGVLMNYR 0.4445 408 WB VP1 DRB1_1501 122 IGITSMLNLHAGSQK  ITSMLNLHA 0.4316 469 WB VP1 DRB4_0101 205 YPVECWIPDPSRNEN  VECWIPDPS 0.5233 174 WB VP1 DRB4_0101 203 NAYPVECWIPDPSRN  VECWIPDPS 0.5154 189 WB VP1 DRB4_0101 204 AYPVECWIPDPSRNE  VECWIPDPS 0.5145 191 WB VP1 DRB4_0101 202 NNAYPVECWIPDPSR  VECWIPDPS 0.5002 223 WB VP1 DRB4_0101 201 KNNAYPVECWIPDPS  YPVECWIPD 0.4824 271 WB VP1 DRB4_0101 206 PVECWIPDPSRNENT  VECWIPDPS 0.4517 377 WB VP1 DRB4_0101 207 VECWIPDPSRNENTR  VECWIPDPS 0.4492 388 WB VP1 DRB5_0101 285 ARYFKIRLRKRSVKN  FKIRLRKRS 0.6288 55 WB VP1 DRB5_0101 284 LARYFKIRLRKRSVK  FKIRLRKRS 0.6287 56 WB VP1 DRB5_0101 282 RGLARYFKIRLRKRS  YFKIRLRKR 0.6211 60 WB VP1 DRB5_0101 283 GLARYFKIRLRKRSV  FKIRLRKRS 0.6196 61 WB VP1 DRB5_0101 286 RYFKIRLRKRSVKNP  FKIRLRKRS 0.5991 77 WB VP1 DRB5_0101 287 YFKIRLRKRSVKNPY  FKIRLRKRS 0.5403 145 WB VP1 DRB5_0101 281 WRGLARYFKIRLRKR  WRGLARYFK 0.4956 235 WB VP1 DRB5_0101 288 FKIRLRKRSVKNPYP  FKIRLRKRS 0.4834 267 WB VP1 DRB5_0101 164 QGVLMNYRTKYPQGT  LMNYRTKYP 0.4622 337 WB VP1 DRB5_0101 165 GVLMNYRTKYPQGTI  YRTKYPQGT 0.4558 361 WB VP1 DRB5_0101 177 GTITPKNPTAQSQVM  ITPKNPTAQ 0.4497 386 WB VP1 DRB5_0101 71 LSAENAFESDSPDRK  AFESDSPDR 0.4477 394 WB VP1 DRB5_0101 72 SAENAFESDSPDRKM  FESDSPDRK 0.4472 396 WB VP1 DRB5_0101 73 AENAFESDSPDRKML  FESDSPDRK 0.4469 397 WB VP1 DRB5_0101 173 KYPQGTITPKNPTAQ  QGTITPKNP 0.4468 398 WB VP1 DRB5_0101 74 ENAFESDSPDRKMLP  FESDSPDRK 0.4464 400 WB VP1 DRB5_0101 275 SSGTQQWRGLARYFK  TQQWRGLAR 0.4455 403 WB VP1 DRB5_0101 174 YPQGTITPKNPTAQS  ITPKNPTAQ 0.4442 409 WB VP1 DRB5_0101 276 SGTQQWRGLARYFKI  WRGLARYFK 0.4440 410 WB VP1 DRB5_0101 279 QQWRGLARYFKIRLR  WRGLARYFK 0.4423 417 WB VP1 DRB5_0101 277 GTQQWRGLARYFKIR  WRGLARYFK 0.4408 424 WB VP1 DRB5_0101 278 TQQWRGLARYFKIRL  WRGLARYFK 0.4408 424 WB VP1 DRB5_0101 176 QGTITPKNPTAQSQV  ITPKNPTAQ 0.4392 432 WB VP1 DRB5_0101 175 PQGTITPKNPTAQSQ  ITPKNPTAQ 0.4390 433 WB VP1 DRB5_0101 166 VLMNYRTKYPQGTIT  YRTKYPQGT 0.4344 455 WB VP1 DRB5_0101 168 MNYRTKYPQGTITPK  YRTKYPQGT 0.4342 456 WB VP1 DRB5_0101 75 NAFESDSPDRKMLPC  FESDSPDRK 0.4294 480 WB VP1 SEQ ID NOS.: 59136-59917

Preferred BK virus fragments of small T antigen capable of interacting with one or more MHC class 2 molecules are listed in Table R.

TABLE R Prediction of BK virus small t protein specific MHC class 2, 15-mer peptide binders for 14 MHC class 2 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHCII/ database. The MHC class 2 molecules for which no binders were found are not listed. Allele pos peptide core 1-log50k(aff) aff(nM) B.L. Identity DRB1_0101 21 RAAWGNLPLMRKAYL  WGNLPLMRK 0.6972 26 SB Small t DRB1_0101 19 LERAAWGNLPLMRKA  WGNLPLMRK 0.6958 27 SB Small t DRB1_0101 20 ERAAWGNLPLMRKAY  WGNLPLMRK 0.6940 27 SB Small t DRB1_0101 22 AAWGNLPLMRKAYLK  WGNLPLMRK 0.6954 27 SB Small t DRB1_0101 18 GLERAAWGNLPLMRK  ERAAWGNLP 0.6928 28 SB Small t DRB1_0101 24 WGNLPLMRKAYLKKC  WGNLPLMRK 0.6020 74 WB Small t DRB1_0101 23 AWGNLPLMRKAYLKK  WGNLPLMRK 0.6000 76 WB Small t DRB1_0101 110 PCMLCQLRLRHLNRK  LCQLRLRHL 0.5884 86 WB Small t DRB1_0101 111 CMLCQLRLRHLNRKF  LCQLRLRHL 0.5833 91 WB Small t DRB1_0101 108 HCPCMLCQLRLRHLN  LCQLRLRHL 0.5732 101 WB Small t DRB1_0101 107 VHCPCMLCQLRLRHL  PCMLCQLRL 0.5712 104 WB Small t DRB1_0101 109 CPCMLCQLRLRHLNR  LCQLRLRHL 0.5711 104 WB Small t DRB1_0101 11 MELMDLLGLERAAWG  MDLLGLERA 0.5102 200 WB Small t DRB1_0101 113 LCQLRLRHLNRKFLR  LCQLRLRHL 0.5082 205 WB Small t DRB1_0101 112 MLCQLRLRHLNRKFL  LCQLRLRHL 0.5077 206 WB Small t DRB1_0101 121 LNRKFLRKEPLVWID  LRKEPLVWI 0.4900 249 WB Small t DRB1_0101 120 HLNRKFLRKEPLVWI  FLRKEPLVW 0.4888 252 WB Small t DRB1_0101 12 ELMDLLGLERAAWGN  MDLLGLERA 0.4876 256 WB Small t DRB1_0101 122 NRKFLRKEPLVWIDC  LRKEPLVWI 0.4836 267 WB Small t DRB1_0101 8 EESMELMDLLGLERA  LMDLLGLER 0.4834 268 WB Small t DRB1_0101 123 RKFLRKEPLVWIDCY  LRKEPLVWI 0.4822 271 WB Small t DRB1_0101 9 ESMELMDLLGLERAA  LMDLLGLER 0.4823 271 WB Small t DRB1_0101 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.4796 279 WB Small t DRB1_0101 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.4754 292 WB Small t DRB1_0101 10 SMELMDLLGLERAAW  MDLLGLERA 0.4730 299 WB Small t DRB1_0101 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4724 302 WB Small t DRB1_0101 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4699 310 WB Small t DRB1_0101 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.4690 313 WB Small t DRB1_0101 2 DKVLNREESMELMDL  LNREESMEL 0.4683 315 WB Small t DRB1_0101 3 KVLNREESMELMDLL  LNREESMEL 0.4672 319 WB Small t DRB1_0101 125 FLRKEPLVWIDCYCI  LRKEPLVWI 0.4622 337 WB Small t DRB1_0101 13 LMDLLGLERAAWGNL  LGLERAAWG 0.4572 355 WB Small t DRB1_0101 1 MDKVLNREESMELMD  LNREESMEL 0.4521 376 WB Small t DRB1_0101 124 KFLRKEPLVWIDCYC  LRKEPLVWI 0.4493 387 WB Small t DRB1_0101 14 MDLLGLERAAWGNLP  LGLERAAWG 0.4451 405 WB Small t DRB1_0101 5 LNREESMELMDLLGL  LNREESMEL 0.4397 429 WB Small t DRB1_0101 126 LRKEPLVWIDCYCID  LRKEPLVWI 0.4391 432 WB Small t DRB1_0101 7 REESMELMDLLGLER  MELMDLLGL 0.4355 449 WB Small t DRB1_0101 91 DTLYCKEWPICSKKP  YCKEWPICS 0.4339 457 WB Small t DRB1_0101 92 TLYCKEWPICSKKPS  YCKEWPICS 0.4323 465 WB Small t DRB1_0101 140 DCFTQWFGLDLTEET  FTQWFGLDL 0.4291 482 WB Small t DRB1_0401 92 TLYCKEWPICSKKPS  YCKEWPICS 0.5564 121 WB Small t DRB1_0401 91 DTLYCKEWPICSKKP  YCKEWPICS 0.5500 130 WB Small t DRB1_0401 90 PDTLYCKEWPICSKK  YCKEWPICS 0.5447 138 WB Small t DRB1_0401 89 CPDTLYCKEWPICSK  YCKEWPICS 0.5423 141 WB Small t DRB1_0401 88 LCPDTLYCKEWPICS  LYCKEWPIC 0.5400 145 WB Small t DRB1_0401 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.5015 220 WB Small t DRB1_0401 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.4994 225 WB Small t DRB1_0401 46 GGDEDKMKRMNTLYK  KMKRMNTLY 0.4992 226 WB Small t DRB1_0401 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4991 226 WB Small t DRB1_0401 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4948 237 WB Small t DRB1_0401 94 YCKEWPICSKKPSVH  YCKEWPICS 0.4689 313 WB Small t DRB1_0401 93 LYCKEWPICSKKPSV  YCKEWPICS 0.4677 317 WB Small t DRB1_0405 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.5687 106 WB Small t DRB1_0405 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.5662 109 WB Small t DRB1_0405 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.5447 138 WB Small t DRB1_0405 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.5432 140 WB Small t DRB1_0405 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.5413 143 WB Small t DRB1_0405 152 EETLQWWVQIIGETP  LQWWVQIIG 0.5365 151 WB Small t DRB1_0405 151 TEETLQWWVQIIGET  LQWWVQIIG 0.5328 157 WB Small t DRB1_0405 150 LTEETLQWWVQIIGE  LQWWVQIIG 0.5314 159 WB Small t DRB1_0405 153 ETLQWWVQIIGETPF  LQWWVQIIG 0.5290 163 WB Small t DRB1_0405 149 DLTEETLQWWVQIIG  TLQWWVQII 0.5260 169 WB Small t DRB1_0405 18 GLERAAWGNLPLMRK  RAAWGNLPL 0.5095 202 WB Small t DRB1_0405 19 LERAAWGNLPLMRKA  RAAWGNLPL 0.4956 235 WB Small t DRB1_0405 137 YCIDCFTQWFGLDLT  FTQWFGLDL 0.4951 236 WB Small t DRB1_0405 139 IDCFTQWFGLDLTEE  TQWFGLDLT 0.4864 259 WB Small t DRB1_0405 51 KMKRMNTLYKKMEQD  MKRMNTLYK 0.4857 261 WB Small t DRB1_0405 52 MKRMNTLYKKMEQDV  MKRMNTLYK 0.4857 261 WB Small t DRB1_0405 138 CIDCFTQWFGLDLTE  TQWFGLDLT 0.4851 263 WB Small t DRB1_0405 155 LQWWVQIIGETPFRD  LQWWVQIIG 0.4691 312 WB Small t DRB1_0405 140 DCFTQWFGLDLTEET  TQWFGLDLT 0.4671 319 WB Small t DRB1_0405 69 AHQPDFGTWNSSEVC  FGTWNSSEV 0.4648 327 WB Small t DRB1_0405 68 VAHQPDFGTWNSSEV  QPDFGTWNS 0.4624 336 WB Small t DRB1_0405 20 ERAAWGNLPLMRKAY  WGNLPLMRK 0.4570 356 WB Small t DRB1_0405 71 QPDFGTWNSSEVCAD  FGTWNSSEV 0.4550 364 WB Small t DRB1_0405 17 LGLERAAWGNLPLMR  RAAWGNLPL 0.4515 378 WB Small t DRB1_0405 70 HQPDFGTWNSSEVCA  FGTWNSSEV 0.4467 398 WB Small t DRB1_0405 154 TLQWWVQIIGETPFR  LQWWVQIIG 0.4465 399 WB Small t DRB1_0405 16 LLGLERAAWGNLPLM  RAAWGNLPL 0.4465 399 WB Small t DRB1_0405 15 DLLGLERAAWGNLPL  ERAAWGNLP 0.4401 427 WB Small t DRB1_0405 136 CYCIDCFTQWFGLDL  IDCFTQWFG 0.4322 465 WB Small t DRB1_0405 141 CFTQWFGLDLTEETL  TQWFGLDLT 0.4323 465 WB Small t DRB1_0405 72 PDFGTWNSSEVCADF  FGTWNSSEV 0.4300 477 WB Small t DRB1_0701 95 CKEWPICSKKPSVHC  ICSKKPSVH 0.4880 255 WB Small t DRB1_0701 96 KEWPICSKKPSVHCP  ICSKKPSVH 0.4829 269 WB Small t DRB1_0701 97 EWPICSKKPSVHCPC  ICSKKPSVH 0.4823 271 WB Small t DRB1_0701 98 WPICSKKPSVHCPCM  ICSKKPSVH 0.4807 276 WB Small t DRB1_0701 94 YCKEWPICSKKPSVH  PICSKKPSV 0.4738 297 WB Small t DRB1_0701 70 HQPDFGTWNSSEVCA  FGTWNSSEV 0.4721 303 WB Small t DRB1_0701 71 QPDFGTWNSSEVCAD  FGTWNSSEV 0.4716 304 WB Small t DRB1_0701 68 VAHQPDFGTWNSSEV  DFGTWNSSE 0.4709 306 WB Small t DRB1_0701 69 AHQPDFGTWNSSEVC  FGTWNSSEV 0.4705 308 WB Small t DRB1_0701 72 PDFGTWNSSEVCADF  FGTWNSSEV 0.4685 314 WB Small t DRB1_1101 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.4550 364 WB Small t DRB1_1101 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4498 385 WB Small t DRB1_1101 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.4495 386 WB Small t DRB1_1101 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4483 391 WB Small t DRB1_1101 46 GGDEDKMKRMNTLYK  EDKMKRMNT 0.4433 413 WB Small t DRB1_1101 18 GLERAAWGNLPLMRK  AWGNLPLMR 0.4312 471 WB Small t DRB1_1101 19 LERAAWGNLPLMRKA  WGNLPLMRK 0.4311 471 WB Small t DRB1_1101 21 RAAWGNLPLMRKAYL  WGNLPLMRK 0.4288 483 WB Small t DRB1_1101 20 ERAAWGNLPLMRKAY  WGNLPLMRK 0.4279 488 WB Small t DRB1_1302 18 GLERAAWGNLPLMRK  LERAAWGNL 0.5752 99 WB Small t DRB1_1302 21 RAAWGNLPLMRKAYL  WGNLPLMRK 0.5714 103 WB Small t DRB1_1302 22 AAWGNLPLMRKAYLK  WGNLPLMRK 0.5704 104 WB Small t DRB1_1302 19 LERAAWGNLPLMRKA  WGNLPLMRK 0.5702 105 WB Small t DRB1_1302 20 ERAAWGNLPLMRKAY  WGNLPLMRK 0.5531 126 WB Small t DRB1_1302 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.5012 221 WB Small t DRB1_1302 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4986 227 WB Small t DRB1_1302 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4966 232 WB Small t DRB1_1302 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.4940 239 WB Small t DRB1_1302 24 WGNLPLMRKAYLKKC  WGNLPLMRK 0.4926 242 WB Small t DRB1_1302 23 AWGNLPLMRKAYLKK  WGNLPLMRK 0.4885 253 WB Small t DRB1_1302 153 ETLQWWVQIIGETPF  WWVQIIGET 0.4827 270 WB Small t DRB1_1302 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.4800 278 WB Small t DRB1_1302 155 LQWWVQIIGETPFRD  VQIIGETPF 0.4679 317 WB Small t DRB1_1302 154 TLQWWVQIIGETPFR  VQIIGETPF 0.4659 323 WB Small t DRB1_1302 113 LCQLRLRHLNRKFLR  LRLRHLNRK 0.4607 342 WB Small t DRB1_1302 112 MLCQLRLRHLNRKFL  LRLRHLNRK 0.4561 360 WB Small t DRB1_1302 114 CQLRLRHLNRKFLRK  LRLRHLNRK 0.4549 364 WB Small t DRB1_1302 156 QWWVQIIGETPFRDL  VQIIGETPF 0.4401 427 WB Small t DRB1_1302 51 KMKRMNTLYKKMEQD  MKRMNTLYK 0.4272 492 WB Small t DRB1_1501 111 CMLCQLRLRHLNRKF  LRLRHLNRK 0.5327 157 WB Small t DRB1_1501 110 PCMLCQLRLRHLNRK  QLRLRHLNR 0.5274 166 WB Small t DRB1_1501 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.5229 174 WB Small t DRB1_1501 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.5190 182 WB Small t DRB1_1501 24 WGNLPLMRKAYLKKC  LMRKAYLKK 0.5176 185 WB Small t DRB1_1501 113 LCQLRLRHLNRKFLR  LRLRHLNRK 0.5166 187 WB Small t DRB1_1501 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.5153 190 WB Small t DRB1_1501 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.5147 191 WB Small t DRB1_1501 112 MLCQLRLRHLNRKFL  LRLRHLNRK 0.5140 192 WB Small t DRB1_1501 23 AWGNLPLMRKAYLKK  LPLMRKAYL 0.5076 206 WB Small t DRB1_1501 25 GNLPLMRKAYLKKCK  LMRKAYLKK 0.5063 209 WB Small t DRB1_1501 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.5026 217 WB Small t DRB1_1501 26 NLPLMRKAYLKKCKE  LMRKAYLKK 0.4961 233 WB Small t DRB1_1501 114 CQLRLRHLNRKFLRK  LRLRHLNRK 0.4919 244 WB Small t DRB1_1501 27 LPLMRKAYLKKCKEF  LMRKAYLKK 0.4850 263 WB Small t DRB1_1501 13 LMDLLGLERAAWGNL  LMDLLGLER 0.4683 315 WB Small t DRB1_1501 11 MELMDLLGLERAAWG  LMDLLGLER 0.4651 326 WB Small t DRB1_1501 115 QLRLRHLNRKFLRKE  LRLRHLNRK 0.4643 329 WB Small t DRB1_1501 120 HLNRKFLRKEPLVWI  FLRKEPLVW 0.4621 337 WB Small t DRB1_1501 121 LNRKFLRKEPLVWID  FLRKEPLVW 0.4374 440 WB Small t DRB1_1501 28 PLMRKAYLKKCKEFH  LMRKAYLKK 0.4332 461 WB Small t DRB1_1501 51 KMKRMNTLYKKMEQD  MKRMNTLYK 0.4331 461 WB Small t DRB1_1501 123 RKFLRKEPLVWIDCY  FLRKEPLVW 0.4300 477 WB Small t DRB1_1501 10 SMELMDLLGLERAAW  LMDLLGLER 0.4261 497 WB Small t DRB4_0101 94 YCKEWPICSKKPSVH  YCKEWPICS 0.5706 104 WB Small t DRB4_0101 112 MLCQLRLRHLNRKFL  LRLRHLNRK 0.5364 151 WB Small t DRB4_0101 113 LCQLRLRHLNRKFLR  LRLRHLNRK 0.5342 155 WB Small t DRB4_0101 111 CMLCQLRLRHLNRKF  LRLRHLNRK 0.5331 156 WB Small t DRB4_0101 110 PCMLCQLRLRHLNRK  LCQLRLRHL 0.5322 158 WB Small t DRB4_0101 95 CKEWPICSKKPSVHC  ICSKKPSVH 0.5323 158 WB Small t DRB4_0101 114 CQLRLRHLNRKFLRK  LRLRHLNRK 0.5291 163 WB Small t DRB4_0101 96 KEWPICSKKPSVHCP  ICSKKPSVH 0.5267 167 WB Small t DRB4_0101 97 EWPICSKKPSVHCPC  ICSKKPSVH 0.5247 171 WB Small t DRB4_0101 98 WPICSKKPSVHCPCM  ICSKKPSVH 0.5172 186 WB Small t DRB4_0101 115 QLRLRHLNRKFLRKE  LRLRHLNRK 0.4556 361 WB Small t DRB4_0101 116 LRLRHLNRKFLRKEP  LRLRHLNRK 0.4510 380 WB Small t DRB4_0101 100 ICSKKPSVHCPCMLC  ICSKKPSVH 0.4432 413 WB Small t DRB4_0101 99 PICSKKPSVHCPCML  ICSKKPSVH 0.4374 440 WB Small t DRB5_0101 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4763 289 WB Small t DRB5_0101 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4758 290 WB Small t DRB5_0101 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.4726 301 WB Small t DRB5_0101 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.4617 338 WB Small t DRB5_0101 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.4567 357 WB Small t DRB5_0101 112 MLCQLRLRHLNRKFL  LRLRHLNRK 0.4397 429 WB Small t DRB5_0101 114 CQLRLRHLNRKFLRK  LRHLNRKFL 0.4398 429 WB Small t DRB5_0101 53 KRMNTLYKKMEQDVK  KRMNTLYKK 0.4284 485 WB Small t DRB5_0101 22 AAWGNLPLMRKAYLK  WGNLPLMRK 0.4268 494 WB Small t SEQ ID NOS.: 59918-60257

Preferred BK virus fragments of large T antigen capable of interacting with one or more MHC class 2 molecules are listed in Table S.

TABLE S Prediction of BK virus Large T protein specific MHC class 2, 15-mer peptide binders for 14 MHC class 2 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHCII/database. The MHC class 2 molecules for which no binders were found are not listed. Allele pos peptide  core 1-log50k(aff) aff(nM) B.L. Identity DRB1_0101 566 LEKRILQSGMTLLLL  LQSGMTLLL 0.7526 15 SB Large T DRB1_0101 567 EKRILQSGMTLLLLL  LQSGMTLLL 0.7519 15 SB Large T DRB1_0101 568 KRILQSGMTLLLLLI  LQSGMTLLL 0.7525 15 SB Large T DRB1_0101 569 RILQSGMTLLLLLIW  LQSGMTLLL 0.7504 15 SB Large T DRB1_0101 565 LLEKRILQSGMTLLL  KRILQSGMT 0.7441 16 SB Large T DRB1_0101 21 RAAWGNLPLMRKAYL  WGNLPLMRK 0.6972 26 SB Large T DRB1_0101 19 LERAAWGNLPLMRKA  WGNLPLMRK 0.6958 27 SB Large T DRB1_0101 20 ERAAWGNLPLMRKAY  WGNLPLMRK 0.6940 27 SB Large T DRB1_0101 22 AAWGNLPLMRKAYLK  WGNLPLMRK 0.6954 27 SB Large T DRB1_0101 18 GLERAAWGNLPLMRK  ERAAWGNLP 0.6928 28 SB Large T DRB1_0101 570 ILQSGMTLLLLLIWF  LQSGMTLLL 0.6646 38 SB Large T DRB1_0101 571 LQSGMTLLLLLIWFR  LQSGMTLLL 0.6561 41 SB Large T DRB1_0101 383 NAVLEQYMAGVAWLH  EQYMAGVAW 0.6528 43 SB Large T DRB1_0101 387 EQYMAGVAWLHCLLP  YMAGVAWLH 0.6516 43 SB Large T DRB1_0101 385 VLEQYMAGVAWLHCL  YMAGVAWLH 0.6507 44 SB Large T DRB1_0101 384 AVLEQYMAGVAWLHC  YMAGVAWLH 0.6486 45 SB Large T DRB1_0101 386 LEQYMAGVAWLHCLL  YMAGVAWLH 0.6483 45 SB Large T DRB1_0101 441 LLDLCGGKALNVNLP  LCGGKALNV 0.6340 52 WB Large T DRB1_0101 144 LHQFLSQAVFSNRTL  LHQFLSQAV 0.6329 53 WB Large T DRB1_0101 143 DLHQFLSQAVFSNRT  LHQFLSQAV 0.6318 54 WB Large T DRB1_0101 442 LDLCGGKALNVNLPM  LCGGKALNV 0.6310 54 WB Large T DRB1_0101 439 AGLLDLCGGKALNVN  LCGGKALNV 0.6263 57 WB Large T DRB1_0101 440 GLLDLCGGKALNVNL  LCGGKALNV 0.6223 60 WB Large T DRB1_0101 438 AAGLLDLCGGKALNV  LLDLCGGKA 0.6207 61 WB Large T DRB1_0101 142 SDLHQFLSQAVFSNR  LHQFLSQAV 0.6178 62 WB Large T DRB1_0101 141 PSDLHQFLSQAVFSN  LHQFLSQAV 0.6165 63 WB Large T DRB1_0101 533 YPVPKTLQARFVRQI  PKTLQARFV 0.6160 64 WB Large T DRB1_0101 534 PVPKTLQARFVRQID  LQARFVRQI 0.6136 65 WB Large T DRB1_0101 140 FPSDLHQFLSQAVFS  LHQFLSQAV 0.6083 69 WB Large T DRB1_0101 138 KDFPSDLHQFLSQAV  FPSDLHQFL 0.6036 73 WB Large T DRB1_0101 139 DFPSDLHQFLSQAVF  LHQFLSQAV 0.6019 74 WB Large T DRB1_0101 24 WGNLPLMRKAYLKKC  WGNLPLMRK 0.6020 74 WB Large T DRB1_0101 23 AWGNLPLMRKAYLKK  WGNLPLMRK 0.6000 76 WB Large T DRB1_0101 517 NKRTQIFPPGLVTMN  IFPPGLVTM 0.5951 80 WB Large T DRB1_0101 518 KRTQIFPPGLVTMNE  IFPPGLVTM 0.5907 84 WB Large T DRB1_0101 428 GPIDSGKTTLAAGLL  IDSGKTTLA 0.5880 86 WB Large T DRB1_0101 519 RTQIFPPGLVTMNEY  IFPPGLVTM 0.5871 87 WB Large T DRB1_0101 520 TQIFPPGLVTMNEYP  IFPPGLVTM 0.5843 90 WB Large T DRB1_0101 268 KQVSWKLITEYAVET  WKLITEYAV 0.5795 95 WB Large T DRB1_0101 269 QVSWKLITEYAVETK  LITEYAVET 0.5780 96 WB Large T DRB1_0101 284 CEDVFLLLGMYLEFQ  VFLLLGMYL 0.5771 97 WB Large T DRB1_0101 285 EDVFLLLGMYLEFQY  VFLLLGMYL 0.5774 97 WB Large T DRB1_0101 535 VPKTLQARFVRQIDF  LQARFVRQI 0.5743 100 WB Large T DRB1_0101 536 PKTLQARFVRQIDFR  LQARFVRQI 0.5746 100 WB Large T DRB1_0101 270 VSWKLITEYAVETKC  LITEYAVET 0.5715 103 WB Large T DRB1_0101 147 FLSQAVFSNRTLACF  SQAVFSNRT 0.5698 105 WB Large T DRB1_0101 388 QYMAGVAWLHCLLPK  YMAGVAWLH 0.5680 107 WB Large T DRB1_0101 603 ERLDSEISMYTFSRM  LDSEISMYT 0.5669 108 WB Large T DRB1_0101 389 YMAGVAWLHCLLPKM  YMAGVAWLH 0.5664 109 WB Large T DRB1_0101 448 KALNVNLPMERLTFE  LNVNLPMER 0.5655 110 WB Large T DRB1_0101 444 LCGGKALNVNLPMER  LCGGKALNV 0.5641 112 WB Large T DRB1_0101 446 GGKALNVNLPMERLT  LNVNLPMER 0.5640 112 WB Large T DRB1_0101 425 LFKGPIDSGKTTLAA  IDSGKTTLA 0.5627 113 WB Large T DRB1_0101 447 GKALNVNLPMERLTF  LNVNLPMER 0.5619 114 WB Large T DRB1_0101 427 KGPIDSGKTTLAAGL  IDSGKTTLA 0.5613 115 WB Large T DRB1_0101 599 VEWKERLDSEISMYT  KERLDSEIS 0.5611 115 WB Large T DRB1_0101 445 CGGKALNVNLPMERL  LNVNLPMER 0.5598 117 WB Large T DRB1_0101 490 GHGINNLDSLRDYLD  INNLDSLRD 0.5597 117 WB Large T DRB1_0101 271 SWKLITEYAVETKCE  LITEYAVET 0.5583 119 WB Large T DRB1_0101 489 SGHGINNLDSLRDYL  INNLDSLRD 0.5574 120 WB Large T DRB1_0101 491 HGINNLDSLRDYLDG  INNLDSLRD 0.5573 120 WB Large T DRB1_0101 424 WLFKGPIDSGKTTLA  KGPIDSGKT 0.5567 121 WB Large T DRB1_0101 487 LPSGHGINNLDSLRD  LPSGHGINN 0.5568 121 WB Large T DRB1_0101 530 MNEYPVPKTLQARFV  YPVPKTLQA 0.5570 121 WB Large T DRB1_0101 426 FKGPIDSGKTTLAAG  IDSGKTTLA 0.5562 122 WB Large T DRB1_0101 600 EWKERLDSEISMYTF  LDSEISMYT 0.5562 122 WB Large T DRB1_0101 602 KERLDSEISMYTFSR  LDSEISMYT 0.5560 122 WB Large T DRB1_0101 488 PSGHGINNLDSLRDY  INNLDSLRD 0.5554 123 WB Large T DRB1_0101 601 WKERLDSEISMYTFS  LDSEISMYT 0.5538 125 WB Large T DRB1_0101 272 WKLITEYAVETKCED  LITEYAVET 0.5514 128 WB Large T DRB1_0101 531 NEYPVPKTLQARFVR  PKTLQARFV 0.5518 128 WB Large T DRB1_0101 521 QIFPPGLVTMNEYPV  FPPGLVTMN 0.5507 129 WB Large T DRB1_0101 443 DLCGGKALNVNLPME  LCGGKALNV 0.5488 132 WB Large T DRB1_0101 228 VNKEYLLYSALTRDP  YLLYSALTR 0.5454 137 WB Large T DRB1_0101 145 HQFLSQAVFSNRTLA  SQAVFSNRT 0.5437 139 WB Large T DRB1_0101 374 MDLIFGAHGNAVLEQ  IFGAHGNAV 0.5440 139 WB Large T DRB1_0101 375 DLIFGAHGNAVLEQY  IFGAHGNAV 0.5439 139 WB Large T DRB1_0101 229 NKEYLLYSALTRDPY  LYSALTRDP 0.5434 140 WB Large T DRB1_0101 146 QFLSQAVFSNRTLAC  SQAVFSNRT 0.5423 141 WB Large T DRB1_0101 373 KMDLIFGAHGNAVLE  IFGAHGNAV 0.5366 150 WB Large T DRB1_0101 564 FLLEKRILQSGMTLL  KRILQSGMT 0.5369 150 WB Large T DRB1_0101 372 DKMDLIFGAHGNAVL  IFGAHGNAV 0.5366 151 WB Large T DRB1_0101 230 KEYLLYSALTRDPYH  LYSALTRDP 0.5334 156 WB Large T DRB1_0101 449 ALNVNLPMERLTFEL  NVNLPMERL 0.5320 158 WB Large T DRB1_0101 286 DVFLLLGMYLEFQYN  LLGMYLEFQ 0.5310 160 WB Large T DRB1_0101 232 YLLYSALTRDPYHII  LYSALTRDP 0.5298 162 WB Large T DRB1_0101 338 ICQQAVDTVLAKKRV  QQAVDTVLA 0.5273 166 WB Large T DRB1_0101 430 IDSGKTTLAAGLLDL  IDSGKTTLA 0.5269 167 WB Large T DRB1_0101 149 SQAVFSNRTLACFAV  FSNRTLACF 0.5259 169 WB Large T DRB1_0101 337 SICQQAVDTVLAKKR  QQAVDTVLA 0.5252 170 WB Large T DRB1_0101 148 LSQAVFSNRTLACFA  FSNRTLACF 0.5244 172 WB Large T DRB1_0101 231 EYLLYSALTRDPYHI  LYSALTRDP 0.5238 173 WB Large T DRB1_0101 522 IFPPGLVTMNEYPVP  IFPPGLVTM 0.5236 173 WB Large T DRB1_0101 532 EYPVPKTLQARFVRQ  PKTLQARFV 0.5222 176 WB Large T DRB1_0101 429 PIDSGKTTLAAGLLD  IDSGKTTLA 0.5198 180 WB Large T DRB1_0101 516 LNKRTQIFPPGLVTM  RTQIFPPGL 0.5156 189 WB Large T DRB1_0101 287 VFLLLGMYLEFQYNV  VFLLLGMYL 0.5144 191 WB Large T DRB1_0101 11 MELMDLLGLERAAWG  MDLLGLERA 0.5102 200 WB Large T DRB1_0101 473 VFEDVKGTGAESKDL  VKGTGAESK 0.5100 201 WB Large T DRB1_0101 474 FEDVKGTGAESKDLP  VKGTGAESK 0.5088 203 WB Large T DRB1_0101 537 KTLQARFVRQIDFRP  LQARFVRQI 0.5092 203 WB Large T DRB1_0101 475 EDVKGTGAESKDLPS  VKGTGAESK 0.5068 208 WB Large T DRB1_0101 195 NIIFFLTPHRHRVSA  IFFLTPHRH 0.5062 209 WB Large T DRB1_0101 335 QKSICQQAVDTVLAK  ICQQAVDTV 0.5063 209 WB Large T DRB1_0101 194 HNIIFFLTPHRHRVS  IFFLTPHRH 0.5053 211 WB Large T DRB1_0101 336 KSICQQAVDTVLAKK  ICQQAVDTV 0.5051 212 WB Large T DRB1_0101 334 NQKSICQQAVDTVLA  ICQQAVDTV 0.5035 215 WB Large T DRB1_0101 450 LNVNLPMERLTFELG  NVNLPMERL 0.5031 216 WB Large T DRB1_0101 527 LVTMNEYPVPKTLQA  MNEYPVPKT 0.5027 217 WB Large T DRB1_0101 528 VTMNEYPVPKTLQAR  YPVPKTLQA 0.5012 221 WB Large T DRB1_0101 371 LDKMDLIFGAHGNAV  LDKMDLIFG 0.4990 226 WB Large T DRB1_0101 572 QSGMTLLLLLIWFRP  MTLLLLLIW 0.4975 230 WB Large T DRB1_0101 282 TKCEDVFLLLGMYLE  VFLLLGMYL 0.4937 239 WB Large T DRB1_0101 283 KCEDVFLLLGMYLEF  VFLLLGMYL 0.4920 244 WB Large T DRB1_0101 376 LIFGAHGNAVLEQYM  FGAHGNAVL 0.4919 244 WB Large T DRB1_0101 394 AWLHCLLPKMDSVIF  LLPKMDSVI 0.4910 246 WB Large T DRB1_0101 604 RLDSEISMYTFSRMK  LDSEISMYT 0.4900 249 WB Large T DRB1_0101 605 LDSEISMYTFSRMKY  LDSEISMYT 0.4889 252 WB Large T DRB1_0101 12 ELMDLLGLERAAWGN  MDLLGLERA 0.4876 256 WB Large T DRB1_0101 472 VVFEDVKGTGAESKD  VKGTGAESK 0.4858 261 WB Large T DRB1_0101 471 MVVFEDVKGTGAESK  FEDVKGTGA 0.4853 262 WB Large T DRB1_0101 340 QQAVDTVLAKKRVDT  VDTVLAKKR 0.4843 265 WB Large T DRB1_0101 172 ILYKKLMEKYSVTFI  YKKLMEKYS 0.4836 267 WB Large T DRB1_0101 339 CQQAVDTVLAKKRVD  VDTVLAKKR 0.4837 267 WB Large T DRB1_0101 8 EESMELMDLLGLERA  LMDLLGLER 0.4834 268 WB Large T DRB1_0101 9 ESMELMDLLGLERAA  LMDLLGLER 0.4823 271 WB Large T DRB1_0101 395 WLHCLLPKMDSVIFD  LPKMDSVIF 0.4815 273 WB Large T DRB1_0101 256 EHDFNPEEPEETKQV  FNPEEPEET 0.4804 276 WB Large T DRB1_0101 152 VFSNRTLACFAVYTT  TLACFAVYT 0.4803 277 WB Large T DRB1_0101 257 HDFNPEEPEETKQVS  FNPEEPEET 0.4796 279 WB Large T DRB1_0101 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.4796 279 WB Large T DRB1_0101 255 KEHDFNPEEPEETKQ  FNPEEPEET 0.4792 280 WB Large T DRB1_0101 396 LHCLLPKMDSVIFDF  LPKMDSVIF 0.4778 284 WB Large T DRB1_0101 254 LKEHDFNPEEPEETK  FNPEEPEET 0.4775 285 WB Large T DRB1_0101 150 QAVFSNRTLACFAVY  FSNRTLACF 0.4767 288 WB Large T DRB1_0101 563 EFLLEKRILQSGMTL  KRILQSGMT 0.4767 288 WB Large T DRB1_0101 226 KGVNKEYLLYSALTR  EYLLYSALT 0.4763 289 WB Large T DRB1_0101 548 DFRPKIYLRKSLQNS  FRPKIYLRK 0.4755 291 WB Large T DRB1_0101 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.4754 292 WB Large T DRB1_0101 549 FRPKIYLRKSLQNSE  YLRKSLQNS 0.4751 293 WB Large T DRB1_0101 171 QILYKKLMEKYSVTF  YKKLMEKYS 0.4745 295 WB Large T DRB1_0101 253 GLKEHDFNPEEPEET  GLKEHDFNP 0.4744 295 WB Large T DRB1_0101 196 IIFFLTPHRHRVSAI  LTPHRHRVS 0.4734 298 WB Large T DRB1_0101 397 HCLLPKMDSVIFDFL  LPKMDSVIF 0.4735 298 WB Large T DRB1_0101 10 SMELMDLLGLERAAW  MDLLGLERA 0.4730 299 WB Large T DRB1_0101 578 LLLLIWFRPVADFSK  LIWFRPVAD 0.4729 300 WB Large T DRB1_0101 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4724 302 WB Large T DRB1_0101 562 SEFLLEKRILQSGMT  LEKRILQSG 0.4722 302 WB Large T DRB1_0101 579 LLLIWFRPVADFSKD  LIWFRPVAD 0.4723 302 WB Large T DRB1_0101 551 PKIYLRKSLQNSEFL  YLRKSLQNS 0.4719 303 WB Large T DRB1_0101 523 FPPGLVTMNEYPVPK  FPPGLVTMN 0.4709 306 WB Large T DRB1_0101 197 IFFLTPHRHRVSAIN  LTPHRHRVS 0.4697 310 WB Large T DRB1_0101 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4699 310 WB Large T DRB1_0101 550 RPKIYLRKSLQNSEF  YLRKSLQNS 0.4698 310 WB Large T DRB1_0101 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.4690 313 WB Large T DRB1_0101 2 DKVLNREESMELMDL  LNREESMEL 0.4683 315 WB Large T DRB1_0101 577 LLLLLIWFRPVADFS  LIWFRPVAD 0.4684 315 WB Large T DRB1_0101 153 FSNRTLACFAVYTTK  LACFAVYTT 0.4677 317 WB Large T DRB1_0101 3 KVLNREESMELMDLL  LNREESMEL 0.4672 319 WB Large T DRB1_0101 281 ETKCEDVFLLLGMYL  EDVFLLLGM 0.4666 321 WB Large T DRB1_0101 573 SGMTLLLLLIWFRPV  MTLLLLLIW 0.4649 327 WB Large T DRB1_0101 493 INNLDSLRDYLDGSV  INNLDSLRD 0.4638 331 WB Large T DRB1_0101 524 PPGLVTMNEYPVPKT  LVTMNEYPV 0.4635 332 WB Large T DRB1_0101 525 PGLVTMNEYPVPKTL  MNEYPVPKT 0.4633 333 WB Large T DRB1_0101 151 AVFSNRTLACFAVYT  FSNRTLACF 0.4625 336 WB Large T DRB1_0101 492 GINNLDSLRDYLDGS  INNLDSLRD 0.4622 336 WB Large T DRB1_0101 227 GVNKEYLLYSALTRD  YLLYSALTR 0.4619 338 WB Large T DRB1_0101 529 TMNEYPVPKTLQARF  YPVPKTLQA 0.4598 345 WB Large T DRB1_0101 459 LTFELGVAIDQYMVV  LGVAIDQYM 0.4589 349 WB Large T DRB1_0101 457 ERLTFELGVAIDQYM  LTFELGVAI 0.4584 351 WB Large T DRB1_0101 398 CLLPKMDSVIFDFLH  LPKMDSVIF 0.4578 353 WB Large T DRB1_0101 552 KIYLRKSLQNSEFLL  YLRKSLQNS 0.4575 354 WB Large T DRB1_0101 13 LMDLLGLERAAWGNL  LGLERAAWG 0.4572 355 WB Large T DRB1_0101 575 MTLLLLLIWFRPVAD  MTLLLLLIW 0.4574 355 WB Large T DRB1_0101 451 NVNLPMERLTFELGV  NVNLPMERL 0.4555 362 WB Large T DRB1_0101 193 GHNIIFFLTPHRHRV  IFFLTPHRH 0.4529 372 WB Large T DRB1_0101 1 MDKVLNREESMELMD  LNREESMEL 0.4521 376 WB Large T DRB1_0101 432 SGKTTLAAGLLDLCG  KTTLAAGLL 0.4504 382 WB Large T DRB1_0101 233 LLYSALTRDPYHIIE  LYSALTRDP 0.4500 384 WB Large T DRB1_0101 377 IFGAHGNAVLEQYMA  IFGAHGNAV 0.4493 387 WB Large T DRB1_0101 273 KLITEYAVETKCEDV  LITEYAVET 0.4490 388 WB Large T DRB1_0101 458 RLTFELGVAIDQYMV  LGVAIDQYM 0.4476 394 WB Large T DRB1_0101 234 LYSALTRDPYHIIEE  LYSALTRDP 0.4472 396 WB Large T DRB1_0101 422 RYWLFKGPIDSGKTT  WLFKGPIDS 0.4473 396 WB Large T DRB1_0101 421 RRYWLFKGPIDSGKT  WLFKGPIDS 0.4465 399 WB Large T DRB1_0101 274 LITEYAVETKCEDVF  LITEYAVET 0.4460 401 WB Large T DRB1_0101 14 MDLLGLERAAWGNLP  LGLERAAWG 0.4451 405 WB Large T DRB1_0101 476 DVKGTGAESKDLPSG  VKGTGAESK 0.4428 415 WB Large T DRB1_0101 477 VKGTGAESKDLPSGH  VKGTGAESK 0.4412 422 WB Large T DRB1_0101 526 GLVTMNEYPVPKTLQ  MNEYPVPKT 0.4408 424 WB Large T DRB1_0101 174 YKKLMEKYSVTFISR  LMEKYSVTF 0.4406 425 WB Large T DRB1_0101 390 MAGVAWLHCLLPKMD  VAWLHCLLP 0.4407 425 WB Large T DRB1_0101 173 LYKKLMEKYSVTFIS  LMEKYSVTF 0.4405 426 WB Large T DRB1_0101 5 LNREESMELMDLLGL  LNREESMEL 0.4397 429 WB Large T DRB1_0101 580 LLIWFRPVADFSKDI  WFRPVADFS 0.4370 442 WB Large T DRB1_0101 391 AGVAWLHCLLPKMDS  VAWLHCLLP 0.4368 443 WB Large T DRB1_0101 7 REESMELMDLLGLER  MELMDLLGL 0.4355 449 WB Large T DRB1_0101 341 QAVDTVLAKKRVDTL  VDTVLAKKR 0.4341 456 WB Large T DRB1_0101 431 DSGKTTLAAGLLDLC  KTTLAAGLL 0.4339 457 WB Large T DRB1_0101 155 NRTLACFAVYTTKEK  LACFAVYTT 0.4312 471 WB Large T DRB1_0101 192 AGHNIIFFLTPHRHR  IFFLTPHRH 0.4310 472 WB Large T DRB1_0101 538 TLQARFVRQIDFRPK  LQARFVRQI 0.4309 472 WB Large T DRB1_0101 266 ETKQVSWKLITEYAV  VSWKLITEY 0.4307 473 WB Large T DRB1_0101 267 TKQVSWKLITEYAVE  WKLITEYAV 0.4303 475 WB Large T DRB1_0101 539 LQARFVRQIDFRPKI  LQARFVRQI 0.4290 482 WB Large T DRB1_0101 225 CKGVNKEYLLYSALT  VNKEYLLYS 0.4288 483 WB Large T DRB1_0101 677 KGFQCFKRPKTPPPK  FKRPKTPPP 0.4281 487 WB Large T DRB1_0101 333 KNQKSICQQAVDTVL  ICQQAVDTV 0.4261 498 WB Large T DRB1_0101 72 PDFGTWNSSEVPTYG  FGTWNSSEV 0.4258 499 WB Large T DRB1_0401 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.5015 220 WB Large T DRB1_0401 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.4994 225 WB Large T DRB1_0401 46 GGDEDKMKRMNTLYK  KMKRMNTLY 0.4992 226 WB Large T DRB1_0401 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4991 226 WB Large T DRB1_0401 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4948 237 WB Large T DRB1_0401 192 AGHNIIFFLTPHRHR  IIFFLTPHR 0.4859 261 WB Large T DRB1_0401 194 HNIIFFLTPHRHRVS  IIFFLTPHR 0.4856 261 WB Large T DRB1_0401 193 GHNIIFFLTPHRHRV  IIFFLTPHR 0.4820 272 WB Large T DRB1_0401 191 CAGHNIIFFLTPHRH  IIFFLTPHR 0.4700 309 WB Large T DRB1_0401 190 MCAGHNIIFFLTPHR  MCAGHNIIF 0.4533 371 WB Large T DRB1_0404 194 HNIIFFLTPHRHRVS  IIFFLTPHR 0.5594 118 WB Large T DRB1_0404 193 GHNIIFFLTPHRHRV  IIFFLTPHR 0.5580 119 WB Large T DRB1_0404 284 CEDVFLLLGMYLEFQ  FLLLGMYLE 0.5487 132 WB Large T DRB1_0404 286 DVFLLLGMYLEFQYN  LLGMYLEFQ 0.5479 133 WB Large T DRB1_0404 285 EDVFLLLGMYLEFQY  LLGMYLEFQ 0.5470 135 WB Large T DRB1_0404 288 FLLLGMYLEFQYNVE  LLGMYLEFQ 0.5425 141 WB Large T DRB1_0404 287 VFLLLGMYLEFQYNV  LLGMYLEFQ 0.5417 142 WB Large T DRB1_0404 192 AGHNIIFFLTPHRHR  IIFFLTPHR 0.5303 161 WB Large T DRB1_0404 191 CAGHNIIFFLTPHRH  IIFFLTPHR 0.5272 167 WB Large T DRB1_0404 575 MTLLLLLIWFRPVAD  LLLLIWFRP 0.5188 182 WB Large T DRB1_0404 389 YMAGVAWLHCLLPKM  VAWLHCLLP 0.5113 198 WB Large T DRB1_0404 387 EQYMAGVAWLHCLLP  YMAGVAWLH 0.5087 203 WB Large T DRB1_0404 576 TLLLLLIWFRPVADF  LLLLIWFRP 0.5091 203 WB Large T DRB1_0404 190 MCAGHNIIFFLTPHR  HNIIFFLTP 0.5052 211 WB Large T DRB1_0404 390 MAGVAWLHCLLPKMD  VAWLHCLLP 0.5054 211 WB Large T DRB1_0404 175 KKLMEKYSVTFISRH  LMEKYSVTF 0.5033 216 WB Large T DRB1_0404 391 AGVAWLHCLLPKMDS  VAWLHCLLP 0.5004 223 WB Large T DRB1_0404 577 LLLLLIWFRPVADFS  LLIWFRPVA 0.5001 223 WB Large T DRB1_0404 388 QYMAGVAWLHCLLPK  VAWLHCLLP 0.4995 225 WB Large T DRB1_0404 195 NIIFFLTPHRHRVSA  IIFFLTPHR 0.4985 227 WB Large T DRB1_0404 179 EKYSVTFISRHMCAG  YSVTFISRH 0.4981 228 WB Large T DRB1_0404 177 LMEKYSVTFISRHMC  YSVTFISRH 0.4969 231 WB Large T DRB1_0404 176 KLMEKYSVTFISRHM  YSVTFISRH 0.4952 236 WB Large T DRB1_0404 178 MEKYSVTFISRHMCA  YSVTFISRH 0.4940 239 WB Large T DRB1_0404 578 LLLLIWFRPVADFSK  LLIWFRPVA 0.4909 247 WB Large T DRB1_0404 196 IIFFLTPHRHRVSAI  IIFFLTPHR 0.4866 258 WB Large T DRB1_0404 574 GMTLLLLLIWFRPVA  LLLLIWFRP 0.4835 267 WB Large T DRB1_0404 371 LDKMDLIFGAHGNAV  MDLIFGAHG 0.4592 348 WB Large T DRB1_0404 290 LLGMYLEFQYNVEEC  LLGMYLEFQ 0.4448 406 WB Large T DRB1_0404 289 LLLGMYLEFQYNVEE  LLGMYLEFQ 0.4447 407 WB Large T DRB1_0404 372 DKMDLIFGAHGNAVL  IFGAHGNAV 0.4437 411 WB Large T DRB1_0405 575 MTLLLLLIWFRPVAD  LLIWFRPVA 0.7757 11 SB Large T DRB1_0405 576 TLLLLLIWFRPVADF  LIWFRPVAD 0.7721 12 SB Large T DRB1_0405 577 LLLLLIWFRPVADFS  LIWFRPVAD 0.7733 12 SB Large T DRB1_0405 578 LLLLIWFRPVADFSK  LIWFRPVAD 0.7738 12 SB Large T DRB1_0405 579 LLLIWFRPVADFSKD  LIWFRPVAD 0.7712 12 SB Large T DRB1_0405 85 YGTEEWESWWSSFNE  WESWWSSFN 0.7453 16 SB Large T DRB1_0405 87 TEEWESWWSSFNEKW  WESWWSSFN 0.7451 16 SB Large T DRB1_0405 86 GTEEWESWWSSFNEK  WESWWSSFN 0.7381 17 SB Large T DRB1_0405 88 EEWESWWSSFNEKWD  WESWWSSFN 0.7402 17 SB Large T DRB1_0405 84 TYGTEEWESWWSSFN  TEEWESWWS 0.7216 20 SB Large T DRB1_0405 580 LLIWFRPVADFSKDI  LIWFRPVAD 0.6804 32 SB Large T DRB1_0405 581 LIWFRPVADFSKDIQ  LIWFRPVAD 0.6771 33 SB Large T DRB1_0405 89 EWESWWSSFNEKWDE  WESWWSSFN 0.6771 33 SB Large T DRB1_0405 90 WESWWSSFNEKWDED  WESWWSSFN 0.6504 44 SB Large T DRB1_0405 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.5687 106 WB Large T DRB1_0405 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.5662 109 WB Large T DRB1_0405 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.5447 138 WB Large T DRB1_0405 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.5432 140 WB Large T DRB1_0405 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.5413 143 WB Large T DRB1_0405 490 GHGINNLDSLRDYLD  INNLDSLRD 0.5182 184 WB Large T DRB1_0405 491 HGINNLDSLRDYLDG  INNLDSLRD 0.5113 198 WB Large T DRB1_0405 18 GLERAAWGNLPLMRK  RAAWGNLPL 0.5095 202 WB Large T DRB1_0405 487 LPSGHGINNLDSLRD  GHGINNLDS 0.4979 229 WB Large T DRB1_0405 19 LERAAWGNLPLMRKA  RAAWGNLPL 0.4956 235 WB Large T DRB1_0405 488 PSGHGINNLDSLRDY  INNLDSLRD 0.4948 237 WB Large T DRB1_0405 489 SGHGINNLDSLRDYL  INNLDSLRD 0.4858 261 WB Large T DRB1_0405 51 KMKRMNTLYKKMEQD  MKRMNTLYK 0.4857 261 WB Large T DRB1_0405 52 MKRMNTLYKKMEQDV  MKRMNTLYK 0.4857 261 WB Large T DRB1_0405 391 AGVAWLHCLLPKMDS  VAWLHCLLP 0.4831 269 WB Large T DRB1_0405 91 ESWWSSFNEKWDEDL  WSSFNEKWD 0.4812 274 WB Large T DRB1_0405 390 MAGVAWLHCLLPKMD  VAWLHCLLP 0.4697 310 WB Large T DRB1_0405 387 EQYMAGVAWLHCLLP  YMAGVAWLH 0.4648 327 WB Large T DRB1_0405 68 VAHQPDFGTWNSSEV  QPDFGTWNS 0.4624 336 WB Large T DRB1_0405 418 VPKRRYWLFKGPIDS  YWLFKGPID 0.4620 337 WB Large T DRB1_0405 388 QYMAGVAWLHCLLPK  VAWLHCLLP 0.4614 339 WB Large T DRB1_0405 420 KRRYWLFKGPIDSGK  YWLFKGPID 0.4599 345 WB Large T DRB1_0405 419 PKRRYWLFKGPIDSG  YWLFKGPID 0.4586 350 WB Large T DRB1_0405 20 ERAAWGNLPLMRKAY  WGNLPLMRK 0.4570 356 WB Large T DRB1_0405 69 AHQPDFGTWNSSEVP  FGTWNSSEV 0.4571 356 WB Large T DRB1_0405 389 YMAGVAWLHCLLPKM  VAWLHCLLP 0.4547 365 WB Large T DRB1_0405 421 RRYWLFKGPIDSGKT  YWLFKGPID 0.4540 368 WB Large T DRB1_0405 417 NVPKRRYWLFKGPID  RYWLFKGPI 0.4530 372 WB Large T DRB1_0405 17 LGLERAAWGNLPLMR  RAAWGNLPL 0.4515 378 WB Large T DRB1_0405 16 LLGLERAAWGNLPLM  RAAWGNLPL 0.4465 399 WB Large T DRB1_0405 493 INNLDSLRDYLDGSV  INNLDSLRD 0.4409 424 WB Large T DRB1_0405 492 GINNLDSLRDYLDGS  INNLDSLRD 0.4405 426 WB Large T DRB1_0405 15 DLLGLERAAWGNLPL  ERAAWGNLP 0.4401 427 WB Large T DRB1_0405 70 HQPDFGTWNSSEVPT  FGTWNSSEV 0.4392 432 WB Large T DRB1_0405 653 CSSQVSDTSAPDSEN  QVSDTSAPD 0.4296 479 WB Large T DRB1_0405 654 SSQVSDTSAPDSENP  QVSDTSAPD 0.4282 486 WB Large T DRB1_0701 412 HCVVFNVPKRRYWLF  VFNVPKRRY 0.5438 139 WB Large T DRB1_0701 413 CVVFNVPKRRYWLFK  VPKRRYWLF 0.5406 144 WB Large T DRB1_0701 414 VVFNVPKRRYWLFKG  VPKRRYWLF 0.5149 190 WB Large T DRB1_0701 415 VFNVPKRRYWLFKGP  VPKRRYWLF 0.5009 221 WB Large T DRB1_0701 71 QPDFGTWNSSEVPTY  FGTWNSSEV 0.4820 272 WB Large T DRB1_0701 72 PDFGTWNSSEVPTYG  FGTWNSSEV 0.4789 281 WB Large T DRB1_0701 68 VAHQPDFGTWNSSEV  DFGTWNSSE 0.4709 306 WB Large T DRB1_0701 69 AHQPDFGTWNSSEVP  FGTWNSSEV 0.4658 324 WB Large T DRB1_0701 70 HQPDFGTWNSSEVPT  FGTWNSSEV 0.4657 324 WB Large T DRB1_0701 416 FNVPKRRYWLFKGPI  VPKRRYWLF 0.4627 335 WB Large T DRB1_0701 194 HNIIFFLTPHRHRVS  IFFLTPHRH 0.4550 364 WB Large T DRB1_0701 195 NIIFFLTPHRHRVSA  IFFLTPHRH 0.4521 375 WB Large T DRB1_0701 193 GHNIIFFLTPHRHRV  IFFLTPHRH 0.4386 434 WB Large T DRB1_0701 176 KLMEKYSVTFISRHM  YSVTFISRH 0.4346 454 WB Large T DRB1_0701 196 IIFFLTPHRHRVSAI  IFFLTPHRH 0.4331 461 WB Large T DRB1_0701 177 LMEKYSVTFISRHMC  YSVTFISRH 0.4315 469 WB Large T DRB1_0701 387 EQYMAGVAWLHCLLP  YMAGVAWLH 0.4303 475 WB Large T DRB1_0701 386 LEQYMAGVAWLHCLL  YMAGVAWLH 0.4292 481 WB Large T DRB1_0701 192 AGHNIIFFLTPHRHR  IFFLTPHRH 0.4288 483 WB Large T DRB1_0701 197 IFFLTPHRHRVSAIN  IFFLTPHRH 0.4289 483 WB Large T DRB1_0901 229 NKEYLLYSALTRDPY  YLLYSALTR 0.4376 439 WB Large T DRB1_0901 230 KEYLLYSALTRDPYH  YLLYSALTR 0.4372 441 WB Large T DRB1_0901 72 PDFGTWNSSEVPTYG  WNSSEVPTY 0.4364 445 WB Large T DRB1_0901 71 QPDFGTWNSSEVPTY  FGTWNSSEV 0.4355 449 WB Large T DRB1_0901 228 VNKEYLLYSALTRDP  YLLYSALTR 0.4325 464 WB Large T DRB1_0901 384 AVLEQYMAGVAWLHC  LEQYMAGVA 0.4270 493 WB Large T DRB1_0901 383 NAVLEQYMAGVAWLH  LEQYMAGVA 0.4259 499 WB Large T DRB1_1101 232 YLLYSALTRDPYHII  YSALTRDPY 0.4594 347 WB Large T DRB1_1101 233 LLYSALTRDPYHIIE  YSALTRDPY 0.4586 350 WB Large T DRB1_1101 231 EYLLYSALTRDPYHI  YSALTRDPY 0.4552 363 WB Large T DRB1_1101 229 NKEYLLYSALTRDPY  YLLYSALTR 0.4548 364 WB Large T DRB1_1101 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.4550 364 WB Large T DRB1_1101 230 KEYLLYSALTRDPYH  YSALTRDPY 0.4537 369 WB Large T DRB1_1101 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4498 385 WB Large T DRB1_1101 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.4495 386 WB Large T DRB1_1101 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4483 391 WB Large T DRB1_1101 46 GGDEDKMKRMNTLYK  EDKMKRMNT 0.4433 413 WB Large T DRB1_1101 18 GLERAAWGNLPLMRK  AWGNLPLMR 0.4312 471 WB Large T DRB1_1101 19 LERAAWGNLPLMRKA  WGNLPLMRK 0.4311 471 WB Large T DRB1_1101 21 RAAWGNLPLMRKAYL  WGNLPLMRK 0.4288 483 WB Large T DRB1_1101 20 ERAAWGNLPLMRKAY  WGNLPLMRK 0.4279 488 WB Large T DRB1_1302 18 GLERAAWGNLPLMRK  LERAAWGNL 0.5752 99 WB Large T DRB1_1302 21 RAAWGNLPLMRKAYL  WGNLPLMRK 0.5714 103 WB Large T DRB1_1302 22 AAWGNLPLMRKAYLK  WGNLPLMRK 0.5704 104 WB Large T DRB1_1302 19 LERAAWGNLPLMRKA  WGNLPLMRK 0.5702 105 WB Large T DRB1_1302 20 ERAAWGNLPLMRKAY  WGNLPLMRK 0.5531 126 WB Large T DRB1_1302 285 EDVFLLLGMYLEFQY  FLLLGMYLE 0.5498 130 WB Large T DRB1_1302 445 CGGKALNVNLPMERL  LNVNLPMER 0.5476 134 WB Large T DRB1_1302 446 GGKALNVNLPMERLT  LNVNLPMER 0.5454 137 WB Large T DRB1_1302 566 LEKRILQSGMTLLLL  ILQSGMTLL 0.5431 140 WB Large T DRB1_1302 444 LCGGKALNVNLPMER  GKALNVNLP 0.5427 141 WB Large T DRB1_1302 565 LLEKRILQSGMTLLL  ILQSGMTLL 0.5420 142 WB Large T DRB1_1302 447 GKALNVNLPMERLTF  LNVNLPMER 0.5392 146 WB Large T DRB1_1302 284 CEDVFLLLGMYLEFQ  FLLLGMYLE 0.5383 148 WB Large T DRB1_1302 283 KCEDVFLLLGMYLEF  FLLLGMYLE 0.5363 151 WB Large T DRB1_1302 567 EKRILQSGMTLLLLL  ILQSGMTLL 0.5327 157 WB Large T DRB1_1302 282 TKCEDVFLLLGMYLE  VFLLLGMYL 0.5292 163 WB Large T DRB1_1302 568 KRILQSGMTLLLLLI  ILQSGMTLL 0.5282 165 WB Large T DRB1_1302 286 DVFLLLGMYLEFQYN  FLLLGMYLE 0.5258 169 WB Large T DRB1_1302 409 DFLHCVVFNVPKRRY  VVFNVPKRR 0.5112 198 WB Large T DRB1_1302 411 LHCVVFNVPKRRYWL  VFNVPKRRY 0.5079 205 WB Large T DRB1_1302 410 FLHCVVFNVPKRRYW  VFNVPKRRY 0.5074 206 WB Large T DRB1_1302 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.5012 221 WB Large T DRB1_1302 448 KALNVNLPMERLTFE  LNVNLPMER 0.4996 225 WB Large T DRB1_1302 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4986 227 WB Large T DRB1_1302 609 ISMYTFSRMKYNICM  MYTFSRMKY 0.4969 231 WB Large T DRB1_1302 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4966 232 WB Large T DRB1_1302 412 HCVVFNVPKRRYWLF  VFNVPKRRY 0.4955 235 WB Large T DRB1_1302 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.4940 239 WB Large T DRB1_1302 564 FLLEKRILQSGMTLL  KRILQSGMT 0.4938 239 WB Large T DRB1_1302 608 EISMYTFSRMKYNIC  ISMYTFSRM 0.4935 240 WB Large T DRB1_1302 24 WGNLPLMRKAYLKKC  WGNLPLMRK 0.4926 242 WB Large T DRB1_1302 23 AWGNLPLMRKAYLKK  WGNLPLMRK 0.4885 253 WB Large T DRB1_1302 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.4800 278 WB Large T DRB1_1302 487 LPSGHGINNLDSLRD  HGINNLDSL 0.4764 289 WB Large T DRB1_1302 489 SGHGINNLDSLRDYL  INNLDSLRD 0.4752 293 WB Large T DRB1_1302 488 PSGHGINNLDSLRDY  INNLDSLRD 0.4736 298 WB Large T DRB1_1302 569 RILQSGMTLLLLLIW  LQSGMTLLL 0.4720 303 WB Large T DRB1_1302 287 VFLLLGMYLEFQYNV  FLLLGMYLE 0.4711 306 WB Large T DRB1_1302 413 CVVFNVPKRRYWLFK  VFNVPKRRY 0.4581 352 WB Large T DRB1_1302 522 IFPPGLVTMNEYPVP  PGLVTMNEY 0.4560 360 WB Large T DRB1_1302 490 GHGINNLDSLRDYLD  INNLDSLRD 0.4532 371 WB Large T DRB1_1302 523 FPPGLVTMNEYPVPK  PGLVTMNEY 0.4489 389 WB Large T DRB1_1302 232 YLLYSALTRDPYHII  YSALTRDPY 0.4367 444 WB Large T DRB1_1302 491 HGINNLDSLRDYLDG  INNLDSLRD 0.4358 448 WB Large T DRB1_1302 570 ILQSGMTLLLLLIWF  ILQSGMTLL 0.4330 462 WB Large T DRB1_1302 449 ALNVNLPMERLTFEL  LNVNLPMER 0.4326 463 WB Large T DRB1_1302 607 SEISMYTFSRMKYNI  ISMYTFSRM 0.4327 463 WB Large T DRB1_1302 51 KMKRMNTLYKKMEQD  MKRMNTLYK 0.4272 492 WB Large T DRB1_1501 192 AGHNIIFFLTPHRHR  IIFFLTPHR 0.6526 43 SB Large T DRB1_1501 193 GHNIIFFLTPHRHRV  IIFFLTPHR 0.6507 44 SB Large T DRB1_1501 575 MTLLLLLIWFRPVAD  LLLLLIWFR 0.6509 44 SB Large T DRB1_1501 574 GMTLLLLLIWFRPVA  LLLLLIWFR 0.6462 46 SB Large T DRB1_1501 191 CAGHNIIFFLTPHRH  IIFFLTPHR 0.6427 48 SB Large T DRB1_1501 194 HNIIFFLTPHRHRVS  IIFFLTPHR 0.6416 48 SB Large T DRB1_1501 576 TLLLLLIWFRPVADF  LLLLLIWFR 0.6127 66 WB Large T DRB1_1501 577 LLLLLIWFRPVADFS  LLIWFRPVA 0.5958 79 WB Large T DRB1_1501 190 MCAGHNIIFFLTPHR  NIIFFLTPH 0.5914 83 WB Large T DRB1_1501 573 SGMTLLLLLIWFRPV  LLLLLIWFR 0.5875 87 WB Large T DRB1_1501 195 NIIFFLTPHRHRVSA  IIFFLTPHR 0.5848 89 WB Large T DRB1_1501 572 QSGMTLLLLLIWFRP  LLLLLIWFR 0.5640 112 WB Large T DRB1_1501 196 IIFFLTPHRHRVSAI  IIFFLTPHR 0.5515 128 WB Large T DRB1_1501 578 LLLLIWFRPVADFSK  LLIWFRPVA 0.5410 144 WB Large T DRB1_1501 571 LQSGMTLLLLLIWFR  TLLLLLIWF 0.5272 167 WB Large T DRB1_1501 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.5229 174 WB Large T DRB1_1501 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.5190 182 WB Large T DRB1_1501 24 WGNLPLMRKAYLKKC  LMRKAYLKK 0.5176 185 WB Large T DRB1_1501 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.5153 190 WB Large T DRB1_1501 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.5147 191 WB Large T DRB1_1501 23 AWGNLPLMRKAYLKK  LPLMRKAYL 0.5076 206 WB Large T DRB1_1501 25 GNLPLMRKAYLKKCK  LMRKAYLKK 0.5063 209 WB Large T DRB1_1501 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.5026 217 WB Large T DRB1_1501 26 NLPLMRKAYLKKCKE  LMRKAYLKK 0.4961 233 WB Large T DRB1_1501 548 DFRPKIYLRKSLQNS  DFRPKIYLR 0.4942 238 WB Large T DRB1_1501 227 GVNKEYLLYSALTRD  YLLYSALTR 0.4878 255 WB Large T DRB1_1501 228 VNKEYLLYSALTRDP  YLLYSALTR 0.4864 259 WB Large T DRB1_1501 229 NKEYLLYSALTRDPY  YLLYSALTR 0.4863 259 WB Large T DRB1_1501 230 KEYLLYSALTRDPYH  YLLYSALTR 0.4859 260 WB Large T DRB1_1501 27 LPLMRKAYLKKCKEF  LMRKAYLKK 0.4850 263 WB Large T DRB1_1501 409 DFLHCVVFNVPKRRY  CVVFNVPKR 0.4823 271 WB Large T DRB1_1501 410 FLHCVVFNVPKRRYW  CVVFNVPKR 0.4819 272 WB Large T DRB1_1501 226 KGVNKEYLLYSALTR  VNKEYLLYS 0.4792 280 WB Large T DRB1_1501 411 LHCVVFNVPKRRYWL  CVVFNVPKR 0.4791 280 WB Large T DRB1_1501 543 FVRQIDFRPKIYLRK  DFRPKIYLR 0.4749 293 WB Large T DRB1_1501 544 VRQIDFRPKIYLRKS  DFRPKIYLR 0.4739 297 WB Large T DRB1_1501 542 RFVRQIDFRPKIYLR  VRQIDFRPK 0.4731 299 WB Large T DRB1_1501 408 FDFLHCVVFNVPKRR  CVVFNVPKR 0.4728 300 WB Large T DRB1_1501 579 LLLIWFRPVADFSKD  LLIWFRPVA 0.4695 311 WB Large T DRB1_1501 13 LMDLLGLERAAWGNL  LMDLLGLER 0.4683 315 WB Large T DRB1_1501 549 FRPKIYLRKSLQNSE  YLRKSLQNS 0.4683 315 WB Large T DRB1_1501 11 MELMDLLGLERAAWG  LMDLLGLER 0.4651 326 WB Large T DRB1_1501 142 SDLHQFLSQAVFSNR  LHQFLSQAV 0.4611 341 WB Large T DRB1_1501 413 CVVFNVPKRRYWLFK  CVVFNVPKR 0.4554 362 WB Large T DRB1_1501 169 KAQILYKKLMEKYSV  ILYKKLMEK 0.4523 375 WB Large T DRB1_1501 170 AQILYKKLMEKYSVT  ILYKKLMEK 0.4511 379 WB Large T DRB1_1501 546 QIDFRPKIYLRKSLQ  DFRPKIYLR 0.4502 383 WB Large T DRB1_1501 419 PKRRYWLFKGPIDSG  WLFKGPIDS 0.4498 385 WB Large T DRB1_1501 418 VPKRRYWLFKGPIDS  KRRYWLFKG 0.4458 402 WB Large T DRB1_1501 547 IDFRPKIYLRKSLQN  FRPKIYLRK 0.4373 440 WB Large T DRB1_1501 420 KRRYWLFKGPIDSGK  WLFKGPIDS 0.4350 452 WB Large T DRB1_1501 414 VVFNVPKRRYWLFKG  PKRRYWLFK 0.4334 460 WB Large T DRB1_1501 28 PLMRKAYLKKCKEFH  LMRKAYLKK 0.4332 461 WB Large T DRB1_1501 51 KMKRMNTLYKKMEQD  MKRMNTLYK 0.4331 461 WB Large T DRB1_1501 172 ILYKKLMEKYSVTFI  ILYKKLMEK 0.4319 467 WB Large T DRB1_1501 550 RPKIYLRKSLQNSEF  YLRKSLQNS 0.4316 469 WB Large T DRB1_1501 545 RQIDFRPKIYLRKSL  DFRPKIYLR 0.4312 471 WB Large T DRB1_1501 580 LLIWFRPVADFSKDI  LLIWFRPVA 0.4297 479 WB Large T DRB1_1501 412 HCVVFNVPKRRYWLF  CVVFNVPKR 0.4294 480 WB Large T DRB1_1501 10 SMELMDLLGLERAAW  LMDLLGLER 0.4261 497 WB Large T DRB4_0101 609 ISMYTFSRMKYNICM  FSRMKYNIC 0.5682 107 WB Large T DRB4_0101 611 MYTFSRMKYNICMGK  FSRMKYNIC 0.5289 163 WB Large T DRB4_0101 608 EISMYTFSRMKYNIC  ISMYTFSRM 0.5272 167 WB Large T DRB4_0101 612 YTFSRMKYNICMGKC  FSRMKYNIC 0.5271 167 WB Large T DRB4_0101 610 SMYTFSRMKYNICMG  FSRMKYNIC 0.5243 172 WB Large T DRB4_0101 576 TLLLLLIWFRPVADF  LIWFRPVAD 0.4721 302 WB Large T DRB4_0101 194 HNIIFFLTPHRHRVS  IFFLTPHRH 0.4700 309 WB Large T DRB4_0101 193 GHNIIFFLTPHRHRV  IFFLTPHRH 0.4668 320 WB Large T DRB4_0101 192 AGHNIIFFLTPHRHR  IFFLTPHRH 0.4660 323 WB Large T DRB4_0101 195 NIIFFLTPHRHRVSA  IFFLTPHRH 0.4640 330 WB Large T DRB4_0101 541 ARFVRQIDFRPKIYL  VRQIDFRPK 0.4637 331 WB Large T DRB4_0101 577 LLLLLIWFRPVADFS  LIWFRPVAD 0.4628 334 WB Large T DRB4_0101 191 CAGHNIIFFLTPHRH  IIFFLTPHR 0.4583 351 WB Large T DRB4_0101 613 TFSRMKYNICMGKCI  FSRMKYNIC 0.4575 354 WB Large T DRB4_0101 542 RFVRQIDFRPKIYLR  VRQIDFRPK 0.4556 362 WB Large T DRB4_0101 578 LLLLIWFRPVADFSK  LIWFRPVAD 0.4526 373 WB Large T DRB4_0101 614 FSRMKYNICMGKCIL  FSRMKYNIC 0.4368 443 WB Large T DRB4_0101 579 LLLIWFRPVADFSKD  LIWFRPVAD 0.4362 446 WB Large T DRB4_0101 539 LQARFVRQIDFRPKI  VRQIDFRPK 0.4355 449 WB Large T DRB4_0101 575 MTLLLLLIWFRPVAD  LLLIWFRPV 0.4344 455 WB Large T DRB4_0101 538 TLQARFVRQIDFRPK  FVRQIDFRP 0.4341 456 WB Large T DRB4_0101 540 QARFVRQIDFRPKIY  VRQIDFRPK 0.4260 498 WB Large T DRB5_0101 543 FVRQIDFRPKIYLRK  RQIDFRPKI 0.6349 52 WB Large T DRB5_0101 544 VRQIDFRPKIYLRKS  FRPKIYLRK 0.6346 52 WB Large T DRB5_0101 545 RQIDFRPKIYLRKSL  FRPKIYLRK 0.6343 52 WB Large T DRB5_0101 546 QIDFRPKIYLRKSLQ  FRPKIYLRK 0.6326 53 WB Large T DRB5_0101 547 IDFRPKIYLRKSLQN  FRPKIYLRK 0.6322 53 WB Large T DRB5_0101 411 LHCVVFNVPKRRYWL  VVFNVPKRR 0.5655 110 WB Large T DRB5_0101 412 HCVVFNVPKRRYWLF  VVFNVPKRR 0.5631 113 WB Large T DRB5_0101 410 FLHCVVFNVPKRRYW  VVFNVPKRR 0.5614 115 WB Large T DRB5_0101 409 DFLHCVVFNVPKRRY  VVFNVPKRR 0.5437 139 WB Large T DRB5_0101 548 DFRPKIYLRKSLQNS  FRPKIYLRK 0.5361 151 WB Large T DRB5_0101 549 FRPKIYLRKSLQNSE  FRPKIYLRK 0.5359 152 WB Large T DRB5_0101 255 KEHDFNPEEPEETKQ  FNPEEPEET 0.5183 183 WB Large T DRB5_0101 254 LKEHDFNPEEPEETK  FNPEEPEET 0.5181 184 WB Large T DRB5_0101 256 EHDFNPEEPEETKQV  FNPEEPEET 0.5168 186 WB Large T DRB5_0101 253 GLKEHDFNPEEPEET  GLKEHDFNP 0.5161 188 WB Large T DRB5_0101 257 HDFNPEEPEETKQVS  FNPEEPEET 0.5162 188 WB Large T DRB5_0101 408 FDFLHCVVFNVPKRR  CVVFNVPKR 0.5052 211 WB Large T DRB5_0101 413 CVVFNVPKRRYWLFK  VVFNVPKRR 0.5006 222 WB Large T DRB5_0101 84 TYGTEEWESWWSSFN  TEEWESWWS 0.4988 227 WB Large T DRB5_0101 85 YGTEEWESWWSSFNE  WESWWSSFN 0.4977 229 WB Large T DRB5_0101 88 EEWESWWSSFNEKWD  WESWWSSFN 0.4975 230 WB Large T DRB5_0101 87 TEEWESWWSSFNEKW  WESWWSSFN 0.4963 233 WB Large T DRB5_0101 86 GTEEWESWWSSFNEK  WESWWSSFN 0.4952 235 WB Large T DRB5_0101 677 KGFQCFKRPKTPPPK  FQCFKRPKT 0.4816 273 WB Large T DRB5_0101 49 EDKMKRMNTLYKKME  MKRMNTLYK 0.4763 289 WB Large T DRB5_0101 50 DKMKRMNTLYKKMEQ  MKRMNTLYK 0.4758 290 WB Large T DRB5_0101 48 DEDKMKRMNTLYKKM  MKRMNTLYK 0.4726 301 WB Large T DRB5_0101 414 VVFNVPKRRYWLFKG  VVFNVPKRR 0.4695 311 WB Large T DRB5_0101 47 GDEDKMKRMNTLYKK  MKRMNTLYK 0.4617 338 WB Large T DRB5_0101 194 HNIIFFLTPHRHRVS  FFLTPHRHR 0.4587 350 WB Large T DRB5_0101 46 GGDEDKMKRMNTLYK  DKMKRMNTL 0.4567 357 WB Large T DRB5_0101 193 GHNIIFFLTPHRHRV  FFLTPHRHR 0.4542 367 WB Large T DRB5_0101 195 NIIFFLTPHRHRVSA  FFLTPHRHR 0.4419 419 WB Large T DRB5_0101 119 TADSQHSTPPKKKRK  QHSTPPKKK 0.4363 446 WB Large T DRB5_0101 120 ADSQHSTPPKKKRKV  QHSTPPKKK 0.4331 461 WB Large T DRB5_0101 259 FNPEEPEETKQVSWK  FNPEEPEET 0.4320 467 WB Large T DRB5_0101 53 KRMNTLYKKMEQDVK  KRMNTLYKK 0.4284 485 WB Large T DRB5_0101 22 AAWGNLPLMRKAYLK  WGNLPLMRK 0.4268 494 WB Large T SEQ ID NOS.: 60258-61275

Preferred BK virus fragments of Agnoprotein capable of interacting with one or more MHC class 2 molecules are listed in Table T.

TABLE T Prediction of BK virus Agnoprotein specific MHC class 2, 15-mer peptide binders for 14 MHC class 2 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHCII/ database. The MHC class 2 molecules for which no binders were found are not listed. 1-log50k affinity Bind Identity Allele pos peptide  core (aff) (nM) Level DRB1_0101 8 LVVLRQLSRQASVKV  LRQLSRQAS 0.6877 29 SB Agno DRB1_0101 9 VVLRQLSRQASVKVG  LSRQASVKV 0.6820 31 SB Agno DRB1_0101 10 VLRQLSRQASVKVGK  LSRQASVKV 0.6587 40 SB Agno DRB1_0101 11 LRQLSRQASVKVGKT  LSRQASVKV 0.6595 40 SB Agno DRB1_0101 5 PKNLVVLRQLSRQAS  VLRQLSRQA 0.6455 46 SB Agno DRB1_0101 7 NLVVLRQLSRQASVK  VLRQLSRQA 0.6439 47 SB Agno DRB1_0101 6 KNLVVLRQLSRQASV  VLRQLSRQA 0.6410 49 SB Agno DRB1_0101 12 RQLSRQASVKVGKTW  LSRQASVKV 0.6369 51 WB Agno DRB1_0101 14 LSRQASVKVGKTWTG  LSRQASVKV 0.6206 61 WB Agno DRB1_0101 18 ASVKVGKTWTGTKKR  VKVGKTWTG 0.5679 107 WB Agno DRB1_0101 17 QASVKVGKTWTGTKK  VKVGKTWTG 0.5669 108 WB Agno DRB1_0101 15 SRQASVKVGKTWTGT  VKVGKTWTG 0.5640 112 WB Agno DRB1_0101 16 RQASVKVGKTWTGTK  VKVGKTWTG 0.5640 112 WB Agno DRB1_0101 4 EPKNLVVLRQLSRQA  PKNLVVLRQ 0.5604 116 WB Agno DRB1_0101 13 QLSRQASVKVGKTWT  LSRQASVKV 0.5447 138 WB Agno DRB1_0101 19 SVKVGKTWTGTKKRA  VKVGKTWTG 0.4852 263 WB Agno DRB1_0101 20 VKVGKTWTGTKKRAQ  VKVGKTWTG 0.4749 293 WB Agno DRB1_0401 8 LVVLRQLSRQASVKV  VLRQLSRQA 0.4745 295 WB Agno DRB1_0401 10 VLRQLSRQASVKVGK  LSRQASVKV 0.4500 384 WB Agno DRB1_0401 9 VVLRQLSRQASVKVG  LSRQASVKV 0.4476 394 WB Agno DRB1_0401 11 LRQLSRQASVKVGKT  LSRQASVKV 0.4393 431 WB Agno DRB1_0401 12 RQLSRQASVKVGKTW  LSRQASVKV 0.4380 437 WB Agno DRB1_0405 55 DGKNKSTTALPAVKD  NKSTTALPA 0.4704 308 WB Agno DRB1_0405 56 GKNKSTTALPAVKDS  TTALPAVKD 0.4657 324 WB Agno DRB1_0405 57 KNKSTTALPAVKDSV  TTALPAVKD 0.4367 443 WB Agno DRB1_0405 58 NKSTTALPAVKDSVK  TTALPAVKD 0.4330 462 WB Agno DRB1_1101 8 LVVLRQLSRQASVKV  LRQLSRQAS 0.4614 340 WB Agno DRB1_1101 5 PKNLVVLRQLSRQAS  PKNLVVLRQ 0.4605 343 WB Agno DRB1_1101 6 KNLVVLRQLSRQASV  LRQLSRQAS 0.4594 347 WB Agno DRB1_1101 9 VVLRQLSRQASVKVG  LRQLSRQAS 0.4595 347 WB Agno DRB1_1101 7 NLVVLRQLSRQASVK  LRQLSRQAS 0.4579 352 WB Agno DRB1_1302 5 PKNLVVLRQLSRQAS  VVLRQLSRQ 0.5120 196 WB Agno DRB1_1302 8 LVVLRQLSRQASVKV  LRQLSRQAS 0.5035 215 WB Agno DRB1_1302 6 KNLVVLRQLSRQASV  LRQLSRQAS 0.5031 216 WB Agno DRB1_1302 9 VVLRQLSRQASVKVG  LRQLSRQAS 0.4904 248 WB Agno DRB1_1302 7 NLVVLRQLSRQASVK  LRQLSRQAS 0.4893 251 WB Agno DRB1_1302 3 CEPKNLVVLRQLSRQ  LVVLRQLSR 0.4329 462 WB Agno DRB1_1501 5 PKNLVVLRQLSRQAS  LVVLRQLSR 0.6754 34 SB Agno DRB1_1501 6 KNLVVLRQLSRQASV  LVVLRQLSR 0.6742 34 SB Agno DRB1_1501 4 EPKNLVVLRQLSRQA  LVVLRQLSR 0.6596 40 SB Agno DRB1_1501 3 CEPKNLVVLRQLSRQ  LVVLRQLSR 0.6209 60 WB Agno DRB1_1501 7 NLVVLRQLSRQASVK  LVVLRQLSR 0.6093 69 WB Agno DRB1_1501 8 LVVLRQLSRQASVKV  LVVLRQLSR 0.6010 75 WB Agno DRB1_1501 2 FCEPKNLVVLRQLSR  NLVVLRQLS 0.5977 78 WB Agno DRB1_1501 9 VVLRQLSRQASVKVG  LRQLSRQAS 0.4406 425 WB Agno DRB4_0101 35 RIFIFILELLLEFCR  ILELLLEFC 0.4266 494 WB Agno SEQ ID NOS: 61276-61367

Preferred Borrelia afzelli fragments of Osp C capable of interacting with one or more MHC class 1 and/or MHC class 2 molecules are listed in Table U.

TABLE U Prediction of MHC class 1 and 2 Borrelia afzelii OspC peptide binders. Prediction of 8-, 9-, 10-, 11-, 13-, 14-, 15-, 16-mer peptides were using the program displayed in FIG. 2 8 mers: MKKNTLSA; KKNTLSAI; KNTLSAIL; NTLSAILM; TLSAILMT; LSAILMTL; SAILMTLF; AILMTLFL; ILMTLFLF; LMTLFLFI; MTLFLFIS; TLFLFISC; LFLFISCN; FLFISCNN; LFISCNNS; FISCNNSG; ISCNNSGK; SCNNSGKG; CNNSGKGG; NNSGKGGD; NSGKGGDS; SGKGGDSA; GKGGDSAS; KGGDSAST; GGDSASTN; GDSASTNP; DSASTNPA; SASTNPAD; ASTNPADE; STNPADES; TNPADESA; NPADESAK; PADESAKG; ADESAKGP; DESAKGPN; ESAKGPNL; SAKGPNLT; AKGPNLTE; KGPNLTEI; GPNLTEIS; PNLTEISK; NLTEISKK; LTEISKKI; TEISKKIT; EISKKITD; ISKKITDS; SKKITDSN; KKITDSNA; KITDSNAF; ITDSNAFV; TDSNAFVL; DSNAFVLA; SNAFVLAV; NAFVLAVK; AFVLAVKE; FVLAVKEV; VLAVKEVE; LAVKEVET; AVKEVETL; VKEVETLV; KEVETLVS; EVETLVSS; VETLVSSI; ETLVSSID; TLVSSIDE; LVSSIDEL; VSSIDELA; SSIDELAN; SIDELANK; IDELANKA; DELANKAI; ELANKAIG; LANKAIGK; ANKAIGKK; NKAIGKKI; KAIGKKIQ; AIGKKIQQ; IGKKIQQN; GKKIQQNG; KKIQQNGL; KIQQNGLG; IQQNGLGA; QQNGLGAE; QNGLGAEA; NGLGAEAN; GLGAEANR; LGAEANRN; GAEANRNE; AEANRNES; EANRNESL; ANRNESLL; NRNESLLA; RNESLLAG; NESLLAGV; ESLLAGVH; SLLAGVHE; LLAGVHEI; LAGVHEIS; AGVHEIST; GVHEISTL; VHEISTLI; HEISTLIT; EISTLITE; ISTLITEK; STLITEKL; TLITEKLS; LITEKLSK; ITEKLSKL; TEKLSKLK; EKLSKLKN; KLSKLKNS; LSKLKNSG; SKLKNSGE; KLKNSGEL; LKNSGELK; KNSGELKA; NSGELKAK; SGELKAKI; GELKAKIE; ELKAKIED; LKAKIEDA; KAKIEDAK; AKIEDAKK; KIEDAKKC; IEDAKKCS; EDAKKCSE; DAKKCSEE; AKKCSEEF; KKCSEEFT; KCSEEFTN; CSEEFTNK; SEEFTNKL; EEFTNKLR; EFTNKLRV; FTNKLRVS; TNKLRVSH; NKLRVSHA; KLRVSHAD; LRVSHADL; RVSHADLG; VSHADLGK; SHADLGKQ; HADLGKQG; ADLGKQGV; DLGKQGVN; LGKQGVND; GKQGVNDD; KQGVNDDD; QGVNDDDA; GVNDDDAK; VNDDDAKK; NDDDAKKA; DDDAKKAI; DDAKKAIL; DAKKAILK; AKKAILKT; KKAILKTN; KAILKTNA; AILKTNAD; ILKTNADK; LKTNADKT; KTNADKTK; TNADKTKG; NADKTKGA; ADKTKGAE; DKTKGAEE; KTKGAEEL; TKGAEELG; KGAEELGK; GAEELGKL; AEELGKLF; EELGKLFK; ELGKLFKS; LGKLFKSV; GKLFKSVE; KLFKSVEG; LFKSVEGL; FKSVEGLV; KSVEGLVK; SVEGLVKA; VEGLVKAA; EGLVKAAQ; GLVKAAQE; LVKAAQEA; VKAAQEAL; KAAQEALT; AAQEALTN; AQEALTNS; QEALTNSV; EALTNSVK; ALTNSVKE; LTNSVKEL; TNSVKELT; NSVKELTS; SVKELTSP; VKELTSPV; KELTSPVV; ELTSPVVA; LTSPVVAE; TSPVVAES; SPVVAESP; PVVAESPK; VVAESPKK; VAESPKKP 9 mers: MKKNTLSAI; KKNTLSAIL; KNTLSAILM; NTLSAILMT; TLSAILMTL; LSAILMTLF; SAILMTLFL; AILMTLFLF; ILMTLFLFI; LMTLFLFIS; MTLFLFISC; TLFLFISCN; LFLFISCNN; FLFISCNNS; LFISCNNSG; FISCNNSGK; ISCNNSGKG; SCNNSGKGG; CNNSGKGGD; NNSGKGGDS; NSGKGGDSA; SGKGGDSAS; GKGGDSAST; KGGDSASTN; GGDSASTNP; GDSASTNPA; DSASTNPAD; SASTNPADE; ASTNPADES; STNPADESA; TNPADESAK; NPADESAKG; PADESAKGP; ADESAKGPN; DESAKGPNL; ESAKGPNLT; SAKGPNLTE; AKGPNLTEI; KGPNLTEIS; GPNLTEISK; PNLTEISKK; NLTEISKKI; LTEISKKIT; TEISKKITD; EISKKITDS; ISKKITDSN; SKKITDSNA; KKITDSNAF; KITDSNAFV; ITDSNAFVL; TDSNAFVLA; DSNAFVLAV; SNAFVLAVK; NAFVLAVKE; AFVLAVKEV; FVLAVKEVE; VLAVKEVET; LAVKEVETL; AVKEVETLV; VKEVETLVS; KEVETLVSS; EVETLVSSI; VETLVSSID; ETLVSSIDE; TLVSSIDEL; LVSSIDELA; VSSIDELAN; SSIDELANK; SIDELANKA; IDELANKAI; DELANKAIG; ELANKAIGK; LANKAIGKK; ANKAIGKKI; NKAIGKKIQ; KAIGKKIQQ; AIGKKIQQN; IGKKIQQNG; GKKIQQNGL; KKIQQNGLG; KIQQNGLGA; IQQNGLGAE; QQNGLGAEA; QNGLGAEAN; NGLGAEANR; GLGAEANRN; LGAEANRNE; GAEANRNES; AEANRNESL; EANRNESLL; ANRNESLLA; NRNESLLAG; RNESLLAGV; NESLLAGVH; ESLLAGVHE; SLLAGVHEI; LLAGVHEIS; LAGVHEIST; AGVHEISTL; GVHEISTLI; VHEISTLIT; HEISTLITE; EISTLITEK; ISTLITEKL; STLITEKLS; TLITEKLSK; LITEKLSKL; ITEKLSKLK; TEKLSKLKN; EKLSKLKNS; KLSKLKNSG; LSKLKNSGE; SKLKNSGEL; KLKNSGELK; LKNSGELKA; KNSGELKAK; NSGELKAKI; SGELKAKIE; GELKAKIED; ELKAKIEDA; LKAKIEDAK; KAKIEDAKK; AKIEDAKKC; KIEDAKKCS; IEDAKKCSE; EDAKKCSEE; DAKKCSEEF; AKKCSEEFT; KKCSEEFTN; KCSEEFTNK; CSEEFTNKL; SEEFTNKLR; EEFTNKLRV; EFTNKLRVS; FTNKLRVSH; TNKLRVSHA; NKLRVSHAD; KLRVSHADL; LRVSHADLG; RVSHADLGK; VSHADLGKQ; SHADLGKQG; HADLGKQGV; ADLGKQGVN; DLGKQGVND; LGKQGVNDD; GKQGVNDDD; KQGVNDDDA; QGVNDDDAK; GVNDDDAKK; VNDDDAKKA; NDDDAKKAI; DDDAKKAIL; DDAKKAILK; DAKKAILKT; AKKAILKTN; KKAILKTNA; KAILKTNAD; AILKTNADK; ILKTNADKT; LKTNADKTK; KTNADKTKG; TNADKTKGA; NADKTKGAE; ADKTKGAEE; DKTKGAEEL; KTKGAEELG; TKGAEELGK; KGAEELGKL; GAEELGKLF; AEELGKLFK; EELGKLFKS; ELGKLFKSV; LGKLFKSVE; GKLFKSVEG; KLFKSVEGL; LFKSVEGLV; FKSVEGLVK; KSVEGLVKA; SVEGLVKAA; VEGLVKAAQ; EGLVKAAQE; GLVKAAQEA; LVKAAQEAL; VKAAQEALT; KAAQEALTN; AAQEALTNS; AQEALTNSV; QEALTNSVK; EALTNSVKE; ALTNSVKEL; LTNSVKELT; TNSVKELTS; NSVKELTSP; SVKELTSPV; VKELTSPVV; KELTSPVVA; ELTSPVVAE; LTSPVVAES; TSPVVAESP; SPVVAESPK; PVVAESPKK; VVAESPKKP 10 mers: MKKNTLSAIL; KKNTLSAILM; KNTLSAILMT; NTLSAILMTL; TLSAILMTLF; LSAILMTLFL; SAILMTLFLF; AILMTLFLFI; ILMTLFLFIS; LMTLFLFISC; MTLFLFISCN; TLFLFISCNN; LFLFISCNNS; FLFISCNNSG; LFISCNNSGK; FISCNNSGKG; ISCNNSGKGG; SCNNSGKGGD; CNNSGKGGDS; NNSGKGGDSA; NSGKGGDSAS; SGKGGDSAST; GKGGDSASTN; KGGDSASTNP; GGDSASTNPA; GDSASTNPAD; DSASTNPADE; SASTNPADES; ASTNPADESA; STNPADESAK; TNPADESAKG; NPADESAKGP; PADESAKGPN; ADESAKGPNL; DESAKGPNLT; ESAKGPNLTE; SAKGPNLTEI; AKGPNLTEIS; KGPNLTEISK; GPNLTEISKK; PNLTEISKKI; NLTEISKKIT; LTEISKKITD; TEISKKITDS; EISKKITDSN; ISKKITDSNA; SKKITDSNAF; KKITDSNAFV; KITDSNAFVL; ITDSNAFVLA; TDSNAFVLAV; DSNAFVLAVK; SNAFVLAVKE; NAFVLAVKEV; AFVLAVKEVE; FVLAVKEVET; VLAVKEVETL; LAVKEVETLV; AVKEVETLVS; VKEVETLVSS; KEVETLVSSI; EVETLVSSID; VETLVSSIDE; ETLVSSIDEL; TLVSSIDELA; LVSSIDELAN; VSSIDELANK; SSIDELANKA; SIDELANKAI; IDELANKAIG; DELANKAIGK; ELANKAIGKK; LANKAIGKKI; ANKAIGKKIQ; NKAIGKKIQQ; KAIGKKIQQN; AIGKKIQQNG; IGKKIQQNGL; GKKIQQNGLG; KKIQQNGLGA; KIQQNGLGAE; IQQNGLGAEA; QQNGLGAEAN; QNGLGAEANR; NGLGAEANRN; GLGAEANRNE; LGAEANRNES; GAEANRNESL; AEANRNESLL; EANRNESLLA; ANRNESLLAG; NRNESLLAGV; RNESLLAGVH; NESLLAGVHE; ESLLAGVHEI; SLLAGVHEIS; LLAGVHEIST; LAGVHEISTL; AGVHEISTLI; GVHEISTLIT; VHEISTLITE; HEISTLITEK; EISTLITEKL; ISTLITEKLS; STLITEKLSK; TLITEKLSKL; LITEKLSKLK; ITEKLSKLKN; TEKLSKLKNS; EKLSKLKNSG; KLSKLKNSGE; LSKLKNSGEL; SKLKNSGELK; KLKNSGELKA; LKNSGELKAK; KNSGELKAKI; NSGELKAKIE; SGELKAKIED; GELKAKIEDA; ELKAKIEDAK; LKAKIEDAKK; KAKIEDAKKC; AKIEDAKKCS; KIEDAKKCSE; IEDAKKCSEE; EDAKKCSEEF; DAKKCSEEFT; AKKCSEEFTN; KKCSEEFTNK; KCSEEFTNKL; CSEEFTNKLR; SEEFTNKLRV; EEFTNKLRVS; EFTNKLRVSH; FTNKLRVSHA; TNKLRVSHAD; NKLRVSHADL; KLRVSHADLG; LRVSHADLGK; RVSHADLGKQ; VSHADLGKQG; SHADLGKQGV; HADLGKQGVN; ADLGKQGVND; DLGKQGVNDD; LGKQGVNDDD; GKQGVNDDDA; KQGVNDDDAK; QGVNDDDAKK; GVNDDDAKKA; VNDDDAKKAI; NDDDAKKAIL; DDDAKKAILK; DDAKKAILKT; DAKKAILKTN; AKKAILKTNA; KKAILKTNAD; KAILKTNADK; AILKTNADKT; ILKTNADKTK; LKTNADKTKG; KTNADKTKGA; TNADKTKGAE; NADKTKGAEE; ADKTKGAEEL; DKTKGAEELG; KTKGAEELGK; TKGAEELGKL; KGAEELGKLF; GAEELGKLFK; AEELGKLFKS; EELGKLFKSV; ELGKLFKSVE; LGKLFKSVEG; GKLFKSVEGL; KLFKSVEGLV; LFKSVEGLVK; FKSVEGLVKA; KSVEGLVKAA; SVEGLVKAAQ; VEGLVKAAQE; EGLVKAAQEA; GLVKAAQEAL; LVKAAQEALT; VKAAQEALTN; KAAQEALTNS; AAQEALTNSV; AQEALTNSVK; QEALTNSVKE; EALTNSVKEL; ALTNSVKELT; LTNSVKELTS; TNSVKELTSP; NSVKELTSPV; SVKELTSPVV; VKELTSPVVA; KELTSPVVAE; ELTSPVVAES; LTSPVVAESP; TSPVVAESPK; SPVVAESPKK; PVVAESPKKP 11 mers: MKKNTLSAILM; KKNTLSAILMT; KNTLSAILMTL; NTLSAILMTLF; TLSAILMTLFL; LSAILMTLFLF; SAILMTLFLFI; AILMTLFLFIS; ILMTLFLFISC; LMTLFLFISCN; MTLFLFISCNN; TLFLFISCNNS; LFLFISCNNSG; FLFISCNNSGK; LFISCNNSGKG; FISCNNSGKGG; ISCNNSGKGGD; SCNNSGKGGDS; CNNSGKGGDSA; NNSGKGGDSAS; NSGKGGDSAST; SGKGGDSASTN; GKGGDSASTNP; KGGDSASTNPA; GGDSASTNPAD; GDSASTNPADE; DSASTNPADES; SASTNPADESA; ASTNPADESAK; STNPADESAKG; TNPADESAKGP; NPADESAKGPN; PADESAKGPNL; ADESAKGPNLT; DESAKGPNLTE; ESAKGPNLTEI; SAKGPNLTEIS; AKGPNLTEISK; KGPNLTEISKK; GPNLTEISKKI; PNLTEISKKIT; NLTEISKKITD; LTEISKKITDS; TEISKKITDSN; EISKKITDSNA; ISKKITDSNAF; SKKITDSNAFV; KKITDSNAFVL; KITDSNAFVLA; ITDSNAFVLAV; TDSNAFVLAVK; DSNAFVLAVKE; SNAFVLAVKEV; NAFVLAVKEVE; AFVLAVKEVET; FVLAVKEVETL; VLAVKEVETLV; LAVKEVETLVS; AVKEVETLVSS; VKEVETLVSSI; KEVETLVSSID; EVETLVSSIDE; VETLVSSIDEL; ETLVSSIDELA; TLVSSIDELAN; LVSSIDELANK; VSSIDELANKA; SSIDELANKAI; SIDELANKAIG; IDELANKAIGK; DELANKAIGKK; ELANKAIGKKI; LANKAIGKKIQ; ANKAIGKKIQQ; NKAIGKKIQQN; KAIGKKIQQNG; AIGKKIQQNGL; IGKKIQQNGLG; GKKIQQNGLGA; KKIQQNGLGAE; KIQQNGLGAEA; IQQNGLGAEAN; QQNGLGAEANR; QNGLGAEANRN; NGLGAEANRNE; GLGAEANRNES; LGAEANRNESL; GAEANRNESLL; AEANRNESLLA; EANRNESLLAG; ANRNESLLAGV; NRNESLLAGVH; RNESLLAGVHE; NESLLAGVHEI; ESLLAGVHEIS; SLLAGVHEIST; LLAGVHEISTL; LAGVHEISTLI; AGVHEISTLIT; GVHEISTLITE; VHEISTLITEK; HEISTLITEKL; EISTLITEKLS; ISTLITEKLSK; STLITEKLSKL; TLITEKLSKLK; LITEKLSKLKN; ITEKLSKLKNS; TEKLSKLKNSG; EKLSKLKNSGE; KLSKLKNSGEL; LSKLKNSGELK; SKLKNSGELKA; KLKNSGELKAK; LKNSGELKAKI; KNSGELKAKIE; NSGELKAKIED; SGELKAKIEDA; GELKAKIEDAK; ELKAKIEDAKK; LKAKIEDAKKC; KAKIEDAKKCS; AKIEDAKKCSE; KIEDAKKCSEE; IEDAKKCSEEF; EDAKKCSEEFT; DAKKCSEEFTN; AKKCSEEFTNK; KKCSEEFTNKL; KCSEEFTNKLR; CSEEFTNKLRV; SEEFTNKLRVS; EEFTNKLRVSH; EFTNKLRVSHA; FTNKLRVSHAD; TNKLRVSHADL; NKLRVSHADLG; KLRVSHADLGK; LRVSHADLGKQ; RVSHADLGKQG; VSHADLGKQGV; SHADLGKQGVN; HADLGKQGVND; ADLGKQGVNDD; DLGKQGVNDDD; LGKQGVNDDDA; GKQGVNDDDAK; KQGVNDDDAKK; QGVNDDDAKKA; GVNDDDAKKAI; VNDDDAKKAIL; NDDDAKKAILK; DDDAKKAILKT; DDAKKAILKTN; DAKKAILKTNA; AKKAILKTNAD; KKAILKTNADK; KAILKTNADKT; AILKTNADKTK; ILKTNADKTKG; LKTNADKTKGA; KTNADKTKGAE; TNADKTKGAEE; NADKTKGAEEL; ADKTKGAEELG; DKTKGAEELGK; KTKGAEELGKL; TKGAEELGKLF; KGAEELGKLFK; GAEELGKLFKS; AEELGKLFKSV; EELGKLFKSVE; ELGKLFKSVEG; LGKLFKSVEGL; GKLFKSVEGLV; KLFKSVEGLVK; LFKSVEGLVKA; FKSVEGLVKAA; KSVEGLVKAAQ; SVEGLVKAAQE; VEGLVKAAQEA; EGLVKAAQEAL; GLVKAAQEALT; LVKAAQEALTN; VKAAQEALTNS; KAAQEALTNSV; AAQEALTNSVK; AQEALTNSVKE; QEALTNSVKEL; EALTNSVKELT; ALTNSVKELTS; LTNSVKELTSP; TNSVKELTSPV; NSVKELTSPVV; SVKELTSPVVA; VKELTSPVVAE; KELTSPVVAES; ELTSPVVAESP; LTSPVVAESPK; TSPVVAESPKK; SPVVAESPKKP; 13 mers: MKKNTLSAILMTL; KKNTLSAILMTLF; KNTLSAILMTLFL; NTLSAILMTLFLF; TLSAILMTLFLFI; LSAILMTLFLFIS; SAILMTLFLFISC; AILMTLFLFISCN; ILMTLFLFISCNN; LMTLFLFISCNNS; MTLFLFISCNNSG; TLFLFISCNNSGK; LFLFISCNNSGKG; FLFISCNNSGKGG; LFISCNNSGKGGD; FISCNNSGKGGDS; ISCNNSGKGGDSA; SCNNSGKGGDSAS; CNNSGKGGDSAST; NNSGKGGDSASTN; NSGKGGDSASTNP; SGKGGDSASTNPA; GKGGDSASTNPAD; KGGDSASTNPADE; GGDSASTNPADES; GDSASTNPADESA; DSASTNPADESAK; SASTNPADESAKG; ASTNPADESAKGP; STNPADESAKGPN; TNPADESAKGPNL; NPADESAKGPNLT; PADESAKGPNLTE; ADESAKGPNLTEI; DESAKGPNLTEIS; ESAKGPNLTEISK; SAKGPNLTEISKK; AKGPNLTEISKKI; KGPNLTEISKKIT; GPNLTEISKKITD; PNLTEISKKITDS; NLTEISKKITDSN; LTEISKKITDSNA; TEISKKITDSNAF; EISKKITDSNAFV; ISKKITDSNAFVL; SKKITDSNAFVLA; KKITDSNAFVLAV; KITDSNAFVLAVK; ITDSNAFVLAVKE; TDSNAFVLAVKEV; DSNAFVLAVKEVE; SNAFVLAVKEVET; NAFVLAVKEVETL; AFVLAVKEVETLV; FVLAVKEVETLVS; VLAVKEVETLVSS; LAVKEVETLVSSI; AVKEVETLVSSID; VKEVETLVSSIDE; KEVETLVSSIDEL; EVETLVSSIDELA; VETLVSSIDELAN; ETLVSSIDELANK; TLVSSIDELANKA; LVSSIDELANKAI; VSSIDELANKAIG; SSIDELANKAIGK; SIDELANKAIGKK; IDELANKAIGKKI; DELANKAIGKKIQ; ELANKAIGKKIQQ; LANKAIGKKIQQN; ANKAIGKKIQQNG; NKAIGKKIQQNGL; KAIGKKIQQNGLG; AIGKKIQQNGLGA; IGKKIQQNGLGAE; GKKIQQNGLGAEA; KKIQQNGLGAEAN; KIQQNGLGAEANR; IQQNGLGAEANRN; QQNGLGAEANRNE; QNGLGAEANRNES; NGLGAEANRNESL; GLGAEANRNESLL; LGAEANRNESLLA; GAEANRNESLLAG; AEANRNESLLAGV; EANRNESLLAGVH; ANRNESLLAGVHE; NRNESLLAGVHEI; RNESLLAGVHEIS; NESLLAGVHEIST; ESLLAGVHEISTL; SLLAGVHEISTLI; LLAGVHEISTLIT; LAGVHEISTLITE; AGVHEISTLITEK; GVHEISTLITEKL; VHEISTLITEKLS; HEISTLITEKLSK; EISTLITEKLSKL; ISTLITEKLSKLK; STLITEKLSKLKN; TLITEKLSKLKNS; LITEKLSKLKNSG; ITEKLSKLKNSGE; TEKLSKLKNSGEL; EKLSKLKNSGELK; KLSKLKNSGELKA; LSKLKNSGELKAK; SKLKNSGELKAKI; KLKNSGELKAKIE; LKNSGELKAKIED; KNSGELKAKIEDA; NSGELKAKIEDAK; SGELKAKIEDAKK; GELKAKIEDAKKC; ELKAKIEDAKKCS; LKAKIEDAKKCSE; KAKIEDAKKCSEE; AKIEDAKKCSEEF; KIEDAKKCSEEFT; IEDAKKCSEEFTN; EDAKKCSEEFTNK; DAKKCSEEFTNKL; AKKCSEEFTNKLR; KKCSEEFTNKLRV; KCSEEFTNKLRVS; CSEEFTNKLRVSH; SEEFTNKLRVSHA; EEFTNKLRVSHAD; EFTNKLRVSHADL; FTNKLRVSHADLG; TNKLRVSHADLGK; NKLRVSHADLGKQ; KLRVSHADLGKQG; LRVSHADLGKQGV; RVSHADLGKQGVN; VSHADLGKQGVND; SHADLGKQGVNDD; HADLGKQGVNDDD; ADLGKQGVNDDDA; DLGKQGVNDDDAK; LGKQGVNDDDAKK; GKQGVNDDDAKKA; KQGVNDDDAKKAI; QGVNDDDAKKAIL; GVNDDDAKKAILK; VNDDDAKKAILKT; NDDDAKKAILKTN; DDDAKKAILKTNA; DDAKKAILKTNAD; DAKKAILKTNADK; AKKAILKTNADKT; KKAILKTNADKTK; KAILKTNADKTKG; AILKTNADKTKGA; ILKTNADKTKGAE; LKTNADKTKGAEE; KTNADKTKGAEEL; TNADKTKGAEELG; NADKTKGAEELGK; ADKTKGAEELGKL; DKTKGAEELGKLF; KTKGAEELGKLFK; TKGAEELGKLFKS; KGAEELGKLFKSV; GAEELGKLFKSVE; AEELGKLFKSVEG; EELGKLFKSVEGL; ELGKLFKSVEGLV; LGKLFKSVEGLVK; GKLFKSVEGLVKA; KLFKSVEGLVKAA; LFKSVEGLVKAAQ; FKSVEGLVKAAQE; KSVEGLVKAAQEA; SVEGLVKAAQEAL; VEGLVKAAQEALT; EGLVKAAQEALTN; GLVKAAQEALTNS; LVKAAQEALTNSV; VKAAQEALTNSVK; KAAQEALTNSVKE; AAQEALTNSVKEL; AQEALTNSVKELT; QEALTNSVKELTS; EALTNSVKELTSP; ALTNSVKELTSPV; LTNSVKELTSPVV; TNSVKELTSPVVA; NSVKELTSPVVAE; SVKELTSPVVAES; VKELTSPVVAESP; KELTSPVVAESPK; ELTSPVVAESPKK; LTSPVVAESPKKP 14 mers: MKKNTLSAILMTLF; KKNTLSAILMTLFL; KNTLSAILMTLFLF; NTLSAILMTLFLFI; TLSAILMTLFLFIS; LSAILMTLFLFISC; SAILMTLFLFISCN; AILMTLFLFISCNN; ILMTLFLFISCNNS; LMTLFLFISCNNSG; MTLFLFISCNNSGK; TLFLFISCNNSGKG; LFLFISCNNSGKGG; FLFISCNNSGKGGD; LFISCNNSGKGGDS; FISCNNSGKGGDSA; ISCNNSGKGGDSAS; SCNNSGKGGDSAST; CNNSGKGGDSASTN; NNSGKGGDSASTNP; NSGKGGDSASTNPA; SGKGGDSASTNPAD; GKGGDSASTNPADE; KGGDSASTNPADES; GGDSASTNPADESA; GDSASTNPADESAK; DSASTNPADESAKG; SASTNPADESAKGP; ASTNPADESAKGPN; STNPADESAKGPNL; TNPADESAKGPNLT; NPADESAKGPNLTE; PADESAKGPNLTEI; ADESAKGPNLTEIS; DESAKGPNLTEISK; ESAKGPNLTEISKK; SAKGPNLTEISKKI; AKGPNLTEISKKIT; KGPNLTEISKKITD; GPNLTEISKKITDS; PNLTEISKKITDSN; NLTEISKKITDSNA; LTEISKKITDSNAF; TEISKKITDSNAFV; EISKKITDSNAFVL; ISKKITDSNAFVLA; SKKITDSNAFVLAV; KKITDSNAFVLAVK; KITDSNAFVLAVKE; ITDSNAFVLAVKEV; TDSNAFVLAVKEVE; DSNAFVLAVKEVET; SNAFVLAVKEVETL; NAFVLAVKEVETLV; AFVLAVKEVETLVS; FVLAVKEVETLVSS; VLAVKEVETLVSSI; LAVKEVETLVSSID; AVKEVETLVSSIDE; VKEVETLVSSIDEL; KEVETLVSSIDELA; EVETLVSSIDELAN; VETLVSSIDELANK; ETLVSSIDELANKA; TLVSSIDELANKAI; LVSSIDELANKAIG; VSSIDELANKAIGK; SSIDELANKAIGKK; SIDELANKAIGKKI; IDELANKAIGKKIQ; DELANKAIGKKIQQ; ELANKAIGKKIQQN; LANKAIGKKIQQNG; ANKAIGKKIQQNGL; NKAIGKKIQQNGLG; KAIGKKIQQNGLGA; AIGKKIQQNGLGAE; IGKKIQQNGLGAEA; GKKIQQNGLGAEAN; KKIQQNGLGAEANR; KIQQNGLGAEANRN; IQQNGLGAEANRNE; QQNGLGAEANRNES; QNGLGAEANRNESL; NGLGAEANRNESLL; GLGAEANRNESLLA; LGAEANRNESLLAG; GAEANRNESLLAGV; AEANRNESLLAGVH; EANRNESLLAGVHE; ANRNESLLAGVHEI; NRNESLLAGVHEIS; RNESLLAGVHEIST; NESLLAGVHEISTL; ESLLAGVHEISTLI; SLLAGVHEISTLIT; LLAGVHEISTLITE; LAGVHEISTLITEK; AGVHEISTLITEKL; GVHEISTLITEKLS; VHEISTLITEKLSK; HEISTLITEKLSKL; EISTLITEKLSKLK; ISTLITEKLSKLKN; STLITEKLSKLKNS; TLITEKLSKLKNSG; LITEKLSKLKNSGE; ITEKLSKLKNSGEL; TEKLSKLKNSGELK; EKLSKLKNSGELKA; KLSKLKNSGELKAK; LSKLKNSGELKAKI; SKLKNSGELKAKIE; KLKNSGELKAKIED; LKNSGELKAKIEDA; KNSGELKAKIEDAK; NSGELKAKIEDAKK; SGELKAKIEDAKKC; GELKAKIEDAKKCS; ELKAKIEDAKKCSE; LKAKIEDAKKCSEE; KAKIEDAKKCSEEF; AKIEDAKKCSEEFT; KIEDAKKCSEEFTN; IEDAKKCSEEFTNK; EDAKKCSEEFTNKL; DAKKCSEEFTNKLR; AKKCSEEFTNKLRV; KKCSEEFTNKLRVS; KCSEEFTNKLRVSH; CSEEFTNKLRVSHA; SEEFTNKLRVSHAD; EEFTNKLRVSHADL; EFTNKLRVSHADLG; FTNKLRVSHADLGK; TNKLRVSHADLGKQ; NKLRVSHADLGKQG; KLRVSHADLGKQGV; LRVSHADLGKQGVN; RVSHADLGKQGVND; VSHADLGKQGVNDD; SHADLGKQGVNDDD; HADLGKQGVNDDDA; ADLGKQGVNDDDAK; DLGKQGVNDDDAKK; LGKQGVNDDDAKKA; GKQGVNDDDAKKAI; KQGVNDDDAKKAIL; QGVNDDDAKKAILK; GVNDDDAKKAILKT; VNDDDAKKAILKTN; NDDDAKKAILKTNA; DDDAKKAILKTNAD; DDAKKAILKTNADK; DAKKAILKTNADKT; AKKAILKTNADKTK; KKAILKTNADKTKG; KAILKTNADKTKGA; AILKTNADKTKGAE; ILKTNADKTKGAEE; LKTNADKTKGAEEL; KTNADKTKGAEELG; TNADKTKGAEELGK; NADKTKGAEELGKL; ADKTKGAEELGKLF; DKTKGAEELGKLFK; KTKGAEELGKLFKS; TKGAEELGKLFKSV; KGAEELGKLFKSVE; GAEELGKLFKSVEG; AEELGKLFKSVEGL; EELGKLFKSVEGLV; ELGKLFKSVEGLVK; LGKLFKSVEGLVKA; GKLFKSVEGLVKAA; KLFKSVEGLVKAAQ; LFKSVEGLVKAAQE; FKSVEGLVKAAQEA; KSVEGLVKAAQEAL; SVEGLVKAAQEALT; VEGLVKAAQEALTN; EGLVKAAQEALTNS; GLVKAAQEALTNSV; LVKAAQEALTNSVK; VKAAQEALTNSVKE; KAAQEALTNSVKEL; AAQEALTNSVKELT; AQEALTNSVKELTS; QEALTNSVKELTSP; EALTNSVKELTSPV; ALTNSVKELTSPVV; LTNSVKELTSPVVA; TNSVKELTSPVVAE; NSVKELTSPVVAES; SVKELTSPVVAESP; VKELTSPVVAESPK; KELTSPVVAESPKK; ELTSPVVAESPKKP 15 mers: MKKNTLSAILMTLFL; KKNTLSAILMTLFLF; KNTLSAILMTLFLFI; NTLSAILMTLFLFIS; TLSAILMTLFLFISC; LSAILMTLFLFISCN; SAILMTLFLFISCNN; AILMTLFLFISCNNS; ILMTLFLFISCNNSG; LMTLFLFISCNNSGK; MTLFLFISCNNSGKG; TLFLFISCNNSGKGG; LFLFISCNNSGKGGD; FLFISCNNSGKGGDS; LFISCNNSGKGGDSA; FISCNNSGKGGDSAS; ISCNNSGKGGDSAST; SCNNSGKGGDSASTN; CNNSGKGGDSASTNP; NNSGKGGDSASTNPA; NSGKGGDSASTNPAD; SGKGGDSASTNPADE; GKGGDSASTNPADES; KGGDSASTNPADESA; GGDSASTNPADESAK; GDSASTNPADESAKG; DSASTNPADESAKGP; SASTNPADESAKGPN; ASTNPADESAKGPNL; STNPADESAKGPNLT; TNPADESAKGPNLTE; NPADESAKGPNLTEI; PADESAKGPNLTEIS; ADESAKGPNLTEISK; DESAKGPNLTEISKK; ESAKGPNLTEISKKI; SAKGPNLTEISKKIT; AKGPNLTEISKKITD; KGPNLTEISKKITDS; GPNLTEISKKITDSN; PNLTEISKKITDSNA; NLTEISKKITDSNAF; LTEISKKITDSNAFV; TEISKKITDSNAFVL; EISKKITDSNAFVLA; ISKKITDSNAFVLAV; SKKITDSNAFVLAVK; KKITDSNAFVLAVKE; KITDSNAFVLAVKEV; ITDSNAFVLAVKEVE; TDSNAFVLAVKEVET; DSNAFVLAVKEVETL; SNAFVLAVKEVETLV; NAFVLAVKEVETLVS; AFVLAVKEVETLVSS; FVLAVKEVETLVSSI; VLAVKEVETLVSSID; LAVKEVETLVSSIDE; AVKEVETLVSSIDEL; VKEVETLVSSIDELA; KEVETLVSSIDELAN; EVETLVSSIDELANK; VETLVSSIDELANKA; ETLVSSIDELANKAI; TLVSSIDELANKAIG; LVSSIDELANKAIGK; VSSIDELANKAIGKK; SSIDELANKAIGKKI; SIDELANKAIGKKIQ; IDELANKAIGKKIQQ; DELANKAIGKKIQQN; ELANKAIGKKIQQNG; LANKAIGKKIQQNGL; ANKAIGKKIQQNGLG; NKAIGKKIQQNGLGA; KAIGKKIQQNGLGAE; AIGKKIQQNGLGAEA; IGKKIQQNGLGAEAN; GKKIQQNGLGAEANR; KKIQQNGLGAEANRN; KIQQNGLGAEANRNE; IQQNGLGAEANRNES; QQNGLGAEANRNESL; QNGLGAEANRNESLL; NGLGAEANRNESLLA; GLGAEANRNESLLAG; LGAEANRNESLLAGV; GAEANRNESLLAGVH; AEANRNESLLAGVHE; EANRNESLLAGVHEI; ANRNESLLAGVHEIS; NRNESLLAGVHEIST; RNESLLAGVHEISTL; NESLLAGVHEISTLI; ESLLAGVHEISTLIT; SLLAGVHEISTLITE; LLAGVHEISTLITEK; LAGVHEISTLITEKL; AGVHEISTLITEKLS; GVHEISTLITEKLSK; VHEISTLITEKLSKL; HEISTLITEKLSKLK; EISTLITEKLSKLKN; ISTLITEKLSKLKNS; STLITEKLSKLKNSG; TLITEKLSKLKNSGE; LITEKLSKLKNSGEL; ITEKLSKLKNSGELK; TEKLSKLKNSGELKA; EKLSKLKNSGELKAK; KLSKLKNSGELKAKI; LSKLKNSGELKAKIE; SKLKNSGELKAKIED; KLKNSGELKAKIEDA; LKNSGELKAKIEDAK; KNSGELKAKIEDAKK; NSGELKAKIEDAKKC; SGELKAKIEDAKKCS; GELKAKIEDAKKCSE; ELKAKIEDAKKCSEE; LKAKIEDAKKCSEEF; KAKIEDAKKCSEEFT; AKIEDAKKCSEEFTN; KIEDAKKCSEEFTNK; IEDAKKCSEEFTNKL; EDAKKCSEEFTNKLR; DAKKCSEEFTNKLRV; AKKCSEEFTNKLRVS; KKCSEEFTNKLRVSH; KCSEEFTNKLRVSHA; CSEEFTNKLRVSHAD; SEEFTNKLRVSHADL; EEFTNKLRVSHADLG; EFTNKLRVSHADLGK; FTNKLRVSHADLGKQ; TNKLRVSHADLGKQG; NKLRVSHADLGKQGV; KLRVSHADLGKQGVN; LRVSHADLGKQGVND; RVSHADLGKQGVNDD; VSHADLGKQGVNDDD; SHADLGKQGVNDDDA; HADLGKQGVNDDDAK; ADLGKQGVNDDDAKK; DLGKQGVNDDDAKKA; LGKQGVNDDDAKKAI; GKQGVNDDDAKKAIL; KQGVNDDDAKKAILK; QGVNDDDAKKAILKT; GVNDDDAKKAILKTN; VNDDDAKKAILKTNA; NDDDAKKAILKTNAD; DDDAKKAILKTNADK; DDAKKAILKTNADKT; DAKKAILKTNADKTK; AKKAILKTNADKTKG; KKAILKTNADKTKGA; KAILKTNADKTKGAE; AILKTNADKTKGAEE; ILKTNADKTKGAEEL; LKTNADKTKGAEELG; KTNADKTKGAEELGK; TNADKTKGAEELGKL; NADKTKGAEELGKLF; ADKTKGAEELGKLFK; DKTKGAEELGKLFKS; KTKGAEELGKLFKSV; TKGAEELGKLFKSVE; KGAEELGKLFKSVEG; GAEELGKLFKSVEGL; AEELGKLFKSVEGLV; EELGKLFKSVEGLVK; ELGKLFKSVEGLVKA; LGKLFKSVEGLVKAA; GKLFKSVEGLVKAAQ; KLFKSVEGLVKAAQE; LFKSVEGLVKAAQEA; FKSVEGLVKAAQEAL; KSVEGLVKAAQEALT; SVEGLVKAAQEALTN; VEGLVKAAQEALTNS; EGLVKAAQEALTNSV; GLVKAAQEALTNSVK; LVKAAQEALTNSVKE; VKAAQEALTNSVKEL; KAAQEALTNSVKELT; AAQEALTNSVKELTS; AQEALTNSVKELTSP; QEALTNSVKELTSPV; EALTNSVKELTSPVV; ALTNSVKELTSPVVA; LTNSVKELTSPVVAE; TNSVKELTSPVVAES; NSVKELTSPVVAESP; SVKELTSPVVAESPK; VKELTSPVVAESPKK; KELTSPVVAESPKKP 16 mers: MKKNTLSAILMTLFLF; KKNTLSAILMTLFLFI; KNTLSAILMTLFLFIS; NTLSAILMTLFLFISC; TLSAILMTLFLFISCN; LSAILMTLFLFISCNN; SAILMTLFLFISCNNS; AILMTLFLFISCNNSG; ILMTLFLFISCNNSGK; LMTLFLFISCNNSGKG; MTLFLFISCNNSGKGG; TLFLFISCNNSGKGGD; LFLFISCNNSGKGGDS; FLFISCNNSGKGGDSA; LFISCNNSGKGGDSAS; FISCNNSGKGGDSAST; ISCNNSGKGGDSASTN; SCNNSGKGGDSASTNP; CNNSGKGGDSASTNPA; NNSGKGGDSASTNPAD; NSGKGGDSASTNPADE; SGKGGDSASTNPADES; GKGGDSASTNPADESA; KGGDSASTNPADESAK; GGDSASTNPADESAKG; GDSASTNPADESAKGP; DSASTNPADESAKGPN; SASTNPADESAKGPNL; ASTNPADESAKGPNLT; STNPADESAKGPNLTE; TNPADESAKGPNLTEI; NPADESAKGPNLTEIS; PADESAKGPNLTEISK; ADESAKGPNLTEISKK; DESAKGPNLTEISKKI; ESAKGPNLTEISKKIT; SAKGPNLTEISKKITD; AKGPNLTEISKKITDS; KGPNLTEISKKITDSN; GPNLTEISKKITDSNA; PNLTEISKKITDSNAF; NLTEISKKITDSNAFV; LTEISKKITDSNAFVL; TEISKKITDSNAFVLA; EISKKITDSNAFVLAV; ISKKITDSNAFVLAVK; SKKITDSNAFVLAVKE; KKITDSNAFVLAVKEV; KITDSNAFVLAVKEVE; ITDSNAFVLAVKEVET; TDSNAFVLAVKEVETL; DSNAFVLAVKEVETLV; SNAFVLAVKEVETLVS; NAFVLAVKEVETLVSS; AFVLAVKEVETLVSSI; FVLAVKEVETLVSSID; VLAVKEVETLVSSIDE; LAVKEVETLVSSIDEL; AVKEVETLVSSIDELA; VKEVETLVSSIDELAN; KEVETLVSSIDELANK; EVETLVSSIDELANKA; VETLVSSIDELANKAI; ETLVSSIDELANKAIG; TLVSSIDELANKAIGK; LVSSIDELANKAIGKK; VSSIDELANKAIGKKI; SSIDELANKAIGKKIQ; SIDELANKAIGKKIQQ; IDELANKAIGKKIQQN; DELANKAIGKKIQQNG; ELANKAIGKKIQQNGL; LANKAIGKKIQQNGLG; ANKAIGKKIQQNGLGA; NKAIGKKIQQNGLGAE; KAIGKKIQQNGLGAEA; AIGKKIQQNGLGAEAN; IGKKIQQNGLGAEANR; GKKIQQNGLGAEANRN; KKIQQNGLGAEANRNE; KIQQNGLGAEANRNES; IQQNGLGAEANRNESL; QQNGLGAEANRNESLL; QNGLGAEANRNESLLA; NGLGAEANRNESLLAG; GLGAEANRNESLLAGV; LGAEANRNESLLAGVH; GAEANRNESLLAGVHE; AEANRNESLLAGVHEI; EANRNESLLAGVHEIS; ANRNESLLAGVHEIST; NRNESLLAGVHEISTL; RNESLLAGVHEISTLI; NESLLAGVHEISTLIT; ESLLAGVHEISTLITE; SLLAGVHEISTLITEK; LLAGVHEISTLITEKL; LAGVHEISTLITEKLS; AGVHEISTLITEKLSK; GVHEISTLITEKLSKL; VHEISTLITEKLSKLK; HEISTLITEKLSKLKN; EISTLITEKLSKLKNS; ISTLITEKLSKLKNSG; STLITEKLSKLKNSGE; TLITEKLSKLKNSGEL; LITEKLSKLKNSGELK; ITEKLSKLKNSGELKA; TEKLSKLKNSGELKAK; EKLSKLKNSGELKAKI; KLSKLKNSGELKAKIE; LSKLKNSGELKAKIED; SKLKNSGELKAKIEDA; KLKNSGELKAKIEDAK; LKNSGELKAKIEDAKK; KNSGELKAKIEDAKKC; NSGELKAKIEDAKKCS; SGELKAKIEDAKKCSE; GELKAKIEDAKKCSEE; ELKAKIEDAKKCSEEF; LKAKIEDAKKCSEEFT; KAKIEDAKKCSEEFTN; AKIEDAKKCSEEFTNK; KIEDAKKCSEEFTNKL; IEDAKKCSEEFTNKLR; EDAKKCSEEFTNKLRV; DAKKCSEEFTNKLRVS; AKKCSEEFTNKLRVSH; KKCSEEFTNKLRVSHA; KCSEEFTNKLRVSHAD; CSEEFTNKLRVSHADL; SEEFTNKLRVSHADLG; EEFTNKLRVSHADLGK; EFTNKLRVSHADLGKQ; FTNKLRVSHADLGKQG; TNKLRVSHADLGKQGV; NKLRVSHADLGKQGVN; KLRVSHADLGKQGVND; LRVSHADLGKQGVNDD; RVSHADLGKQGVNDDD; VSHADLGKQGVNDDDA; SHADLGKQGVNDDDAK; HADLGKQGVNDDDAKK; ADLGKQGVNDDDAKKA; DLGKQGVNDDDAKKAI; LGKQGVNDDDAKKAIL; GKQGVNDDDAKKAILK; KQGVNDDDAKKAILKT; QGVNDDDAKKAILKTN; GVNDDDAKKAILKTNA; VNDDDAKKAILKTNAD; NDDDAKKAILKTNADK; DDDAKKAILKTNADKT; DDAKKAILKTNADKTK; DAKKAILKTNADKTKG; AKKAILKTNADKTKGA; KKAILKTNADKTKGAE; KAILKTNADKTKGAEE; AILKTNADKTKGAEEL; ILKTNADKTKGAEELG; LKTNADKTKGAEELGK; KTNADKTKGAEELGKL; TNADKTKGAEELGKLF; NADKTKGAEELGKLFK; ADKTKGAEELGKLFKS; DKTKGAEELGKLFKSV; KTKGAEELGKLFKSVE; TKGAEELGKLFKSVEG; KGAEELGKLFKSVEGL; GAEELGKLFKSVEGLV; AEELGKLFKSVEGLVK; EELGKLFKSVEGLVKA; ELGKLFKSVEGLVKAA; LGKLFKSVEGLVKAAQ; GKLFKSVEGLVKAAQE; KLFKSVEGLVKAAQEA; LFKSVEGLVKAAQEAL; FKSVEGLVKAAQEALT; KSVEGLVKAAQEALTN; SVEGLVKAAQEALTNS; VEGLVKAAQEALTNSV; EGLVKAAQEALTNSVK; GLVKAAQEALTNSVKE; LVKAAQEALTNSVKEL; VKAAQEALTNSVKELT; KAAQEALTNSVKELTS; AAQEALTNSVKELTSP; AQEALTNSVKELTSPV; QEALTNSVKELTSPVV; EALTNSVKELTSPVVA; ALTNSVKELTSPVVAE; LTNSVKELTSPVVAES; TNSVKELTSPVVAESP; NSVKELTSPVVAESPK; SVKELTSPVVAESPKK; VKELTSPVVAESPKKP SEQ ID NOS: 49527-51126

Preferred Borrelia burgdorferi fragments of Osp A capable of interacting with one or more MHC molecules are listed in Table V.

TABLE V Prediction of Borrelia burgdorferi OspA protein specific MHC class1, 8-, 9-, 10-, 11-mer peptide binders for 42 MHC class 1 alleles (see FIG. 11) using the www.cbs.dtu.dk/services/NetMHC/ database. The MHC class 1 molecules for which no binders were found are not listed. CAA44492.1|Outer surface HLA- protein A [Borrelia burgdorferi] A0101 Seq9 HLA- YLLGIGLIL A0201 FTLEGTLAA KTSTLTISV FTKEDTITV ALIACKQNV LLGIGLILA SLEATVDKL ILKSGEITV KVTEGTVVL STLDEKNSV TLVSKKVTL GIGLILALI YLLGIGLILA TLDEKNSVSV ALDDSDTTQA LLGIGLILAL NILKSGEITV TLAADGKTTL VLKDFTLEGT YSLEATVDKL YLLGIGLILAL LVFTKEDTITV LLGIGLILALI ILALIACKQNV STLDEKNSVSV ALDDSDTTQAT VLKDFTLEGTL SLEATVDKLEL ILKSGEITVAL ALIACKQNVST TTLKVTEGTVV LAADGKTTLKV LIACKQNVSTL HLA- VVLSKNILK A0301 KTKNLVFTK LVSKKVTLK LILALIACK LTISVNSQK KAVEITTLK AADGKTTLK ISVNSQKTK RANGTRLEY SQTKFEIFK KSDGSGKAK TQATKKTGK MTELVSKEK TLVSKKVTLK TLTISVNSQK TVVLSKNILK GLILALIACK TLKELKNALK LSQTKFEIFK LAADGKTTLK VTEGTVVLSK KLELKGTSDK TTQATKKTGK GMTELVSKEK KYSLEATVDK KQNVSTLDEK TIADDLSQTK TISVNSQKTK KEDAKTLVSK GSGKAKEVLK KTIVRANGTR GTLEGEKTDK GKAVEITTLK GTRLEYTDIK VSKKVTLKDK IKSDGSGKAK TLAADGKTTLK STLTISVNSQK KTLVSKKVTLK KVTEGTVVLSK TTLKELKNALK LTISVNSQKTK GTVVLSKNILK FTKEDTITVQK IVRANGTRLEY TLKDKSSTEEK LVSKKVTLKDK KFNEKGETSEK LTIADDLSQTK SQKTKNLVFTK KSSTEEKFNEK ATKKTGKWDSK HLA- VVLSKNILK A1101 KTKNLVFTK SQTKFEIFK LTISVNSQK ATVDKLELK LILALIACK STEEKFNEK KAVEITTLK LVSKKVTLK MTELVSKEK AADGKTTLK SAGTNLEGK YSLEATVDK GSGTLEGEK TQATKKTGK RANGTRLEY IADDLSQTK ISVNSQKTK KSDGSGKAK GGMTELVSK TEGTVVLSK EITTLKELK TIVRANGTR TVVLSKNILK TTQATKKTGK TIADDLSQTK VTEGTVVLSK LSQTKFEIFK SSTEEKFNEK GLILALIACK KQNVSTLDEK TLTISVNSQK TLVSKKVTLK TISVNSQKTK LAADGKTTLK GMTELVSKEK TLKELKNALK KTIVRANGTR GSGKAKEVLK GTLEGEKTDK VSKKVTLKDK GTRLEYTDIK KLELKGTSDK DSAGTNLEGK STLTISVNSQK TTLKELKNALK KVTEGTVVLSK KTLVSKKVTLK GTVVLSKNILK LTIADDLSQTK TLAADGKTTLK AVEITTLKELK LTISVNSQKTK SQKTKNLVFTK KSSTEEKFNEK ATKKTGKWDSK TLKDKSSTEEK FTKEDTITVQK TLEGTLAADGK LVSKKVTLKDK MTELVSKEKDK DLSQTKFEIFK YTDIKSDGSGK LVSKEKDKDGK KFNEKGETSEK IGLILALIACK HLA- KYLLGIGLI A2402 KWDSKTSTL KYDSAGTNL KYLLGIGLIL KWDSKTSTLTI KYSLEATVDKL HLA- IVRANGTRLEY A2902 TIADDLSQTKF HLA- LTISVNSQK A6801 ETSEKTIVR MTELVSKEK EITTLKELK TIVRANGTR KAVEITTLK DAKTLVSKK KTKNLVFTK STEEKFNEK ATVDKLELK LVSKKVTLK SQTKFEIFK YSLEATVDK EGTLAADGK ISVNSQKTK LILALIACK DIKSDGSGK VVLSKNILK EDAKTLVSK DSDTTQATK SAGTNLEGK TVVLSKNILK TLTISVNSQK EATVDKLELK TIADDLSQTK DSAGTNLEGK TTQATKKTGK LAADGKTTLK KTIVRANGTR TISVNSQKTK TLVSKKVTLK SSTEEKFNEK TLKELKNALK LSQTKFEIFK VTEGTVVLSK EDAKTLVSKK DSDTTQATKK GLILALIACK HLA- IVRANGTRL B0702 KVTEGTVVL LAADGKTTL LPGGMTELV TVVLSKNIL KAVEITTLKEL HLA- TLKELKNAL B0801 ILKSGEITVAL YLLGIGLILAL TLKVTEGTVVL HLA- SQKTKNLVF B1501 RANGTRLEY YLLGIGLIL KVTEGTVVL TLKELKNAL KAKEVLKDF IVRANGTRL LGIGLILAL TLAADGKTTL IVRANGTRLEY YLLGIGLILAL VQKYDSAGTNL ILKSGEITVAL VSKEKDKDGKY VLKDFTLEGTL TLKVTEGTVVL VNSQKTKNLVF HLA- KKYLLGIGL B2705 VRANGTRLEY GKWDSKTSTL KKYLLGIGLIL HLA- LAADGKTTL B3501 RANGTRLEY FTLEGTLAA TVVLSKNIL VALDDSDTT YLLGIGLIL LPGGMTELV IADDLSQTKF LPGGMTELVS LKVTEGTVVL YSLEATVDKL YLLGIGLILAL NSVSVDLPGGM IVRANGTRLEY TIADDLSQTKF KAVEITTLKEL HLA- KEVLKDFTL B4403 GEITVALDD KEKDKDGKY KEDAKTLVS GEITVALDDS KEDTITVQKY GEITVALDDSD KEVLKDFTLEG HLA- LPGGMTELV B5101 HLA- TTQATKKTGKW B5701 SEQ ID NOS: 51127-51380

Preferred Borrelia garinii fragments of FlaB capable of interacting with one or more MHC molecules are listed in Table X.

TABLE X Prediction of Borrelia garinii FlaB protein specific MHC class 2, 15-mer peptide binders for 14 MHC class 2 alleles (see FIG. 11) using the www.cbs.dtu.dk/ services/NetMHCII/ database. The MHC class 2 molecules for which no binders were found are not listed. BAD18055.1 HLA-A0101 NQDEAIAVNIY FlaB protein ELAVQSGNGTY [Borrelia garinii] HLA-A0201 SQASWTLRV Seq15 QLTDEINRI AQAAQTAPV AIAVNIYAA SLAKIENAI AVNIYAANV AQYNQMHML TTVDANTSL SQGGVNSPV QTAPVQEGV NIYAANVANL NLNEVEKVLV VLVRMKELAV QLTDEINRIA NLFSGEGAQA IAVNIYAANV SLSGSQASWTL MLSNKSASQNV AIAVNIYAANV SQASWTLRVHV GMQPAKINTPA KVLVRMKELAV SLAKIENAIRM NLFSGEGAQAA HLA-A0301 NQMHMLSNK GSQASWTLR TVDANTSLAK YNQMHMLSNK LSGSQASWTLR TTVDANTSLAK LSNKSASQNVR HLA-A1101 NQMHMLSNK GSQASWTLR AVQSGNGTY TVDANTSLAK YNQMHMLSNK EVEKVLVRMK TTVDANTSLAK TTEGNLNEVEK TAEELGMQPAK TSLAKIENAIR QYNQMHMLSNK LSGSQASWTLR LSNKSASQNVR HLA-A2402 IYAANVANL YAANVANLF IYAANVANLF TYSDADRGSI IYAANVANLFS HLA-A2902 AVQSGNGTY YAANVANLF ELAVQSGNGTY EINRIADQAQY HLA-A6801 LAKIENAIR EGNLNEVEK YAANVANLF NGTYSDADR GSQASWTLR NQMHMLSNK TSKAINFIQ NKSASQNVR EVEKVLVRMK SLAKIENAIR TVDANTSLAK NTSKAINFIQ SGSQASWTLR TTVDANTSLA TTVDANTSLAK TTEGNLNEVEK EIEQLTDEINR LSNKSASQNVR TSLAKIENAIR EINRIADQAQY NLNEVEKVLVR LSGSQASWTLR TAEELGMQPAK QYNQMHMLSNK NIYAANVANLF QTAPVQEGVQQ HLA-B0702 SPVNVTTTV QPAKINTPA QPAPATAPS LVRMKELAV TPASLSGSQ APSQGGVNS APATAPSQG APVQEGVQQ TPASLSGSQA SPVNVTTTVD APSQGGVNSP QPAKINTPAS APSQGGVNSPV QPAKINTPASL APATAPSQGGV SPVNVTTTVDA TPASLSGSQAS HLA-B0801 KVLVRMKEL VEKVLVRMKEL HLA-B1501 YAANVANLF AVQSGNGTY AQAAQTAPV AQYNQMHML SQGGVNSPV SLSGSQASW SQASWTLRV IQIEIEQLT LAVQSGNGTY SQASWTLRVH SQNVRTAEEL VQQEGAQQPA INRIADQAQY AQAAQTAPVQ MQPAKINTPA ELAVQSGNGTY NIYAANVANLF NQDEAIAVNIY SLSGSQASWTL HLA-B2705 NRIADQAQY HLA-B3501 YAANVANLF QPAPATAPS SPVNVTTTV DEAIAVNIY TTVDANTSL LAVQSGNGT QPAKINTPA AVQSGNGTY QASWTLRVH IAVNIYAAN LAVQSGNGTY IADQAQYNQM QPAKINTPAS LAKIENAIRM QPAPATAPSQ YAANVANLFS TAEELGMQPA EAIAVNIYAA QAQYNQMHML TPASLSGSQA SPVNVTTTVD TPASLSGSQAS ELAVQSGNGTY NQDEAIAVNIY QPAKINTPASL IAVNIYAANVA NIYAANVANLF SPVNVTTTVDA EINRIADQAQY IADQAQYNQMH APSQGGVNSPV LAVQSGNGTYS HLA-B4403 EELGMQPAKI NEVEKVLVRM DEINRIADQA DEINRIADQAQ HLA-B5101 SPVNVTTTV APATAPSQGGV APSQGGVNSPV HLA-B5701 ASLSGSQASW SEQ ID NOS: 51381-51540

Preferred Mycobacterium tuberculosis fragments of CFP10 protein (Rv3874) capable of interacting with one or more class 1 and/or one or more class 2 MHC molecules are listed in Table Y.

TABLE Y Prediction of MHC class 1 and 2 Mycobacterium tuberculosis CFP10 peptide binders. Prediction of 8-, 9-, 10-, 11-, 13-, 14-, 15-, 16-mer peptides were using the program displayed in FIG. 2 8 mers: MAEMKTDA; AEMKTDAA; EMKTDAAT; MKTDAATL; KTDAATLA; TDAATLAQ; DAATLAQE; AATLAQEA; ATLAQEAG; TLAQEAGN; LAQEAGNF; AQEAGNFE; QEAGNFER; EAGNFERI; AGNFERIS; GNFERISG; NFERISGD; FERISGDL; ERISGDLK; RISGDLKT; ISGDLKTQ; SGDLKTQI; GDLKTQID; DLKTQIDQ; LKTQIDQV; KTQIDQVE; TQIDQVES; QIDQVEST; IDQVESTA; DQVESTAG; QVESTAGS; VESTAGSL; ESTAGSLQ; STAGSLQG; TAGSLQGQ; AGSLQGQW; GSLQGQWR; SLQGQWRG; LQGQWRGA; QGQWRGAA; GQWRGAAG; QWRGAAGT; WRGAAGTA; RGAAGTAA; GAAGTAAQ; AAGTAAQA; AGTAAQAA; GTAAQAAV; TAAQAAVV; AAQAAVVR; AQAAVVRF; QAAVVRFQ; AAVVRFQE; AVVRFQEA; VVRFQEAA; VRFQEAAN; RFQEAANK; FQEAANKQ; QEAANKQK; EAANKQKQ; AANKQKQE; ANKQKQEL; NKQKQELD; KQKQELDE; QKQELDEI; KQELDEIS; QELDEIST; ELDEISTN; LDEISTNI; DEISTNIR; EISTNIRQ; ISTNIRQA; STNIRQAG; TNIRQAGV; NIRQAGVQ; IRQAGVQY; RQAGVQYS; QAGVQYSR; AGVQYSRA; GVQYSRAD; VQYSRADE; QYSRADEE; YSRADEEQ; SRADEEQQ; RADEEQQQ; ADEEQQQA; DEEQQQAL; EEQQQALS; EQQQALSS; QQQALSSQ; QQALSSQM; QALSSQMG; ALSSQMGF 9 mers: MAEMKTDAA; AEMKTDAAT; EMKTDAATL; MKTDAATLA; KTDAATLAQ; TDAATLAQE; DAATLAQEA; AATLAQEAG; ATLAQEAGN; TLAQEAGNF; LAQEAGNFE; AQEAGNFER; QEAGNFERI; EAGNFERIS; AGNFERISG; GNFERISGD; NFERISGDL; FERISGDLK; ERISGDLKT; RISGDLKTQ; ISGDLKTQI; SGDLKTQID; GDLKTQIDQ; DLKTQIDQV; LKTQIDQVE; KTQIDQVES; TQIDQVEST; QIDQVESTA; IDQVESTAG; DQVESTAGS; QVESTAGSL; VESTAGSLQ; ESTAGSLQG; STAGSLQGQ; TAGSLQGQW; AGSLQGQWR; GSLQGQWRG; SLQGQWRGA; LQGQWRGAA; QGQWRGAAG; GQWRGAAGT; QWRGAAGTA; WRGAAGTAA; RGAAGTAAQ; GAAGTAAQA; AAGTAAQAA; AGTAAQAAV; GTAAQAAVV; TAAQAAVVR; AAQAAVVRF; AQAAVVRFQ; QAAVVRFQE; AAVVRFQEA; AVVRFQEAA; VVRFQEAAN; VRFQEAANK; RFQEAANKQ; FQEAANKQK; QEAANKQKQ; EAANKQKQE; AANKQKQEL; ANKQKQELD; NKQKQELDE; KQKQELDEI; QKQELDEIS; KQELDEIST; QELDEISTN; ELDEISTNI; LDEISTNIR; DEISTNIRQ; EISTNIRQA; ISTNIRQAG; STNIRQAGV; TNIRQAGVQ; NIRQAGVQY; IRQAGVQYS; RQAGVQYSR; QAGVQYSRA; AGVQYSRAD; GVQYSRADE; VQYSRADEE; QYSRADEEQ; YSRADEEQQ; SRADEEQQQ; RADEEQQQA; ADEEQQQAL; DEEQQQALS; EEQQQALSS; EQQQALSSQ; QQQALSSQM; QQALSSQMG; QALSSQMGF; 10 mers: MAEMKTDAAT; AEMKTDAATL; EMKTDAATLA; MKTDAATLAQ; KTDAATLAQE; TDAATLAQEA; DAATLAQEAG; AATLAQEAGN; ATLAQEAGNF; TLAQEAGNFE; LAQEAGNFER; AQEAGNFERI; QEAGNFERIS; EAGNFERISG; AGNFERISGD; GNFERISGDL; NFERISGDLK; FERISGDLKT; ERISGDLKTQ; RISGDLKTQI; ISGDLKTQID; SGDLKTQIDQ; GDLKTQIDQV; DLKTQIDQVE; LKTQIDQVES; KTQIDQVEST; TQIDQVESTA; QIDQVESTAG; IDQVESTAGS; DQVESTAGSL; QVESTAGSLQ; VESTAGSLQG; ESTAGSLQGQ; STAGSLQGQW; TAGSLQGQWR; AGSLQGQWRG; GSLQGQWRGA; SLQGQWRGAA; LQGQWRGAAG; QGQWRGAAGT; GQWRGAAGTA; QWRGAAGTAA; WRGAAGTAAQ; RGAAGTAAQA; GAAGTAAQAA; AAGTAAQAAV; AGTAAQAAVV; GTAAQAAVVR; TAAQAAVVRF; AAQAAVVRFQ; AQAAVVRFQE; QAAVVRFQEA; AAVVRFQEAA; AVVRFQEAAN; VVRFQEAANK; VRFQEAANKQ; RFQEAANKQK; FQEAANKQKQ; QEAANKQKQE; EAANKQKQEL; AANKQKQELD; ANKQKQELDE; NKQKQELDEI; KQKQELDEIS; QKQELDEIST; KQELDEISTN; QELDEISTNI; ELDEISTNIR; LDEISTNIRQ; DEISTNIRQA; EISTNIRQAG; ISTNIRQAGV; STNIRQAGVQ; TNIRQAGVQY; NIRQAGVQYS; IRQAGVQYSR; RQAGVQYSRA; QAGVQYSRAD; AGVQYSRADE; GVQYSRADEE; VQYSRADEEQ; QYSRADEEQQ; YSRADEEQQQ; SRADEEQQQA; RADEEQQQAL; ADEEQQQALS; DEEQQQALSS; EEQQQALSSQ; EQQQALSSQM; QQQALSSQMG; QQALSSQMGF; 11 mers: MAEMKTDAATL; AEMKTDAATLA; EMKTDAATLAQ; MKTDAATLAQE; KTDAATLAQEA; TDAATLAQEAG; DAATLAQEAGN; AATLAQEAGNF; ATLAQEAGNFE; TLAQEAGNFER; LAQEAGNFERI; AQEAGNFERIS; QEAGNFERISG; EAGNFERISGD; AGNFERISGDL; GNFERISGDLK; NFERISGDLKT; FERISGDLKTQ; ERISGDLKTQI; RISGDLKTQID; ISGDLKTQIDQ; SGDLKTQIDQV; GDLKTQIDQVE; DLKTQIDQVES; LKTQIDQVEST; KTQIDQVESTA; TQIDQVESTAG; QIDQVESTAGS; IDQVESTAGSL; DQVESTAGSLQ; QVESTAGSLQG; VESTAGSLQGQ; ESTAGSLQGQW; STAGSLQGQWR; TAGSLQGQWRG; AGSLQGQWRGA; GSLQGQWRGAA; SLQGQWRGAAG; LQGQWRGAAGT; QGQWRGAAGTA; GQWRGAAGTAA; QWRGAAGTAAQ; WRGAAGTAAQA; RGAAGTAAQAA; GAAGTAAQAAV; AAGTAAQAAVV; AGTAAQAAVVR; GTAAQAAVVRF; TAAQAAVVRFQ; AAQAAVVRFQE; AQAAVVRFQEA; QAAVVRFQEAA; AAVVRFQEAAN; AVVRFQEAANK; VVRFQEAANKQ; VRFQEAANKQK; RFQEAANKQKQ; FQEAANKQKQE; QEAANKQKQEL; EAANKQKQELD; AANKQKQELDE; ANKQKQELDEI; NKQKQELDEIS; KQKQELDEIST; QKQELDEISTN; KQELDEISTNI; QELDEISTNIR; ELDEISTNIRQ; LDEISTNIRQA; DEISTNIRQAG; EISTNIRQAGV; ISTNIRQAGVQ; STNIRQAGVQY; TNIRQAGVQYS; NIRQAGVQYSR; IRQAGVQYSRA; RQAGVQYSRAD; QAGVQYSRADE; AGVQYSRADEE; GVQYSRADEEQ; VQYSRADEEQQ; QYSRADEEQQQ; YSRADEEQQQA; SRADEEQQQAL; RADEEQQQALS; ADEEQQQALSS; DEEQQQALSSQ; EEQQQALSSQM; EQQQALSSQMG; QQQALSSQMGF 13 mers: MAEMKTDAATLAQ; AEMKTDAATLAQE; EMKTDAATLAQEA; MKTDAATLAQEAG; KTDAATLAQEAGN; TDAATLAQEAGNF; DAATLAQEAGNFE; AATLAQEAGNFER; ATLAQEAGNFERI; TLAQEAGNFERIS; LAQEAGNFERISG; AQEAGNFERISGD; QEAGNFERISGDL; EAGNFERISGDLK; AGNFERISGDLKT; GNFERISGDLKTQ; NFERISGDLKTQI; FERISGDLKTQID; ERISGDLKTQIDQ; RISGDLKTQIDQV; ISGDLKTQIDQVE; SGDLKTQIDQVES; GDLKTQIDQVEST; DLKTQIDQVESTA; LKTQIDQVESTAG; KTQIDQVESTAGS; TQIDQVESTAGSL; QIDQVESTAGSLQ; IDQVESTAGSLQG; DQVESTAGSLQGQ; QVESTAGSLQGQW; VESTAGSLQGQWR; ESTAGSLQGQWRG; STAGSLQGQWRGA; TAGSLQGQWRGAA; AGSLQGQWRGAAG; GSLQGQWRGAAGT; SLQGQWRGAAGTA; LQGQWRGAAGTAA; QGQWRGAAGTAAQ; GQWRGAAGTAAQA; QWRGAAGTAAQAA; WRGAAGTAAQAAV; RGAAGTAAQAAVV; GAAGTAAQAAVVR; AAGTAAQAAVVRF; AGTAAQAAVVRFQ; GTAAQAAVVRFQE; TAAQAAVVRFQEA; AAQAAVVRFQEAA; AQAAVVRFQEAAN; QAAVVRFQEAANK; AAVVRFQEAANKQ; AVVRFQEAANKQK; VVRFQEAANKQKQ; VRFQEAANKQKQE; RFQEAANKQKQEL; FQEAANKQKQELD; QEAANKQKQELDE; EAANKQKQELDEI; AANKQKQELDEIS; ANKQKQELDEIST; NKQKQELDEISTN; KQKQELDEISTNI; QKQELDEISTNIR; KQELDEISTNIRQ; QELDEISTNIRQA; ELDEISTNIRQAG; LDEISTNIRQAGV; DEISTNIRQAGVQ; EISTNIRQAGVQY; ISTNIRQAGVQYS; STNIRQAGVQYSR; TNIRQAGVQYSRA; NIRQAGVQYSRAD; IRQAGVQYSRADE; RQAGVQYSRADEE; QAGVQYSRADEEQ; AGVQYSRADEEQQ; GVQYSRADEEQQQ; VQYSRADEEQQQA; QYSRADEEQQQAL; YSRADEEQQQALS; SRADEEQQQALSS; RADEEQQQALSSQ; ADEEQQQALSSQM; DEEQQQALSSQMG; EEQQQALSSQMGF; 14 mers: MAEMKTDAATLAQE; AEMKTDAATLAQEA; EMKTDAATLAQEAG; MKTDAATLAQEAGN; KTDAATLAQEAGNF; TDAATLAQEAGNFE; DAATLAQEAGNFER; AATLAQEAGNFERI; ATLAQEAGNFERIS; TLAQEAGNFERISG; LAQEAGNFERISGD; AQEAGNFERISGDL; QEAGNFERISGDLK; EAGNFERISGDLKT; AGNFERISGDLKTQ; GNFERISGDLKTQI; NFERISGDLKTQID; FERISGDLKTQIDQ; ERISGDLKTQIDQV; RISGDLKTQIDQVE; ISGDLKTQIDQVES; SGDLKTQIDQVEST; GDLKTQIDQVESTA; DLKTQIDQVESTAG; LKTQIDQVESTAGS; KTQIDQVESTAGSL; TQIDQVESTAGSLQ; QIDQVESTAGSLQG; IDQVESTAGSLQGQ; DQVESTAGSLQGQW; QVESTAGSLQGQWR; VESTAGSLQGQWRG; ESTAGSLQGQWRGA; STAGSLQGQWRGAA; TAGSLQGQWRGAAG; AGSLQGQWRGAAGT; GSLQGQWRGAAGTA; SLQGQWRGAAGTAA; LQGQWRGAAGTAAQ; QGQWRGAAGTAAQA; GQWRGAAGTAAQAA; QWRGAAGTAAQAAV; WRGAAGTAAQAAVV; RGAAGTAAQAAVVR; GAAGTAAQAAVVRF; AAGTAAQAAVVRFQ; AGTAAQAAVVRFQE; GTAAQAAVVRFQEA; TAAQAAVVRFQEAA; AAQAAVVRFQEAAN; AQAAVVRFQEAANK; QAAVVRFQEAANKQ; AAVVRFQEAANKQK; AVVRFQEAANKQKQ; VVRFQEAANKQKQE; VRFQEAANKQKQEL; RFQEAANKQKQELD; FQEAANKQKQELDE; QEAANKQKQELDEI; EAANKQKQELDEIS; AANKQKQELDEIST; ANKQKQELDEISTN; NKQKQELDEISTNI; KQKQELDEISTNIR; QKQELDEISTNIRQ; KQELDEISTNIRQA; QELDEISTNIRQAG; ELDEISTNIRQAGV; LDEISTNIRQAGVQ; DEISTNIRQAGVQY; EISTNIRQAGVQYS; ISTNIRQAGVQYSR; STNIRQAGVQYSRA; TNIRQAGVQYSRAD; NIRQAGVQYSRADE; IRQAGVQYSRADEE; RQAGVQYSRADEEQ; QAGVQYSRADEEQQ; AGVQYSRADEEQQQ; GVQYSRADEEQQQA; VQYSRADEEQQQAL; QYSRADEEQQQALS; YSRADEEQQQALSS; SRADEEQQQALSSQ; RADEEQQQALSSQM; ADEEQQQALSSQMG; DEEQQQALSSQMGF 15 mers: MAEMKTDAATLAQEA; AEMKTDAATLAQEAG; EMKTDAATLAQEAGN; MKTDAATLAQEAGNF; KTDAATLAQEAGNFE; TDAATLAQEAGNFER; DAATLAQEAGNFERI; AATLAQEAGNFERIS; ATLAQEAGNFERISG; TLAQEAGNFERISGD; LAQEAGNFERISGDL; AQEAGNFERISGDLK; QEAGNFERISGDLKT; EAGNFERISGDLKTQ; AGNFERISGDLKTQI; GNFERISGDLKTQID; NFERISGDLKTQIDQ; FERISGDLKTQIDQV; ERISGDLKTQIDQVE; RISGDLKTQIDQVES; ISGDLKTQIDQVEST; SGDLKTQIDQVESTA; GDLKTQIDQVESTAG; DLKTQIDQVESTAGS; LKTQIDQVESTAGSL; KTQIDQVESTAGSLQ; TQIDQVESTAGSLQG; QIDQVESTAGSLQGQ; IDQVESTAGSLQGQW; DQVESTAGSLQGQWR; QVESTAGSLQGQWRG; VESTAGSLQGQWRGA; ESTAGSLQGQWRGAA; STAGSLQGQWRGAAG; TAGSLQGQWRGAAGT; AGSLQGQWRGAAGTA; GSLQGQWRGAAGTAA; SLQGQWRGAAGTAAQ; LQGQWRGAAGTAAQA; QGQWRGAAGTAAQAA; GQWRGAAGTAAQAAV; QWRGAAGTAAQAAVV; WRGAAGTAAQAAVVR; RGAAGTAAQAAVVRF; GAAGTAAQAAVVRFQ; AAGTAAQAAVVRFQE; AGTAAQAAVVRFQEA; GTAAQAAVVRFQEAA; TAAQAAVVRFQEAAN; AAQAAVVRFQEAANK; AQAAVVRFQEAANKQ; QAAVVRFQEAANKQK; AAVVRFQEAANKQKQ; AVVRFQEAANKQKQE; VVRFQEAANKQKQEL; VRFQEAANKQKQELD; RFQEAANKQKQELDE; FQEAANKQKQELDEI; QEAANKQKQELDEIS; EAANKQKQELDEIST; AANKQKQELDEISTN; ANKQKQELDEISTNI; NKQKQELDEISTNIR; KQKQELDEISTNIRQ; QKQELDEISTNIRQA; KQELDEISTNIRQAG; QELDEISTNIRQAGV; ELDEISTNIRQAGVQ; LDEISTNIRQAGVQY; DEISTNIRQAGVQYS; EISTNIRQAGVQYSR; ISTNIRQAGVQYSRA; STNIRQAGVQYSRAD; TNIRQAGVQYSRADE; NIRQAGVQYSRADEE; IRQAGVQYSRADEEQ; RQAGVQYSRADEEQQ; QAGVQYSRADEEQQQ; AGVQYSRADEEQQQA; GVQYSRADEEQQQAL; VQYSRADEEQQQALS; QYSRADEEQQQALSS; YSRADEEQQQALSSQ; SRADEEQQQALSSQM; RADEEQQQALSSQMG; ADEEQQQALSSQMGF 16 mers: MAEMKTDAATLAQEAG; AEMKTDAATLAQEAGN; EMKTDAATLAQEAGNF; MKTDAATLAQEAGNFE; KTDAATLAQEAGNFER; TDAATLAQEAGNFERI; DAATLAQEAGNFERIS; AATLAQEAGNFERISG; ATLAQEAGNFERISGD; TLAQEAGNFERISGDL; LAQEAGNFERISGDLK; AQEAGNFERISGDLKT; QEAGNFERISGDLKTQ; EAGNFERISGDLKTQI; AGNFERISGDLKTQID; GNFERISGDLKTQIDQ; NFERISGDLKTQIDQV; FERISGDLKTQIDQVE; ERISGDLKTQIDQVES; RISGDLKTQIDQVEST; ISGDLKTQIDQVESTA; SGDLKTQIDQVESTAG; GDLKTQIDQVESTAGS; DLKTQIDQVESTAGSL; LKTQIDQVESTAGSLQ; KTQIDQVESTAGSLQG; TQIDQVESTAGSLQGQ; QIDQVESTAGSLQGQW; IDQVESTAGSLQGQWR; DQVESTAGSLQGQWRG; QVESTAGSLQGQWRGA; VESTAGSLQGQWRGAA; ESTAGSLQGQWRGAAG; STAGSLQGQWRGAAGT; TAGSLQGQWRGAAGTA; AGSLQGQWRGAAGTAA; GSLQGQWRGAAGTAAQ; SLQGQWRGAAGTAAQA; LQGQWRGAAGTAAQAA; QGQWRGAAGTAAQAAV; GQWRGAAGTAAQAAVV; QWRGAAGTAAQAAVVR; WRGAAGTAAQAAVVRF; RGAAGTAAQAAVVRFQ; GAAGTAAQAAVVRFQE; AAGTAAQAAVVRFQEA; AGTAAQAAVVRFQEAA; GTAAQAAVVRFQEAAN; TAAQAAVVRFQEAANK; AAQAAVVRFQEAANKQ; AQAAVVRFQEAANKQK; QAAVVRFQEAANKQKQ; AAVVRFQEAANKQKQE; AVVRFQEAANKQKQEL; VVRFQEAANKQKQELD; VRFQEAANKQKQELDE; RFQEAANKQKQELDEI; FQEAANKQKQELDEIS; QEAANKQKQELDEIST; EAANKQKQELDEISTN; AANKQKQELDEISTNI; ANKQKQELDEISTNIR; NKQKQELDEISTNIRQ; KQKQELDEISTNIRQA; QKQELDEISTNIRQAG; KQELDEISTNIRQAGV; QELDEISTNIRQAGVQ; ELDEISTNIRQAGVQY; LDEISTNIRQAGVQYS; DEISTNIRQAGVQYSR; EISTNIRQAGVQYSRA; ISTNIRQAGVQYSRAD; STNIRQAGVQYSRADE; TNIRQAGVQYSRADEE; NIRQAGVQYSRADEEQ; IRQAGVQYSRADEEQQ; RQAGVQYSRADEEQQQ; QAGVQYSRADEEQQQA; AGVQYSRADEEQQQAL; GVQYSRADEEQQQALS; VQYSRADEEQQQALSS; QYSRADEEQQQALSSQ; YSRADEEQQQALSSQM; SRADEEQQQALSSQMG; RADEEQQQALSSQMGF SEQ ID NOS: 51541-52252

INDEX TO SEQUENCE LIST SEQ ID NO Table C: Bcl-2 fragments (class I) 44893-45800 Table B: BclX(L) fragments (class I) 45801-46593 Table A: Cancer antigens 44889-44892 Table H: BK virus antigens 1-6 Table I: BK virus 8-11 mers class I   7-24956 Table J: BK virus 8-11 mers class I 52253-53779 Table K: BK virus 8-11 mers class I 53780-54917 Table L: BK virus 8-11 mers class I 54918-55453 Table M: BK virus 8-11 mers class I 55454-58054 Table N: BK virus 8-11 mers class I 58055-58311 Table E: Bcl-2 fragments (class II) 46594-47133 Table D: BclX(L) fragments (class II) 47134-47645 Table O: BK 13-16 mers class II 24957-44888 Table P: BK 13-16 mers class II 58312-59135 Table Q: BK 13-16 mers class II 59136-59917 Table R: BK 13-16 mers class II 59918-60257 Table S: BK 13-16 mers class II 60258-61275 Table T: BK 13-16 mers class II 61276-61367 Table F: Survivin fragments (class I) 47646-48180 Table G: Mcl-1 fragments (class II) 48181-49526 Table U: Borrelia OspC 8-11 mers and 13-16 mers 49527-51126 Table V: Borrelia OspA fragments 51127-51380 Table X: Borrelia FlaB fragments 51381-51540 Table Y: Mycobacterium tuberculosis CFP10 8-11 51541-52252 mers and 13-16 mers FIG. 7 61368-61663 FIG. 8 and 9 61664 FIG. 12 61665-61726 FIG. 15, 16 and 17 61727 FIG. 18 61728 FIG. 19 61729 FIG. 20 61730

EXAMPLES Example 1

This example describes how to make a MHC class I complex with a peptide in the peptide binding-groove using in vitro refolding. The MHC-complex in this example consisted of light chain β2m, the MHC class I Heavy Chain allele HLA-A*0201 (a truncated version in which the intracellular and transmembrane domains have been deleted) and the peptide QLFEELQEL. MHC I-complexes consists of 3 components; Light Chain (β2m), Heavy Chain and a peptide of typically 8-10 amino acids. In this example MHC-complexes was generated by in vitro refolding of heavy chain, β2m and peptide in a buffer containing reduced and oxidized glutathione. By incubation in this buffer a non-covalent complex between Heavy Chain, β2m and peptide was formed. Heavy chain and β2m was expressed as inclusion bodies in E. coli prior to in vitro refolding following standard procedures as described in Garboczi et al., (1996), Nature 384, 134-141. Following refolding the MHC complexes was biotinylated using BirA enzyme able to biotinylate a specific amino acid residue in a recognition sequence fused to the C-terminal of the Heavy Chain by genetic fusion. Monomer MHC complexes was then purified by size exclusion chromatography.

-   1. 200 ml of refolding buffer (100 mM Tris, 400 mM L-arginin-HCL, 2     mM NaEDTA, 0.5 mM oxidized Gluthathione, 5 mM reduced Glutathione,     pH 8.0) was supplied with protease inhibitors PMSF     (phenylmethylsulphonyl fluoride), Pepstatin A and Leupeptin (to a     final concentration of 1 mM, 1 mg/l and 1 mg/l, respectively).     -   The refolding buffer was placed at 10° C. on a stirrer. -   2. 12 mg of peptide QLFEELQEL was dissolved in DMSO or another     suitable solvent (300-500 μl), and added drop-wise to the refolding     buffer at vigorous stirring. -   3. 4.4 mg of human Light Chain β2m was added drop-wise to the     refolding buffer at vigorous stirring. -   4. 6.2 mg of Heavy Chain HLA-A*0201 (supplied with DTT to a     concentration of 0.1 mM) was added drop-wise to the refolding buffer     at vigorous stirring. -   5. The folding reaction was placed at 10° C. at slow stirring for     4-8 hours. -   6. After 4-8 hours, step 3 and 4 was repeated and the folding     reaction is placed at 10° C. at slow stirring O/N. -   7. Step 3 and 4 was repeated, and the folding reaction is placed at     10° C. at slow stirring for 6-8 hours.

Optionally, steps 5-7 may be done in less time, e.g. a total of 0.5-5 hours.

-   8. After 6-8 hours the folding reaction was filtrated through a 0.2     μm filter to remove aggregates. -   9. The folding reaction was concentrated O/N at 10° C. shaking     gently in a suitable concentrator with a 5000 mw cut-off filter. The     folding reaction was concentrated to approximately 5-10 ml.     (Optionally the filtrate can be stored at 4° C. and reused for     another folding with the same peptide and heavy chain.) -   10. The concentrated folding reaction was buffer-exchanged at least     8 times, into a MHC-buffer (20 mM Tris-HCl, 50 mM NaCl, pH 8.0) and     concentrated (at 10° C. in a suitable concentrator with a 5000 mw     cut-off filter) down to approximately 1 ml. -   11. The heavy chain part of the MHC-complex was biotinylated by     mixing the following components: approximately 1000 μl folded     MHC-complex, 100 μl each of Biomix-A, Biomix-B and d-Biotin (all 3     from Biotin Protein Ligase Kit from Avidity, 10 μl birA enzyme (3     mg/ml, from Biotin Protein Ligase Kit from Avidity, 0.5 μl Pepstatin     A (2 mg/ml) and 0.5 μl Leupeptin (2 mg/ml). The above was gently     mixed and incubated O/N at room temperature. -   12. The biotinylated and folded MHC-complex solution was centrifuged     for 5 min. at 1700×g, room temperature. -   13. Correctly folded MHC-complex was separated and purified from     excess biotin, excess β2m, excess heavy chain and aggregates     thereof, by size exclusion chromatography on a column that separates     proteins in the 10-100 kDa range. Correctly folded monomer     MHC-complex was eluted with a MHC-buffer (20 mM Tris-HCl, 50 mM     NaCl, pH 8.0). The elution profile consisted of 4 peaks,     corresponding to aggregated Heavy Chain, correctly folded monomer     MHC-complex, β2m and excess biotin and peptide (See FIG. 8). -   14. Fractions containing the folded MHC-complex were pooled and     concentrated to approximately 1 ml in a suitable concentrator with a     5000 mw cut-off filter. The protein-concentration was estimated from     its absorption at 280 nm. -   15. Folded MHC-complex can optionally be stored at −170° C. before     further use. -   16. The grade of biotinylation was analyzed by a SDS PAGE     SHIFT-assay with Streptavidin (FIG. 9) and correct folding was     confirmed by ELISA, using the antibody W6/32 that recognizes     correctly folded MHC-peptide complex. -   17.

The above procedure may be used for folding any MHC I complexes consisting of any β2m, any heavy chain and any peptide approx. 8-11 amino acids long. Either of the components can be truncated or otherwise modified. The above procedure can also be used for generation of “empty” MHC I complexes consisting of β2m and heavy chain without peptide.

Example 2

This example describes how to generate soluble biotinylated MHC II complexes using a baculovirus expression system, where the MHC II complex was DR4 consisting of the α-chain DRA1*0101 and the β-chain DRB1*0401 as described by Svendsen et al., (2004), J. Immunol. 173(11):7037-45. Briefly, The hydrophobic transmembrane regions of the DRα and DRβ chains of DR4 were replaced by leucine zipper dimerization domains from the transcription factors Fos and Jun to promote DR α/β assembly. This was done by ligating cytoplasmic cDNA sequences of DRA1*0101 and DRB1*0401 to fos- and jun-encoding sequences. A birA site GLNDIFEAQKIEWH was added to the 3′ end of the DRA1*0101-fos template. Covalently bound peptide AGFKGEQGPKGEP derived from collagen II amino acid 261-273 were genetically attached by a flexible linker peptide to the N terminus of the DRβ-chain. Finally, the modified DRA1*0101 and DRB1*0401 inserts were cloned into the expression vector pAcAb3. The pAcAB3-DRA1*0101/DRB1*0401 plasmids were cotransfected with linearized baculovirus DNA (BD Pharmingen; BaculoGold kit) into Sf9 insect cells, according to the manufacturer's instructions. Following two rounds of plaque purification, clonal virus isolates were further amplified three times before preparation of high-titer virus (10⁸-10¹⁰/ml). These stocks were used to infect High Five or serum-free Sf21 insect cells (Invitrogen Life Technologies, Carlsbad, Calif.) for protein production. Spinner cultures (2-3×10⁶ cells/ml) were infected at a multiplicity of infection of 1-3 in a volume of 150 ml per 2 L spinner flask. Supernatants were harvested and proteinase inhibitor tablets (Roche, Basel, Switzerland) were added before affinity purification on MiniLeak-Low columns (Kem-En-Tec) coupled with the anti-HLA-DR monoclonal antibody L243. HLA-DR4 complexes were eluted with diethylamine (pH 11) into neutralization buffer (2 M Tris, pH 6.5) and immediately buffer exchanged and concentrated in PBS, 0.01% NaN₃, using Millipore (Bedford, Mass.) concentrators. The purity of protein was confirmed by SDS-PAGE. The purified DR4 complexes were biotinylated in vitro as described for MHC I complexes elsewhere herein. These complexes may now be used for coupling to any dimerization domain, e.g. divynylsulfone activated dextran 270 coupled with SA and a fluorochrome.

Example 3

This example describes how to generate empty biotinylated MHC II complexes using a baculovirus expression system, where the MHC II complex consist of any α-chain and any β-chain, including truncated and otherwise modified versions of the two. Briefly, The hydrophobic transmembrane regions of the DRα and DRβ chains of MHC II are replaced by leucine zipper dimerization domains from the transcription factors Fos and Jun to promote DR α/β assembly. This is done by ligating cytoplasmic cDNA sequences of DRα and DRβ to fos- and jun-encoding sequences. A birA site GLNDIFEAQKIEWH is added to the 3′ end of either the DRα-fos/DRα-jun or the DRβ-jun/DRβ-fos template. The modified DRα and DRβ inserts is cloned into the expression vector pAcAb3 and cotransfected with linearized baculovirus DNA into Sf9 insect cells, according to the manufacturer's instructions. Following rounds of plaque purification, clonal virus isolates is further amplified before preparation of high-titer virus. These stocks are used to infect High Five or serum-free Sf21 insect cells (Invitrogen Life Technologies, Carlsbad, Calif.) for protein production, e.g. as Spinner cultures. Supernatants are harvested and proteinase inhibitors added before affinity purification, e.g. using a MiniLeak-Low columns (Kem-En-Tec) coupled with anti-MHC II antibody. The purified MHC II complexes is biotinylated in vitro as described for MHC I complexes elsewhere herein. These biotinylated MHC II complexes may now be used for coupling to any dimerization domain, e.g. divynylsulfone activated dextran 270 coupled with SA and a fluorochrome.

Example 4

This example describes how to generate biotinylated MHC II complexes using a cell based protein expression system, where the MHC II complex consist of any α-chain and any β-chain, including truncated and otherwise modified versions of the two. The MHC II complex may also have a peptide bound in the peptide binding cleft.

The hydrophobic transmembrane regions of the MHC II α-chain and MHC II β-chain are replaced by leucine zipper dimerization domains from the transcription factors Fos and Jun to promote α/β chain assembly. This is done by ligating cytoplasmic cDNA sequences of α-chain and β-chain to fos- and jun-encoding sequences. A birA site GLNDIFEAQKIEWH is added to the 3′ end of the DRα-fos template. Optionally covalently bound peptide is genetically attached by a flexible linker peptide to the N terminus of the DRβ-chain. The modified DRα and DRβ inserts is cloned into a suitable expression vector and transfected into a cell line capable of protein expression, e.g. insect cells, CHO cells or similar. Transfected cells are grown in culture, supernatants are harvested and proteinase inhibitors added before affinity purification, e.g. using a MiniLeak-Low columns (Kem-En-Tec) coupled with anti-MHC II antibody. Alternatively the expressed MHC II complexes may be purified by anion- or cation-exchange chromatography. The purified MHC II complexes is biotinylated in vitro as described for MHC I complexes elsewhere herein. These biotinylated MHC II complexes may now be used for coupling to any dimerization domain, e.g. divynylsulfone activated dextran 270 coupled with SA and a fluorochrome.

Example 5

This is an example of how to make a MHC multimer that is a tetramer and where the MHC are attached to the multimerization domain through a non-covalent interaction The multimerization domain consist of Streptavidin. The MHC molecule was biotinylated DR4 consisting of the α-chain DRA1*0101 and the β-chain DRB1*0401 and the peptide AGFKGEQGPKGEP derived from collagen II amino acid 261-273. The biotinylated MHC-peptide complexes was generated as described in a previous example herein.

Fluorescent DR4-peptide tetramer complexes were assembled by addition of ultra-avidin-R-PE (Leinco Technologies, St. Louis, Mo.) at a final molar ratio of biotinylated to DR4-peptide ultra-avidin-R-PE of 6:1. The resulting DR4-peptide multimer complexes were subjected to size exclusion on a Superdex-200 column to separate the tetramer complexes from protein aggregates and lower molecular weight complexes and excess fre DR4-peptide. The tetramer complexes were concentrated using Centicon-30 concentrators and stored at 0.1-0.3 mg/ml in a mixture of protease inhibitors.

These complexes could be used to detect specific T cells in a flow cytometry assay as described by Svendsen et al. (2004) Tracking of Proinflammatory Collagen-Specific T cells in Early and Late Collagen-Induced Arthritis in Humanized mice. J. Immunol. 173:7037-7045.

Example 6

This example describes how an activated divinylsylfone-dextran (270 kDa) (VS-dex270) was coupled with streptavidin (SA) and Allophycocyanin (APC).

-   -   1. Streptavidin (approx. 100 mg SA/ml in 10 mM HEPES, 0.1M NaCl,         pH 7.85) was dialysed with gentle stirring for 2 days against 10         mM HEPES, 0.1M NaCl, pH 7.85 (20 fold excess volume) at 2-8° C.         with 1 buffer change/day.     -   2. 5 ml of APC from a homogen suspension (approx. 10 mg/ml) was         centrifuged 40 min. at 3000 rpm. The supernatant was discharged         and the precipitate dissolved in 5 ml of 10 mM HEPES, 0.1M NaCl,         pH 7.85. This APC solution was dialysed with gentle stirring in         the dark for 2 days against 10 mM HEPES, 0.1M NaCl, pH 7.85 (20         fold excess volume) at 2-8° C. with 1 buffer change/day.     -   3. The APC-solution was concentrated to 1 ml and the         concentration measured to 47 g/L at UV 650 nm. The         A650/A278-ratio was measured to 4.2.     -   4. The SA-solution was filtrated through a 0.45 μm filter and         the protein concentration was measured to 61.8 g SA/L at UV 278         nm.     -   5. Conjugation: The reagents was mixed to a total volume of 500         μl in the following order with 8.1 mol SA/mol Dex and 27 mol         APC/mol Dex.:         -   a) 90 μl water         -   b) 160 μl activated VS-dex270         -   c) 23 μl SA (61.8 g/L)˜8.1 equivalents,         -   d) 177 μl APC (47 g/L)˜27 equivalents,         -   e) 50 μl of 100 mM HEPES, 1M NaCl, pH 8

The reaction was placed in a water bath with stirring at 30° C. in the dark for 18 hours.

-   -   6. The coupling was stopped by adding 50 μl 0.1M ethanolamine,         pH 8.0.     -   7. The conjugate was purified on a Sephacryl S-200 column with         10 mM HEPES, 0.1M NaCl buffer, pH 7.2.     -   8. 3 peaks were collected (peak 1: APC-SA-dex270; peak 2: Free         APC; peak 3: Free SA). Volume, UV A650 and UV A278 were         measured.     -   9. The concentration of dextran270, APC/Dex and SA/Dex were         calculated to 22.4×10⁻⁸ M; 3.48 and 9.54 respectively.     -   10. The conjugate were added NaN₃ and BSA to a final         concentration of 15 mM and 1% respectively. The volume was         adjusted with 10 mM HEPES, 0.1M NaCl, pH 7.2 to a final         concentration of 16×10⁻⁸ M Dex270.     -   11. The conjugate were kept at 2-8° C. in dark until further         use.

Example 7

This example describes how an activated divinylsylfone-dextran (270 kDa) (VS-dex270) was coupled with streptavidin (SA) and R-phycoerythrin (RPE).

The coupling procedure described for coupling of SA and APC to VS-dex270 (as described elsewhere herein) were followed with the exception that APC were replaced with RPE

Example 8

This example describes how to couple an empty MHC or a MHC-complex to a dextran multimerization domain through a non-covalent coupling, to generate a MHC-dextramer. The MHC-dextramer in this example consisted of APC-streptavidin (APC-SA)-conjugated 270 kDA dextran and a biotinylated, folded MHC-complex composed of β2m, HLA-A*0201 heavy chain and the peptide NLVPMVATV.

The APC-SA conjugated 270 kDA dextran contained 3.7 molecules of SA per dextran (each SA can bind 3 MHC-complexes) and the concentration was 16×10⁻⁸ M. The concentration of the HLA-A*0201/NLVPMVATV-complex was 4 mg/ml (1 μg=20,663 pmol). The molecular concentration of the MHC-complex was 8.27×10⁻⁵M.

The MHC-Complex was Attached to the Dextran by a Non-Covalent Biotin-Streptavidin Interaction Between the Biotinylated Heavy Chain Part of the MHC-Complex and the SA, Conjugated to Dextran.

Here follows a protocol for how to produce 1000 μl of a MHC-dextramer solution with a final concentration of approximately 32×10⁻⁹M:

-   1. 200 μL 270 kDA vinylsulfone-activated dextran, corresponding to     3.2×10⁻¹¹ mol, and 4 μl MHC-complex, corresponding to 3.55×10⁻¹⁰ mol     was mixed and incubated at room temperature in the dark for 30 min. -   2. A buffer of 0.05M Tris-HCl, 15 mM NaN₃, 1% BSA, pH 7.2 was added     to a total volume of 1000 μl. -   3. The resulting MHC-dextramer preparation may now be used in flow     cytometry experiments.

Example 9

This is an example of how to make and use MHC multimers that are trimers consisting of a streptavidin multimerization domain with 3 biotinylated MHC complexes and 1 fluorophore molecule attached to the biotin binding pockets of streptavidin.

MHC complexes consisting of HLA-A*0201 heavy chain, beta2microglobulin and NLVPMVATV peptide or the negative control peptide GLAGDVSAV were generated as described elsewhere herein. The fluorophore in this example was Fluorescein-linker molecules as shown in FIG. 10. Each of these molecules consist of a linker-biotin molecule mounted with 4 trippel fluorescein-linker molecules. The linker-biotin molecule was here H-L30-Lys(NH₂)-L30-Lys(NH₂)-L30-Lys(NH₂)L300Lys(caproylamidobiotin)-NH₂ where L30 was a 30 atom large linker and L300 was a 300 atom large linker. Both L30 and L300 was composed of multiple L15 linkers with the structure shown in FIG. 10B. Linker-biotin molecules were generated as follows: Downloaded Boc-L300-Lys(Fmoc) resin (100 mg) was deprotected and subjected to coupling with Boc-Lys(2ClZ)—OH, Boc-L30-OH, Boc-Lys(2ClZ)—OH, Boc-L30-OH, Boc-Lys(2ClZ)—OH then Boc-L30-OH. The resin was Fmoc deprotected and reacted twice (2×2 h) with caproylamido biotin NHS ester (25 mg in 0.5 mL NMP+25 microL DIPEA). The resin was washed with TFA and the product cleaved off with TFA:TFMSA:mCresol:thioanisol (6:2:1:1), 1 mL, precipitated with diethyl ether and purified by RP-HPLC. MS calculated for C₃₀₀H₅₄₄N₆₄O₁₃₇S is 7272.009 Da, found 7271.19 Da.

Alternatively linker-biotin molecule was H-L60-Lys(NH₂)-L60-Lys(NH₂)-L60-Lys(NH₂)L300Lys(caproylamidobiotin)-NH₂ and made from downloaded Boc-L300-Lys(Fmoc) resin (100 mg), and then prepared analogously to H-L30-Lys(NH₂)-L30-Lys(NH₂)-L30-Lys(NH₂)L300Lys(caproylamidobiotin)-NH₂. MS calculated for C₃₆₀H₆₅₂N₇₆O₁₆₇S is 8749.5848 Da and was found to be 7271.19 Da. Yield 3 mg.

The trippel fluorescein-linker molecules was here betaalanin-L90-Lys(Flu)-L90-Lys(Flu)-L90-Lys(Flu)-NH₂ where Lys=Lysine, Flu=Fluorescein and L90 is a 90 atom linker (se FIG. 10 for further details). The trippel-fluorescein-linker molecule was generated as follows:

Downloaded Boc-Lys(Fmoc) resin, 2 g, was Boc deprotected and subjected to 3× coupling with Boc-L30-OH, Boc-Lys(Fmoc)-OH, 3×Boc-L30-OH, Boc-Lys(Fmoc)-OH, 3×Boc-L30-OH. The three Fmoc groups were removed and carboxyfluorescein, 301 mg, activated with HATU, 274 mg, and DIPEA, 139 μL, in 8 mL NMP, was added to the resin twice for 30 min. The resin was Boc deprotected and subjected to 2×30 min coupling with beta-alanine-N,N-diacetic acid benzyl ester, followed by 5 min treatment with 20% piperidine in NMP. The resin was washed with DCM, then TFA and the product was cleaved off the resin, precipitated with diethyl ether and purified by RP-HPLC. Yield was 621 mg. MS calculated for C268H402N44O116 is 6096.384 Da, while MS found was 6096 Da.

Biotin-linker molecule were coupled together with 4 trippel fluorescein-linker molecules as follows: (500 nmol) was dissolved in 88 microliter NMP+2 μl pyridine and activated for 10 min at room temperature (conversion to cyclic anhydride) by addition of 10 μl N,N′ diisopropylcarbodiimide. Following activation the trippel fluorescein-linker was precipitated with diethyl ether and redissolved in 100 microliter NMP containing 10 nmol biotin-linker Once dissolved the coupling was initiated by addition of 5 μl diisopropyl ethyl amine, and was complete after 30 min.

Streptavidin and Fluorescein-linker molecules are then mixed in a molar ration of 1:1 and incubated for ½ hour. Then MHC complexes are added in 3-fold molar excess in respect to streptavidin and incubated for another ½ hour. Alternatively, MHC complexes are added first, then Fluorescein-linker molecules or MHC complexes are mixed with Fluorescein-linker molecules before addition to Streptavidin.

These MHC multimers are then used to stain CMV specific T cells in a flow Cytometry experiment. 1×10⁶ purified HPBMC from a donor with T cells specific for HLA-A*0201(NLVPMVATV) are incubated with 10 μl of each of the two HLA-A*0201(peptide)/Fluorescein constructs described above for 10 minutes in the dark at room temperature with a cell concentration of 2×10⁷ cells/ml. 10 μl of mouse-anti-human CD8/PB (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on a flowcytometer.

In the above described example the Fluorescein-linker is as shown in FIG. 10 but the linker molecule can be any linker molecule as described in patent application WO 2007/015168 A2 (Lohse (2007)) or alternatively chemical biotinylated fluorochrom can be used instead of Fluorescein-linker molecules. The MHC complexes described in this example is a MHC I molecule composed of HLA-A*0201 heavy chain, beta2microglobulin and NLVPMVATV peptide but can in principle be any MHC complex or MHC like molecule as described elsewhere herein.

Example 10

This is an example of how to make MHC multimers consisting of a streptavidin multimerization domain with 3 biotinylated MHC complexes attached to the biotin binding pockets of streptavidin and how to use such trimer MHC complexes to detect specific T cells by direct detection of individual cells in a flow cytometry experiment by addition of a biotinylated fluorophore molecule. In this example the fluorophore is Fluorescein linker molecules constructed as described elsewhere herein.

MHC complexes consisting of HLA-A*0201 heavy chain, beta2microglobulin and peptide are generated as described elsewhere. MHC complexes are incubated with streptavidin in a molar ratio of 3:1 for ½ hour.

These trimer MHC multimers are then used to stain CMV specific T cells in a flow Cytometry experiment. 1×10⁶ purified HPBMC from a donor with T cells specific for HLA-A*0201(NLVPMVATV) are incubated with 10 μl HLA-A*0201(peptide) multimer construct for 10 minutes in the dark at room temperature with a cell concentration of 2×10⁷ cells/ml. Then Fluorescein linker molecules (as described in Example 42) are added and incubation continued for 5 minutes. 10 μl mouse-anti-human CD8/PB antibody (clone DK25 from Dako) is added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by addition of 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. Cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on a flowcytometer.

In this example the Fluorescein-linker is as shown in FIG. 10 but the linker molecule can be any linker molecule as described in Lohse, Jesper, (2007), WO 2007/015168 A2 or alternative chemically biotinylated fluorochrome may be used. The MHC complexes described in this example is a MHC I molecule composed of HLA-A*0201 heavy chain, beta2microglobulin and NLVPMVATV peptide but can in principle be any MHC complex or MHC like molecule as described elsewhere herein.

Example 11

This is an example of how to make MHC multimers where the multimerization domain is dextran and the MHC complexes are chemically conjugated to the dextran multimerization domain.

MHC complexes consisting of HLA-A*0201 heavy chain, beta2microglobulin and NLVPMVATV peptide or the negative control peptide GLAGDVSAV are generated as described elsewhere herein. Dextran with a molecular weight of 270 kDa is activated with divinylsulfone. Activated Dextran is then incubated with MHC and RPE in a 0.05 M NaCHO₃ buffer; pH=9.5 with a molar ratio between MHC and Dextran of 30-60 and a molar ratio between RPE and dextran of 3-7:1 The mixture is placed in a water bath at 30° C. for 16 hours. Excess fluorochrome, MHC and dextran are removed by FPLC using a sephacryl S-300 column.

These MHC/RPE dextramers are then used to stain CMV specific T cells in a flow Cytometry experiment. Briefly, 1×10⁶ purified HPBMC from a donor with T cells specific for HLA-A*0201(NLVPMVATV) are incubated with 10 μl of each of the two HLA-A*0201(peptide)/RPE constructs described above for 10 minutes in the dark at room temperature with a cell concentration of 2×10⁷ cells/ml. 10 μl mouse-anti-human CD8/PB antibody (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The cells are then resuspended in 400-500 μl PBS; pH=7.2 and analyzed on a flow cytometer.

Example 12

This is an example of how to make MHC multimers where the multimerization domain is dextran and MHC complexes are MHC I molecules chemically conjugated to dextran multimerization domain and the dextran multimerization domain also have fluorochrome chemically coupled.

Human beta2microglobulin is coupled to dextran as follows. Dextran with a molecular weight of 270 kDa is activated with divinylsulfone. Activated dextran is incubated with human beta2microglobulin and RPE in a 0.05 M NaCHO₃ buffer; pH=9.5 with a molar ratio between beta2microglobulin and Dextran of 30-60 and a molar ratio between RPE and dextran of 3-7:1. The molar ratio of the final product is preferable 4-6 RPE and 15-24 beta2microglobulin per dextran. The mixture is placed in a water bath at 30° C. for 16 hours. Excess fluorochrome, beta2microglobulin and dextran are removed by FPLC using a sephacryl S-300 column. The beta2microglobulin-RPE-dextran construct is then refolded in vitro together with heavy chain and peptide using the following procedure. 200 ml refolding buffer (100 mM Tris, 400 mM L-arginin-HCL, 2 mM NaEDTA, 0.5 mM oxidized Gluthathione, 5 mM reduced Glutathione, pH 8.0) supplied with protease inhibitors PMSF, Pepstatin A and Leupeptin (to a final concentration of 1 mM, 1 mg/l and 1 mg/l, respectively) is made and cooled to 10° C. 12 mg NLVPMVATV peptide is dissolved in DMSO and added to the refolding buffer together with 20-30 mg beta2microglobulin-RPE-dex and 6 mg HLA-A*0201 heavy chain. Incubation at 10° C. for 4-8 hours, then 20-30 mg beta2microglobulin-RPE-dex and 6 mg HLA-A*0201 heavy chain is added and incubation continued for 4-8 hours. Another 20-30 mg beta2microglobulin-RPE-dex and 6 mg HLA-A*0201 heavy chain is added and incubation continued for 6-8 hours. The folding reaction is filtrated through a 0.2 μm filter to remove larger aggregates and then buffer exchanged into a buffer containing 20 mM Tris-HCl, 50 nM NaCl; pH=8.0 followed by concentration to 1-2 ml sample. Dextran-RPE-MHC complexes are then separated from excess heavy chain and peptide by size exclusion chromatography using a sephacryl S-300, S-400 or sephacryl S-500 column.

These MHC/RPE dextramers may be used to stain CMV specific T cells in a flow Cytometry experiment. Briefly, 1×10⁶ purified HPBMC from a donor with T cells specific for HLA-A*0201(NLVPMVATV) are incubated with 10 μl of each of the two HLA-A*0201(peptide)/RPE constructs described above for 10 minutes in the dark at room temperature with a cell concentration of 2×10⁷ cells/ml. 10 μl of mouse-anti-human CD8/PB antibody (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The cells are then resuspended in 400-500 μl PBS; pH=7.2 and analyzed on a flowcytometer.

Example 13

The preparation of a Pentamer is described in e.g. (United States Patent application 20040209295). Briefly, the following steps lead to a fluorescent Pentamer reagent:

The following is a detailed example for cloning, expressing, and purifying a pentameric class I MHC complex, which comprises a chimeric fusion of .beta.2m with COMP. The chimeric .beta.2m-COMP protein is expressed in insoluble inclusion bodies in E. coli and subsequently assembled as pentameric .beta.2m-COMP in vitro. The pentameric class I MHC peptide complex is then formed in a second refolding reaction by combining beta.2m-COMP pentamers and the human MHC class I .alpha. molecule known as HLA-A*0201, in the presence of an appropriate synthetic binding peptide representing the T cell antigen. In this example, a well characterized antigen derived from Epstein-Barr virus BMLF1 protein, GLCTLVAML (a.a. 289-297) [SEQ ID NO: 1], is used. The resultant complex is labelled with a fluorescent entity and used as a staining reagent for detecting antigen-specific T cells from a mixed lymphocyte population, in a flow cytometry application.

The strategy involves the sequential cloning into pET-24c vector of .beta.2m, yielding a construct referred to as pETBMC01, followed by the insertion of the oligomerisation domain of cartilage oligomeric matrix protein (COMP) with a biotin acceptor sequence (BP) for site-specific biotinylation with the biotin-protein ligase BirA, yielding a construct referred to as pETBMC02. Thirdly a polyglycine linker is cloned in between .beta.2m and COMP, yielding a construct referred to as pETBMC03, and finally, a serine-residue is removed by site-directed mutagenesis, which serine residue precedes the poly-glycine linker, to give the final .beta.2m-COMP/pET-24c construct, referred to as pETBMC04 (see also FIG. 3). Removal of the serine residue is carried out to avoid steric hindrance when the .beta.2m molecule is associated with the MHC class I chain protein.

The extracellular portion of .beta.2m comprises of 99 amino acids (equivalent to Ile1-Met99 of the mature protein) encoded by 74 bp-370 by of the DNA sequence. This region of the .beta.2m sequence is amplified from a normal human lymphocyte cDNA library, by polymerase chain reaction (PCR)

beta.2m PCR product is purified from the above reaction mix using a QIAquick® PCR purification kit according to the manufacturer's instructions (Qiagen). 200 ng of purified PCR product and 1.mu.g pET-24c vector (Novagen) are each digested with BamH I (10 U) and Nde I (10 U) restriction enzymes (New England Biolabs, NEB) for 4 h at 37.degree. C., in accordance with the manufacturer's instructions, and purified.

The gel-purified insert and vector DNA are ligated at a 1:3 molar ratio (vector: insert, 50 ng: 7.5 ng) using T4 DNA ligase (5 U; Bioline), in T4 DNA ligase buffer (as supplied) for 16 hrs at 16.degree. C.

The ligation mixtures and appropriate controls are subsequently transformed into XL1-Blue strain competent E. coli cells, according to the manufacturer's instructions (Stratagene). Successful transformants are selected by plating the cells on Luria-Bertani (LB) agar plates containing 30 .mu.g/ml kanamycin, and incubating overnight at 37.degree. C.

A selection of single colonies from the bacterial transformation plates are screened by PCR with T7 promoter [SEQ ID NO: 4] (1 .mu.M) and T7 terminator [SEQ ID NO: 5] (1 .mu.M) primers (Sigma Genosys, see Appendix I for primer sequences), which are complementary to regions of the pET vector flanking the cloning site. Amplification is carried out using Taq DNA polymerase (1 U, Bioline) in Taq reaction buffer (as supplied), supplemented with 2 mM MgSO.sub.4 and 0.2 mM dNTPs, using 25 thermal-cycling reactions as detailed above. Successful transformants generated a DNA fragment of approximately 500 bp, ascertained by 1.5% agarose gel electrophoresis.

Bacterial transformants that generated the correct size of PCR products are inoculated into 6 ml of sterile LB-kanamycin medium and incubated overnight at 37.degree. C. with 200 rpm shaking. pETBMC01 plasmid DNA is recovered from the bacterial cultures using a QIAprep® Spin Mini-prep kit according to the manufacturer's instructions (Qiagen). The presence of the .beta.2m fragment in these plasmids is further verified by automated DNA sequencing.

The sequence of the oligomerisation domain of COMP is obtained from the Genbank database (accession #1705995) and a region encoding the coiled-coil domain (amino acids 21-85) is selected based on self-association experiments of COMP (Efinov et al., FEBS Letters 341:54-58 (1994)). A biotin acceptor sequence ‘BP’: SLNDIFEAQKIEWHE [SEQ ID NO: 6] is incorporated at the C terminus and an additional 14 amino acid linker, PQPQPKPQPKPEPET [SEQ ID NO:7] is included to provide a physical separation between the COMP oligomerising domain and BP.

The whole region is synthesized using the overlapping complementary oligonucleotides, and purified COMP-BP and 1 /.mu.g pETBMC01 vector are digested for 4 hrs at 37.degree. C. using Hind III (10 U) and Xho I (10 U) restriction enzymes (NEB), as described in Section 1.1. The digestion products are purified, ligated, transformed and PCR screened as in Section 1.1. Plasmids positive from the screen are purified and sequenced as described in Section 1.1.

The poly-glycine linker is synthesized by annealing overlapping oligonucleotides. Since the nucleotide sequence of the polyGlycine linker only incorporates the 5′ overhang of the cut BamH I restriction site, and the 3′ overhang of the cut Hind III nucleotide recognition motifs, there is no need to digest the annealed product to produce the complementary single-stranded overhangs suitable for subsequent ligation. The oligonucleotides are phosphorylated and annealed as described in Section 1.2.

pETBMC02 is digested with BamH I (10 U) and Hind III (10 U). Ligation of the annealed poly-glycine linker into pETBMC02 was as described previously (Section 1.1), assuming 96 fmoles of annealed oligonucleotide/.mu.l. The transformation and PCR-screening reactions are as described in Section 1.1, but in addition, the presence of an inserted linker is verified by a restriction enzyme digestion of the PCR screen product to ascertain the presence or absence of a Sal I restriction site. Successful transformants are not susceptible to Sal I digestion, given the removal of the site from the plasmid vector backbone. Purification of pETBMC03 and automated sequencing is as described in Section 1.1.

Analysis of X-ray crystallography models of MHC class I molecules reveal that the C terminus of .beta.2m closely abuts the .alpha.3 domain of the .alpha. chain. It is therefore desirable to achieve maximum flexibility at the start of the poly-glycine linker.

The extracellular portion of HLA-A*0201 .alpha. chain (EMBL M84379) comprises of 276 amino acids (equivalent to Gly1-Pro276 of the mature protein) encoded by bases 73-900 of the messenger RNA sequence. This region of the A*0201 sequence is amplified from a normal human lymphocyte cDNA library by PCR, using the primers A2S#1 [SEQ ID NO: 20] and A2S#2 [SEQ ID NO: 21] which incorporated NcoI and BamHI restriction sites respectively. The procedure for cloning the A*0201 insert into Nco I/BamH I-digested pET-11d vector (Novagen) is essentially as described for .beta.2m in Section 1.1.

An identical procedure is carried out to produce either .beta.2m-COMP or A*0201 .alpha. chain proteins. Plasmid DNA is transformed into an E. coli expression host strain in preparation for a large scale bacterial prep. Protein is produced as insoluble inclusion bodies within the bacterial cells, and is recovered by sonication. Purified inclusion bodies are solubilised in denaturing buffer and stored at −80.degree. C. until required.

Purified plasmid DNA is transformed into the BL21(DE3)pLysS E. coli strain, which carries a chromosomal copy of the T7 RNA polymerase required to drive protein expression from pET-based constructs. Transformations into BL21(DE3)pLysS competent cells (Stratagene) are carried out with appropriate controls.

A single bacterial transformant colony is innoculated into 60 ml sterile LB medium, containing appropriate antibiotics for selection, and left to stand overnight in a warm room (.about.24.degree. C.) The resulting overnight culture is added to 6 liters of LB and grown at 37.degree. C. with shaking (.about.240 rpm), up to mid-log phase (OD.sub.600=0.3-0.4). Protein expression is induced at this stage by addition of 1.0 ml of 1M IPTG to each flask. The cultures are left for a further 4 h at 37.degree. C. with shaking, after which the cells are harvested by centrifugation and the supernatant discarded.

The bacterial cell pellet is resuspended in ice-cold balanced salt solution and sonicated (XL series sonicator; Misonix Inc., USA) in a small glass beaker on ice in order to lyse the cells and release the protein inclusion bodies. Once the cells are completely lysed the inclusion bodies are spun down in 50 ml polycarbonate Oak Ridge centrifuge tubes in a Beckman high-speed centrifuge (J2 series) at 15,000 rpm for 10 min. The inclusion bodies are then washed three times in chilled Triton® wash This is followed by a final wash in detergent-free wash buffer.

The resultant purified protein preparation is solubilised in 20-50 ml of 8 M urea buffer, containing 50 mM MES, pH 6.5, 0.1 mM EDTA and 1 mM DTT, and left on an end-over-end rotator overnight at 4.degree. C. Insoluble particles are removed by centrifugation and the protein yield is determined using Bradford's protein assay reagent (Bio-Rad Laboratories) and by comparison with known standards. Urea-solubilised protein is dispensed in 10 mg aliquots and stored at −80.degree. C. for future use.

Assembly of .beta.2m-COMP from the urea-solubilised inclusion bodies is performed by diluting the protein into 20 mM CAPS buffer, pH 11.0, containing 0.2 M sodium chloride and 1 mM EDTA, to give a final protein concentration of 1.5 mg/ml. The protein is oxidised at room temperature by addition of oxidised and reduced glutathione to final concentrations of 20 mM and 2 mM, respectively. Following an overnight incubation, disulphide bond formation is analysed by non-reducing SDS-PAGE on 10% bis-tricine gels (Invitrogen).

The protein mixture is subsequently buffer exchanged into 20 mM Tris, pH 8.0, 50 mM sodium chloride (‘S200 buffer’), and concentrated to a final volume of 4.5 ml, in preparation for enzymatic biotinylation with BirA (Affinity, Denver, Colo.). 0.5 ml of 10.times. BirA reaction buffer (as supplied) is added, and recombinant BirA enzyme at 10 /.mu.M final concentration, supplemented with 10 mM ATP, pH 7.0. A selection of protease inhibitors is also used to preserve the proteins: 0.2 mM PMSF, 2 /.mu.g/ml pepstatin and 2 /.mu.g/ml leupeptin. The reaction is left for 4 hours at room temperature.

Biotinylated .beta.2m-COMP is purified by size exclusion chromatography (SEC) on a Superdex®200 HR 26/60 column (Amersham Biosciences), running S200 buffer.

500 ml of refolding buffer is prepared as follows: 100 mM Tris, pH 8.0, 400 mM Larginine hydrochloride, 2 mM EDTA, 5 mM reduced glutathione and 0.5 mM oxidised glutathione, dissolved in deionised water and left stirring at 4.degree. C. 15 mg of lyophilised synthetic peptide GLCTLVAML is dissolved in 0.5 ml dimethylsulfoxide and added to the refolding buffer whilst stirring. 50 mg of biotinylated pentameric .beta.2m-COMP and 30 mg of A*0201 .alpha. chain is added sequentially, injected through a 23 gauge hypodermic needle directly into the vigorously-stirred buffer, to ensure adequate dispersion. The refolding mixture is then left stirring gently for 16 hours at 4.degree. C.

The protein refolding mixture is subsequently concentrated from 500 ml to 20 ml using a MiniKros hollow fibre ultrafiltration cartridge (Spectrum Labs, Rancho Dominguez, Calif.) with a 30 kD molecular weight cutoff. Further concentration of the complex from 20 ml to 5 ml is carried out in Centricon Plus-20 centrifugal concentrators (30 kD molecular weight cut-off) according to the manufacturers instructions, followed by buffer exchange into S200 buffer using disposable PD10 desalting columns (Amersham Biosciences), according to the manufacturer's instructions. Final volume is 7.5 ml. The concentrated protein refold mixture is first purified by SEC on a Superdex® 200 HR 26/60 gel filtration chromatography column, as in Section 4.2. Fractions containing protein complexes in the region of 310 kD is collected.

Fractions collected from SEC are pooled and subjected to further purification by anion exchange chromatography on a MonoQ® HR 5/5 column (Amersham Biosciences), running a salt gradient from 0-0.5 M sodium chloride in 20 mM Tris over 15 column volumes. The dominant peak is collected. Protein recovery is determined using the Bradford assay.

Since each streptavidin molecule is able to bind up to 4 biotin entities, final labelling with phycoerythrin (PE)-conjugated streptavidin is carried out in a molar ratio of 1:0.8, streptavidin to biotinylated pentamer complex respectively, taking into account the initial biotinylation efficiency measurement made for .beta.2m-COMP in Section 4.2. The total required amount of pentamer complex is subdivided (e.g. into 5 equal amounts) and titrated successively into streptavidin-PE. The concentration of A*0201 pentamer-streptavidin complex is adjusted to 1 mg/ml with phosphate buffered saline (PBS), supplemented with 0.01% azide and 1% BSA.

This resultant fluorescent Pentamer reagent is stored at 4.degree. C.

Example 14. Prediction of MHC Class 1 BK Virus Peptide Binders

This example describes the total approach, applied to the BK virus genome. It thus involves the translation of the genome in both directions, i.e. in six possible reading frames.

Prediction of MHC class 1 BK virus peptide sequences for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus-specific T-cells. Prediction is carried out using the total approach. Thus, the 8-, 9-, 10- and 11-mer peptide sequences are generated from six amino acid sequences representing direct translation of the BK virus genome sequence in all six reading frames. The 8-, 9-, 10- and 11-mer peptide sequences are derived from the genome sequence by application of the software program described in (FIG. 2). The 8-, 9-, 10- and 11-mer peptide sequences are shown in table I.

Example 15. Prediction of MHC Class 2 BK Virus Peptide Binders

This example describes the total approach, applied to the BK virus genome. It thus involves the translation of the genome in both directions, i.e. in six possible reading frames.

Prediction of MHC class 2 BK virus peptide sequences for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus-specific T-cells. Prediction is carried out using the total approach. Thus, the 13-, 14-, 15- and 16-mer peptide sequences are generated from six amino acid sequences representing direct translation of the BK virus genome sequence in all six reading frames. The 13-, 14-, 15- and 16-mer peptide sequences are derived from the genome sequence by application of the software program described in (FIG. 2). The 13-, 14-, 15- and 16-mer peptide sequences are shown in table O.

Example 16. Prediction of MHC Class 1 Peptide Binders for BK Agnoprotein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the Agnoprotein encoded by the BK virus genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 1 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 42 HLA class 1 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 8-, 9-, 10- and 11-mer peptide binders of the 42 HLA class 1 alleles. The result can be seen in table N. The MHC class 1 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 17. Prediction of MHC Class 1 Peptide Binders for BK Small t Protein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the small t protein encoded by the BK virus genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 1 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 42 HLA class 1 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 8-, 9-, 10- and 11-mer peptide binders of the 42 HLA class 1 alleles. The result can be seen in table L. The MHC class 1 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 18. Prediction of MHC Class 1 Peptide Binders for BK Large T Protein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the Large T protein encoded by the BK virus genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 1 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 42 HLA class 1 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 8-, 9-, 10- and 11-mer peptide binders of the 42 HLA class 1 alleles. The result can be seen in table M. The MHC class 1 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 19. Prediction of MHC Class 1 Peptide Binders for BK VP1 Protein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the VP1 protein encoded by the BK virus genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 1 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 42 HLA class 1 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 8-, 9-, 10- and 11-mer peptide binders of the 42 HLA class 1 alleles. The result can be seen in table K. The MHC class 1 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 20. Prediction of MHC Class 1 Peptide Binders for BK VP2-3 Protein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the VP2-3 protein encoded by the human genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 1 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 42 HLA class 1 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 8-, 9-, 10- and 11-mer peptide binders of the 42 HLA class 1 alleles. The result can be seen in table J. The MHC class 1 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 21. Prediction of MHC Class 1 Peptide Binders for Human Cancer Protein Bcl-2 Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the cancer protein Bcl-2 encoded by the human genome. The purpose is to predict Bcl-2 peptide sequences that binds to MHC class 1 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with human Bcl-2 specific T-cells. Prediction is carried out using the known preferences of the 42 HLA class 1 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 8-, 9-, 10- and 11-mer peptide binders of the 42 HLA class 1 alleles. The result can be seen in table C. The MHC class 1 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 22. Prediction of MHC Class 1 Peptide Binders for Human Cancer Protein BclX(L) Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the cancer protein BclX(L) encoded by the human genome. The purpose is to predict BclX(L) peptide sequences that binds to MHC class 1 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with human BclX(L) specific T-cells. Prediction is carried out using the known preferences of the 42 HLA class 1 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 8-, 9-, 10- and 11-mer peptide binders of the 42 HLA class 1 alleles. The result can be seen in table B. The MHC class 1 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 23. Prediction of MHC Class 1 Human Cancer Protein Survivin Peptide Binders

This example describes the prediction of MHC class 1 human Survivin peptide sequences for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with human Survivin specific T-cells. Prediction of the 8-, 9-, 10- and 11-mer peptide sequences are carried out using the peptide generation software program described in FIG. 2. The outcome is shown in table F.

Example 24. Prediction of MHC Class 2 Peptide Binders for BK Agnoprotein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the Agnoprotein encoded by the BK virus genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 2 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 14 HLA class 2 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 15-mer peptide binders of the 14 HLA class 2 alleles. It also finds the important central nonamer core peptide sequence of each binding peptide. The result can be seen in table T. The MHC class 2 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 25. Prediction of MHC Class 2 Peptide Binders for BK Small t Protein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the small t protein encoded by the BK virus genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 2 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 14 HLA class 2 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 15-mer peptide binders of the 14 HLA class 2 alleles. It also finds the important central nonamer core peptide sequence of each binding peptide. The result can be seen in table R. The MHC class 2 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 26. Prediction of MHC Class 2 Peptide Binders for BK Large T Protein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the Large T protein encoded by the BK virus genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 2 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 14 HLA class 2 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 15-mer peptide binders of the 14 HLA class 2 alleles. It also finds the important central nonamer core peptide sequence of each binding peptide. The result can be seen in table S. The MHC class 2 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 27. Prediction of MHC Class 2 Peptide Binders for BK VP1 Protein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the VP1 protein encoded by the BK virus genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 2 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 14 HLA class 2 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 15-mer peptide binders of the 14 HLA class 2 alleles. It also finds the important central nonamer core peptide sequence of each binding peptide. The result can be seen in table Q. The MHC class 2 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 28. Prediction of MHC Class 2 Peptide Binders for BK VP2-3 Protein Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the VP1 protein encoded by the BK virus genome. The purpose is to predict BK virus peptide sequences that binds to MHC class 2 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with BK virus specific T-cells. Prediction is carried out using the known preferences of the 14 HLA class 2 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 15-mer peptide binders of the 14 HLA class 2 alleles. It also finds the important central nonamer core peptide sequence of each binding peptide. The result can be seen in table P. The MHC class 2 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 29. Prediction of MHC Class 2 Human Cancer Protein Mcl-1 Peptide Binders

This example describes the prediction of MHC class 2 human Mcl-1 peptide sequences for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with human Mcl-1 specific T-cells. Prediction of the 13-, 14-, 15- and 16-mer peptide sequences are carried out using the peptide generation software program described in FIG. 2. The outcome is shown in table G.

Example 30. Prediction of MHC Class 2 Peptide Binders for Human Cancer Protein Bcl-2 Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the cancer protein Bcl-2 encoded by the human genome. The purpose is to predict Bcl-2 peptide sequences that binds to MHC class 2 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with human Bcl-2 specific T-cells. Prediction is carried out using the known preferences of the 14 HLA class 2 alleles included in the www.cbs.dtu.dk/services/NetMHCII/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 15-mer peptide binders of the 14 HLA class 2 alleles. It also finds the important central nonamer core peptide sequence of each binding peptide. The result can be seen in table E. The MHC class 2 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 31. Prediction of MHC Class 2 Peptide Binders for Human Cancer Protein BclX(L) Using Directed Approach

This example describes the directed approach, applied to a known protein sequence, the cancer protein BclX(L) encoded by the human genome. The purpose is to predict BclX(L) peptide sequences that binds to MHC class 2 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with human BclX(L) specific T-cells. Prediction is carried out using the known preferences of the 14 HLA class 2 alleles included in the www.cbs.dtu.dk/services/NetMHCII/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 15-mer peptide binders of the 14 HLA class 2 alleles. It also finds the important central nonamer core peptide sequence of each binding peptide. The result can be seen in table D. The MHC class 2 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 32. Prediction of MHC Class 1 and 2 Borrelia afzelii OspC Peptide Binders

This example describes the prediction of MHC class 1 and 2 Borrelia afzelii OspC peptide sequences for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with Borrelia afzelii OspC specific T-cells. Prediction of the 8-, 9-, 10-, 11-, 13-, 14-, 15- and 16-mer peptide sequences are carried out using the peptide generation software program described in FIG. 2. The outcome is shown in table U.

Example 33. Prediction of MHC Class 1 Borrelia burgdorferi OspA Peptide Binders

This example describes the directed approach, applied to a known protein sequence, the Borrelia burgdorferi protein OspA encoded by the Borrelia genome. The purpose is to predict OspA peptide sequences that binds to MHC class 1 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with human OspA specific T-cells. Prediction is carried out using the known preferences of the 42 HLA class 1 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 8-, 9-, 10- and 11-mer peptide binders of the 42 HLA class 1 alleles. The result can be seen in table V. The MHC class 1 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 34. Prediction of MHC Class 1 Borrelia garinii Flab Peptide Binders

This example describes the directed approach, applied to a known protein sequence, the Borrelia garinii protein FlaB encoded by the Borrelia genome. The purpose is to predict FlaB peptide sequences that binds to MHC class 1 molecules for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with human FlaB specific T-cells. Prediction is carried out using the known preferences of the 42 HLA class 1 alleles included in the www.cbs.dtu.dk/services/NetMHC/ database (FIG. 11).

The result of the prediction software is used to find all strong and weak 8-, 9-, 10- and 11-mer peptide binders of the 42 HLA class 1 alleles. The result can be seen in table X. The MHC class 1 alleles for whom no binders are predicted are omitted from the list. The listed peptides are ranked according to decreased binding affinity for the individual MHC alleles. Strong binders are defined as binders with an affinity value of less than 50 nM and weak binders with a value of less than 500 nM. Only peptides defined as weak or strong binders are shown.

Example 35. Prediction of MHC Class 1 and 2 Mycobacterium tuberculosis CFP10 Peptide Binders

This example describes the prediction of MHC class 1 and 2 Mycobacterium tuberculosis CFP10 peptide sequences for use in construction of MHC′mers designed to be used for analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with Mycobacterium tuberculosis CFP10 specific T-cells. Prediction of the 8-, 9-, 10-, 11-, 13-, 14-, 15- and 16-mer peptide sequences are carried out using the peptide generation software program described in FIG. 2. The outcome is shown in table Y.

Example 36. Prediction of MHC Class 1 LCMV Gp1 Nonamer Peptide Binders for Mouse H-2Kd

An Example of Non-Human MHC Peptide Binding Motifs.

This example describes the directed approach, applied to the known protein sequence of a mouse virus protein LCMV gp1 in context of mouse MHC class 1.

Prediction of LCMV gp1 peptide sequences that binds to the MHC class 1 molecule H-2Kd for use in construction of MHC′mers designed to be used for as analytical, diagnostic, prognostic, therapeutic and vaccine purposes, through the interaction of the MHC′mers with LCMV specific mouse T-cells. Prediction is carried out using the known preferences of the given H-2 molecules for peptide binding as laid down in the prediction program found on www.syfpeithi.de. The generated 9-mer peptides are ranked according to their binding efficiency to the individual HLA class 1 molecules. The output is shown in FIG. 2.

Example 37. Test of Predicted BclX(L) 10-mer Binding Peptide Functionality in Elispot

In example 22 the best binding BclX(L) 10-mer peptide for HLA-A*0201 was identified to be YLNDHLEPWI (SEQ ID NO.: 46196). This peptide has then been tested in ELISPOT to see if it were able to detect the presence Bcl-X(L)-specific, CD8 positive T cells in PBL (Peripheral Blood Lymphocytes) from a breast cancer patient. PBL from a breast cancer patient was analyzed by ELISPOT ex vivo either with or without the Bcl-X(L)173-182 peptide (YLNDHLEPWI (SEQ ID NO.: 46196)), 106 PBL/well in doublets. The number of spots was counted using the Immunospot Series 2.0 Analyzer (CTL Analysers). The result is given as number of spots above the pictures of the result as shown in FIG. 15 and it clearly shows the presence of BclX(L) specific T-cells and thereby the functionality of the peptide as compared to the absence of added peptide.

Example 38. Test of Predicted BclX(L) 10-mer Binding Peptide Functionality in Flow Cytometry

In example 22 the best binding BclX(L) 10-mer peptide for HLA-A*0201 was identified to be YLNDHLEPWI (SEQ ID NO.: 46196). In the present example the functionality of the peptide is shown in a flow cytometric analysis of PBL from the patient was analyzed ex vivo by Flow cytometry to identify Bcl-X(L)173-182 specific CD8 T cells using the dextramer complex HLA-A2/Bcl-X(L)173-182-APC, 7-AAD-PerCP, CD3-FITC, and CD8-APC-Cy7. The dextramer complex HLA-A2/HIV-1 pol476-484-APC was used as negative control. The result (FIG. 16) clearly demonstrate that a MHC Dextramer HLA-A*0201/YLNDHLEPWI (SEQ ID NO.: 46196) complex detects BclX(L) antigen specific CD-8 cells in the patient sample at a level of 0.03% as compared with the negative control using HIV specific MHC Dextramer.

Example 39. Use of BclX(L) Specific MHC Dextramer for Sorting of Antigen Specific CD8 T Cells from Patient Sample

The antigen specific CD8 positive T-cells of example 38 were sorted out during the flow cytometric analysis using the MHC Dextramer HLA-A*0201/YLNDHLEPWI (SEQ ID NO.: 46196). The detectable population of dextramer positive CD8 T cells was sorted as single cells into 96 well plates using the following protocol:

Small lymphocytes were gated by forward and side scatter profile, before cloning according to CD8/MHC-multimer double staining. CD8/MHC-multimer double-positive cells were sorted as single cells into 96 well plates (Nunc) already containing 10⁵ cloning mix cells/well. The cloning mix was prepared containing 10⁶ irradiated (20 Gy) lymphocytes from three healthy donors per nil in X-vivo with 5% heat-inactivated human serum, 25 mM HEPES buffer (GibcoBRL), 1 μg/ml phytohemagglutinin (PHA) (Peprotech) and 120 U/ml IL-2. The cloning mix was incubated for two hours at 37° C./5% CO₂, prior to cloning. After cloning, the plates were incubated at 37° C./5% CO₂. Every 3-4 days 50 μL1 fresh media were added containing IL-2 to a final concentration of 120 U/ml. Following 10-14 days of incubation, growing clones were further expanded using cloning mix cells. Consequently, each of the growing clones were transferred (split) into two or three wells (depending on the number of growing cells) of a new 96 well plate containing 5×10⁴ cloning mix cells/well. Clones that were not growing at this time were incubated for another week with IL-2, and then expanded. Subsequently, the specificity of the growing clones was tested in a ⁵¹Cr-release assay or by FACS.

Out of twenty-isolated dextramer positive CD8 T cells, ten were able to be expanded into T-cell clones.

Example 40. Demonstration of Specific Cytolytic Activity of Isolated BclX(L) Specific CD8 T-Cells

The ten expanded T cell clones isolated by Flow sorting as shown in example 39 were tested for their specificity by analysis in a standard 51-Cr release assay. For this purpose, T2 cells loaded with either Bcl-X(L)173-182 peptide or an irrelevant peptide (BA4697-105, GLQHWVPEL) were used as target cells. Five CD8 T-cell clones (Clone 8, 9, 10, 11, and 12) effectively lysed T2 cells pulsed with Bcl-X(L)173-182 without killing of T2 cells pulsed with an irrelevant peptide (FIG. 17). One of these BclX(L)173-182 specific CD8 T-cell clones [Clone 9] were expanded for further analyses. The remaining five expanded clones (Clone 7, 13, 15, 17, and 18) did not show specific lysis against T2 cells pulsed with Bcl-X(L)173-182 peptide (FIG. 8).

Example 41. Demonstration of the Cytotoxic Capacity of a BclX(L)173-182 Specific CD8 T Cell Clone Isolated by Flow Aided Sorting of Antigen (HLA-A*0201/YLNDHLEPWI (SEQ ID NO.: 46196) Specific T Cells

The Bcl-X(L)173-182 specific clone 9 was expanded for additional 2 weeks before the cytotoxic potential was examined further in 51Cr-release assays. Two assays were performed a Cell lysis of T2 cells pulsed with Bcl-X(L)173-182 peptide or an irrelevant peptide (BA4697-105, GLQHWVPEL) in three E:T ratios. b Cell lysis of T2 cells pulsed with different concentrations of Bcl-X(L)173-182 peptide at the E:T ratio 1:1 The result is given in FIG. 18. As can be seen the presence of the specific peptide is necessary to get killing of the target cell and the effect of the peptide is significant even at low concentrations.

Example 42. Synthesis of a Comprehensive Library of Antigenic Peptides of Variable Size Derived from a Full-Length Antigen Sequence

In this example it is described how virtually all of the possible 8′- to 20′-mer peptide epitopes of an antigen may be synthetically prepared by modification of the standard Fmoc peptide synthesis protocol.

N-□-amino acids are incorporated into a peptide of the desired sequence with one end of the sequence remaining attached to a solid support matrix. All soluble reagents can be removed from the peptide-solid support matrix by filtration and washed away at the end of each coupling step. After each of the coupling steps, and after the removal of reagents, a fraction of the generated peptides are removed and recovered from the polymeric support by cleavage of the cleavable linker that links the growing peptide to solid support.

The solid support can be a synthetic polymer that bears reactive groups such as —OH. These groups are made so that they can react easily with the carboxyl group of an N-□-protected amino acid, thereby covalently binding it to the polymer. The amino protecting group can then be removed and a second N-□-protected amino acid can be coupled to the attached amino acid. These steps are repeated until the desired sequence is obtained. At the end of the synthesis, a different reagent is applied to cleave the bond between the C-terminal amino acid and the polymer support; the peptide then goes into solution and can be obtained from the solution.

Initially, the first Fmoc amino acid (starting at the C-terminal end of the antigen sequence) is coupled to a precursor molecule on an insoluble support resin via an acid labile linker. Deprotection of Fmoc is accomplished by treatment of the amino acid with a base, usually piperidine. Before coupling the next amino acid, a fraction of the synthesized peptide (for example 0.1%) is detached from the solid support, and recovered. Then additional beads carrying only the precursor molecule including the linker (for example corresponding to 0.1% of the total amount of solid support in the reaction) is added. Then the next Fmoc amino acid is coupled utilizing a pre-activated species or in situ activation.

This cycle of amino acid coupling, removal of reagents, detachment of a small fraction of synthesized peptide and recovery of these, and activation of the immobilized peptide to prepare for the next round of coupling, goes on until the entire antigen sequence has been processed.

The recovered peptides thus represent different fragments of the antigen, with varying lengths. The peptide pool thus contains most or all of the possible peptide epitopes of the antigen, and may be used in the preparation of MHC multimers as a pool.

The entire process, including the detachment of a fraction of the peptides after each round of coupling, follows standard Fmoc peptide synthesis protocols, and involves weak acids such as TFA or TMSBr, typical scavengers such as thiol compounds, phenol and water, and involves standard protecting groups.

Example 43

This is an example of how MHC multimers may be used for detection of cancer specific T cells in blood samples from patients.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow Cytometry. The antigen origin is cancer, thus, immune monitoring of a cancer.

MHC multimers carrying cancer specific peptides is in this example used to detect the presence of cancer specific T cells in the blood from cancer patients.

Purified MHC-peptide complexes consisting of HLA-A*1101 heavy chain, human beta2microglobulin and peptide derived from a region in Survivin (Table F) or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes were then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain was generated as described elsewhere herein. MHC-peptide complexes were added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contains 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran was 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs were made:

-   -   1. APC-SA conjugated 270 kDa dextran coupled with HLA-A*1101 in         complex with beta2microglobulin and the peptide DLAQCFFCFK         derived from Survivin.     -   2. APC-SA conjugated 270 kDa dextran coupled with HLA-A*1101 in         complex with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran was used to determine the presence of Survivin specific T cells in the blood from cancer patients by flow cytometry following a standard flow cytometry protocol.

Blood from a cancer patient is isolated and 100 ul of this blood is incubated with 10 μl of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako), and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continues for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC dextran construct 1 described above and thereby the presence of Survivin specific T cells in the blood. Blood analysed with MHC(peptide)/APC dextran construct 2 show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the Survivin specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of Survivin specific T cells in the blood of cancer.

Example 44

This is an example of how MHC multimers may be used for detection of cancer specific T cells in blood samples from patients.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled multimerisation domain Streptavidin (SA, used for direct detection of TCR in flow Cytometry. The antigen origin is cancer, thus, immune monitoring of a cancer.

MHC multimers carrying cancer specific peptides is in this example used to detect the presence of cancer specific T cells in the blood from cancer patients.

Purified MHC-peptide complexes consisting of HLA-A*1101 heavy chain, human beta2microglobulin and peptide derived from a region in Survivin (Table F) or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes were added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes were purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   3. APC-SA coupled with HLA-A*1101 in complex with         beta2microglobulin and the peptide DLAQCFFCFK derived from         Survivin.     -   4. APC-SA coupled with HLA-A*1101 in complex with         beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Survivin specific T cells in the blood from cancer patients by flow cytometry following a standard flow cytometry protocol.

Blood from a cancer patient is isolated and 100 ul of this blood is incubated with either of the SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the SA-MHC(peptide)/APC tetramers 3 described above and thereby the presence of Survivin specific T cells in the blood. Blood analysed with SA-MHC(peptide)/APC tetramers 4 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the Survivin specific T cells.

We conclude that the APC-SA coupled MHC(peptide) constructs may be used to detect the presence of Survivin specific T cells in the blood of cancer patients.

Example 45

This is an example of how MHC multimers may be used for detection of cancer specific T cells in blood samples from patients.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow Cytometry. The antigen origin is cancer, thus, immune monitoring of a cancer.

MHC multimers carrying cancer specific peptides is in this example used to detect the presence of cancer specific T cells in the blood from cancer patients.

Purified MHC-peptide complexes consisting of HLA-A*1101 heavy chain, human beta2microglobulin and peptide derived a region in Survivin (Table F) or a negative control peptide were generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   5. APC-multimerisation domain coupled with HLA-A*1101 in complex         with beta2microglobulin and the peptide DLAQCFFCFK derived from         Survivin.     -   6. APC-multimerisation domain coupled with HLA-A*1101 in complex         with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of Survivin specific T cells in the blood from cancer patients by flow cytometry following a standard flow cytometry protocol.

Blood from a cancer patient is isolated and 100 ul of this blood is incubated with either of the MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC multimers 5 described above and thereby the presence of Survivin specific T cells in the blood. Blood analysed with MHC(peptide)/APC multimer 6 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the Survivin specific T cells.

We conclude that the APC-multimerisation domain coupled MHC(peptide) constructs may be used to detect the presence of Survivin specific T cells in the blood of cancer patients.

Example 46

This is an example of how MHC multimers may be used for detection of Epstein-Barr Virus (EBV) specific T cells in blood samples from humans infected with EBV.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow cytometry.

The antigen origin is EBV, thus, immune monitoring of EBV infection MHC multimers carrying EBV specific peptides is in this example used to detect the presence of EBV specific T cells in the blood of patients infected with Epstein-Barr virus.

Purified MHC-peptide complexes consisting of HLA-B*0702 heavy chain, human beta2microglobulin and peptide derived from a region in EBV nuclear antigen (EBNA) or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain is generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contains 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran is 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs are made:

-   -   7. APC-SA conjugated 270 kDa dextran coupled with HLA-B*0702 in         complex with beta2microglobulin and the peptide RPPIFIRRL         derived from EBNA 3A.     -   8. APC-SA conjugated 270 kDa dextran coupled with HLA-B*0702 in         complex with beta2microglobulin and the peptide QPRAPIRPI         derived from EBNA 6.     -   9. APC-SA conjugated 270 kDa dextran coupled with HLA-B*0702 in         complex with beta2microglobulin and the HIV peptide TPGPGVRYPL.

The binding of the above described MHC(peptide)/APC dextran is used to determine the presence of EBV specific T cells in the blood from EBV infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with EBV infection is isolated and 100 ul of this blood is incubated with 10 μl of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako), and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continues for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 300×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC dextran construct 1 or 2 described above and thereby the presence of EBV specific T cells indicate that the patient are infected with Epstein-Barr virus. Blood analysed with MHC(peptide)/APC dextran construct 3 show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the EBV specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of EBV specific T cells in the blood of patients infected with Epstein-Barr virus.

Example 47

This is an example of how MHC multimers may be used for detection of Epstein-Barr Virus (EBV) specific T cells in blood samples from humans infected with EBV.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow cytometry. The antigen origin is EBV, thus, immune monitoring of EBV infection

MHC multimers carrying EBV specific peptides is in this example used to detect the presence of EBV specific T cells in the blood of patients infected with Epstein-Barr virus.

Purified MHC-peptide complexes consisting of HLA-B*0702 heavy chain, human beta2microglobulin and peptide derived from a region in EBV nuclear antigen (EBNA) or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes were added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes were purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   10. APC-SA coupled with HLA-B*0702 in complex with         beta2microglobulin and the peptide RPPIFIRRL derived from EBNA         3A.     -   11. APC-SA coupled with HLA-B*0702 in complex with         beta2microglobulin and the peptide QPRAPIRPI derived from EBNA         6.     -   12. APC-SA coupled with HLA-B*0702 in complex with         beta2microglobulin and the HIV peptide TPGPGVRYPL.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of EBV specific T cells in the blood from Epstein-Barr virus infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with EBV is isolated and 100 ul of this blood is incubated with either of the SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the SA-MHC(peptide)/APC tetramers 4 or 5 described above and thereby the presence of EBV specific T cells will indicate that the patient are infected with Epstein-Barr virus. Blood analysed with SA-MHC(peptide)/APC tetramers 6 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the EBV specific T cells.

We conclude that the APC-SA coupled MHC(peptide) constructs may be used to detect the presence of EBV specific T cells in the blood of patients infected with Epstein-Barr virus

Example 48

This is an example of how MHC multimers may be used for detection of Epstein-Barr Virus (EBV) specific T cells in blood samples from humans infected with EBV.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is EBV, thus, immune monitoring of EBV infection

MHC multimers carrying EBV specific peptides is in this example used to detect the presence of EBV specific T cells in the blood of patients infected with Epstein-Barr virus.

Purified MHC-peptide complexes consisting of HLA-B*0702 heavy chain, human beta2microglobulin and peptide derived a region in EBV nuclear antigen (EBNA) or a negative control peptide were generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   13. APC-multimerisation domain coupled with HLA-B*0702 in         complex with beta2microglobulin and the peptide RPPIFIRRL         derived from EBNA 3A.     -   14. APC-multimerisation domain coupled with HLA-B*0702 in         complex with beta2microglobulin and the peptide QPRAPIRPI         derived from EBNA 6.     -   15. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the HIV peptide TPGPGVRYPL.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of EBV specific T cells in the blood from EBV infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with EBV infection is isolated and 100 ul of this blood is incubated with either of the MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC multimers 7 or 8 described above and thereby the presence of EBV specific T cells will indicate that the patient are infected with Epstein-Barr virus. Blood analysed with MHC(peptide)/APC multimer 9 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the EBV specific T cells.

We conclude that the APC-multimerisation domain coupled MHC(peptide) constructs may be used to detect the presence of EBV specific T cells in the blood of patients infected with Epstein-Barr virus.

Example 49

This is an example of how MHC multimers may be used for detection of influenza matrix peptide in blood samples from humans infected with influenza.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow cytometry. The antigen origin is Influenza, thus, immune monitoring of influenza.

The MHC multimer used are MHC complexes coupled to labeled dextran.

MHC multimers carrying influenza specific peptides is in this example used to detect the presence of influenza specific T cells in the blood of patients infected with influenza virus.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from a region in influenza matrix peptide (Flu-MP) or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes were then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain was generated as described elsewhere herein. MHC-peptide complexes were added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contains 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran was 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs were made:

-   -   16. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide GILGFVFTL         derived from Flu-MP.     -   17. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the non-sense peptide         GLAGDVSAV.

The binding of the above described MHC(peptide)/APC dextran was used to determine the presence of influenza specific T cells in the blood from influenza infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a influenza infected patient is isolated and 100 ul of this blood is incubated with 10 μl of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako), and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continues for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC dextran construct 1 described above and thereby the presence of influenza specific T cells indicate that the patient are infected with influenza virus. Blood analysed with MHC(peptide)/APC dextran construct 2 show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the influenza specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of influenza specific T cells in the blood of patients infected with influenza virus.

Example 50

This is an example of how MHC multimers may be used for detection of influenza matrix peptide in blood samples from humans infected with influenza.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow cytometry. The antigen origin is Influenza, thus, immune monitoring of influenza.

The MHC multimer used are MHC complexes coupled to labeled dextran.

MHC multimers carrying influenza specific peptides is in this example used to detect the presence of influenza specific T cells in the blood of patients infected with influenza virus.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from a region in influenza matrix peptide (Flu-MP) or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes were added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes were purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   18. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide GILGFVFTL derived from         Flu-MP.     -   19. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the non-sense peptide GLAGDVSAV.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of influenza specific T cells in the blood from influenza infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a cancer patient is isolated and 100 ul of this blood is incubated with either of the SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the SA-MHC(peptide)/APC tetramers 3 described above and thereby the presence of influenza specific T cells will indicate that the patient are infected with influenza virus. Blood analysed with SA-MHC(peptide)/APC tetramers 4 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the influenza specific T cells.

We conclude that the APC-SA coupled MHC(peptide) constructs may be used to detect the presence of influenza specific T cells in the blood of patients infected with influenza virus.

Example 51

This is an example of how MHC multimers may be used for detection of influenza matrix peptide in blood samples from humans infected with influenza.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is Influenza, thus, immune monitoring of influenza.

The MHC multimer used are MHC complexes coupled to labeled dextran.

MHC multimers carrying influenza specific peptides is in this example used to detect the presence of influenza specific T cells in the blood of patients infected with influenza virus.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived a region in influenza matrix peptide (Flu-MP) or a negative control peptide were generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   20. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide GILGFVFTL         derived from Flu-MP.     -   21. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the non-sense peptide         GLAGDVSAV.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of influenza specific T cells in the blood from influenza infected by flow cytometry following a standard flow cytometry protocol.

Blood from a influenza infected patient is isolated and 100 ul of this blood is incubated with either of the MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC multimers 5 described above and thereby the presence of influenza specific T cells will indicate that the patient are infected with influenza virus. Blood analysed with MHC(peptide)/APC multimer 6 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the influenza specific T cells.

We conclude that the APC-multimerisation domain coupled MHC(peptide) constructs may be used to detect the presence of influenza specific T cells in the blood of patients infected with influenza virus.

Example 52

This is an example of how MHC multimers may be used for detection of Multiple sclerosis (MS) specific T cells in blood samples from MS patients.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow Cytometry. The antigen origin is MS, thus, immune monitoring of MS.

MHC multimers carrying MS specific peptides is in this example used to detect the presence of MS specific T cells in the blood of MS patients.

Purified MHC-peptide complexes consisting of HLA-DR2 heavy chains and peptide derived from a region in Myelin Basic Protein (MBP) in MS or a negative control peptide are generated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain was generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contains 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran was 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs are made:

-   -   22. APC-SA conjugated 270 kDa dextran coupled with HLA-DR2 in         complex with the peptide MBP 83-102 YDENPVVHFF KNIVTPRTPP         derived from Multiple sclerosis.     -   23. APC-SA conjugated 270 kDa dextran coupled with HLA-DR2 in         complex with the peptide MBP 144-163 VDAQGTLSKIFKLGGRDSRS         derived from Multiple sclerosis.     -   24. APC-SA conjugated 270 kDa dextran coupled with HLA-DR2 in         complex with a non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran was used to determine the presence of MS specific T cells in the blood from MS patients by flow cytometry following a standard flow cytometry protocol.

Blood from a MS patient is isolated and 100 ul of this blood is incubated with 10 μl of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako), and mouse-anti-human CD4/PE (clone MT310 from Dako) are added and the incubation continues for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD4/PE and either of the MHC(peptide)/APC dextran construct 1 or 2 described above and thereby the presence of MS specific T cells in the blood. Blood analysed with MHC(peptide)/APC dextran construct 3 show no staining of CD3 and CD4 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the MS specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of MS specific T cells in the blood of MS patients.

Example 53

This is an example of how MHC multimers may be used for detection of Multiple sclerosis (MS) specific T cells in blood samples from MS patients.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled multimerisation domain Streptavidin (SA, used for direct detection of TCR in flow Cytometry. The antigen origin is MS, thus, immune monitoring of MS.

MHC multimers carrying MS specific peptides is in this example used to detect the presence of MS specific T cells in the blood of MS patients.

Purified MHC-peptide complexes consisting of HLA-DR2 heavy chains and peptide derived from a region in Myelin Basic Protein (MBP) in MS or a negative control peptide are generated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes are added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes are purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   25. APC-SA coupled with HLA-DR2 in complex with the peptide MBP         83-102 YDENPVVHFFKNIVTPRTPP derived from Multiple sclerosis.     -   26. APC-SA coupled with HLA-DR2 in complex with the peptide MBP         144-163 VDAQGTLSKIFKLGGRDSRS derived from Multiple sclerosis.     -   27. APC-SA coupled with HLA-DR2 in complex with a non-sense         peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of MS specific T cells in the blood from MS patients by flow cytometry following a standard flow cytometry protocol.

Blood from a MS patient is isolated and 100 ul of this blood is incubated with either of the SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD4/PE (clone MT310 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD4/PE and either of the SA-MHC(peptide)/APC tetramers 4 or 5 described above and thereby the presence of MS specific T cells in the blood. Blood analysed with SA-MHC(peptide)/APC tetramers 6 should show no staining of CD3 and CD4 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the MS specific T cells.

We conclude that the APC-SA coupled MHC(peptide) constructs may be used to detect the presence of MS specific T cells in the blood of MS patients.

Example 54

This is an example of how MHC multimers may be used for detection of Multiple sclerosis (MS) specific T cells in blood samples from MS patients.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow Cytometry. The antigen origin is MS, thus, immune monitoring of MS.

MHC multimers carrying MS specific peptides is in this example used to detect the presence of MS specific T cells in the blood of MS patients.

Purified MHC-peptide complexes consisting of HLA-DR2 heavy chains and peptide derived from a region in Myelin Basic Protein (MBP) in MS or a negative control peptide are generated. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   28. APC-multimerisation domain coupled with HLA-DR2 in complex         with the peptide MBP 83-102 YDENPVVHFFKNIVTPRTPP derived from         Multiple sclerosis.     -   29. APC-multimerisation domain coupled with HLA-DR2 in complex         with the peptide MBP 144-163 VDAQGTLSKIFKLGGRDSRS derived from         Multiple sclerosis.     -   30. APC-multimerisation domain coupled with HLA-DR2 in complex         with a non-sense peptide.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of MS specific T cells in the blood from MS patients by flow cytometry following a standard flow cytometry protocol.

Blood from a MS patient is isolated and 100 ul of this blood is incubated with either of the MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD4/PE (clone MT310 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD4/PE and either of the MHC(peptide)/APC multimers 7 or 8 described above and thereby the presence of MS specific T cells in the blood. Blood analysed with MHC(peptide)/APC multimer 9 should show no staining of CD3 and CD4 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the MS specific T cells.

We conclude that the APC-multimerisation domain coupled MHC(peptide) constructs may be used to detect the presence of MS specific T cells in the blood of MS patients.

Example 55

This is an example of how MHC multimers may be used for detection of Rheumatoid arthritis (RA) specific T cells in blood samples from RA patients.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow cytometry. The antigen origin is RA, thus, immune monitoring of RA.

MHC multimers carrying RA specific peptides is in this example used to detect the presence of RA specific T cells in the blood of MS patients.

Purified MHC-peptide complexes consisting of HLA-DR4 heavy chains and peptide derived from a region in Collagen Type II (CII) in RA or a negative control peptide are generated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain was generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contains 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran was 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs are made:

-   -   31. APC-SA conjugated 270 kDa dextran coupled with HLA-DR4 in         complex with the peptide CII 261-273 AGFKGEQGPKGEP derived from         Rheumatoid arthritis     -   32. APC-SA conjugated 270 kDa dextran coupled with HLA-DR4 in         complex with a non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran was used to determine the presence of RA specific T cells in the blood from RA patients by flow cytometry following a standard flow cytometry protocol.

Blood from a RA patient is isolated and 100 ul of this blood is incubated with 10 μl of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako), and mouse-anti-human CD4/PE (clone MT310 from Dako) are added and the incubation continues for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD4/PE and the MHC(peptide)/APC dextran construct 1 described above and thereby the presence of RA specific T cells in the blood. Blood analysed with MHC(peptide)/APC dextran construct 2 show no staining of CD3 and CD4 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the RA specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of RA specific T cells in the blood of RA patients.

Example 56

This is an example of how MHC multimers may be used for detection of Rheumatoid arthritis (RA) specific T cells in blood samples from RA patients In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow cytometry. The antigen origin is RA, thus, immune monitoring of RA.

MHC multimers carrying RA specific peptides is in this example used to detect the presence of RA specific T cells in the blood of RA patients.

Purified MHC-peptide complexes consisting of HLA-DR4 heavy chains and peptide derived from a region in Collagen type II (CII) in RA or a negative control peptide are generated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes are added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes are purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   33. APC-SA coupled with HLA-DR4 in complex with the peptide CII         261-273 AGFKGEQGPKGEP derived from Rheumatoid arthritis.     -   34. APC-SA coupled with HLA-DR4 in complex with a non-sense         peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of RA specific T cells in the blood from RA patients by flow cytometry following a standard flow cytometry protocol.

Blood from a RA patient is isolated and 100 ul of this blood is incubated with either of the SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD4/PE (clone MT310 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD4/PE and the SA-MHC(peptide)/APC tetramers 3 described above and thereby the presence of RA specific T cells in the blood. Blood analysed with SA-MHC(peptide)/APC tetramers 4 should show no staining of CD3 and CD4 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the RA specific T cells.

We conclude that the APC-SA coupled MHC(peptide) constructs may be used to detect the presence of RA specific T cells in the blood of RA patients.

Example 57

This is an example of how MHC multimers may be used for detection of Rheumatoid arthritis (RA) specific T cells in blood samples from RA patients.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is RA, thus, immune monitoring of RA. MHC multimers carrying RA specific peptides is in this example used to detect the presence of RA specific T cells in the blood of MS patients.

This is an example of how MHC multimers may be used for detection of Rheumatoid arthritis (RA) specific T cells in blood samples from RA patients. The MHC multimer used are MHC complexes coupled to

MHC multimers carrying RA specific peptides is in this example used to detect the presence of RA specific T cells in the blood of RA patients.

Purified MHC-peptide complexes consisting of HLA-DR4 heavy chains and peptide derived from a region in Myelin Basic Protein (MBP) in MS or a negative control peptide are generated. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   35. APC-multimerisation domain coupled with HLA-DR4 in complex         with the peptide CII 261-273 AGFKGEQGPKGEP derived from         Rheumatoid arthritis.     -   36. APC-multimerisation domain coupled with HLA-DR4 in complex         with a non-sense peptide.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of RA specific T cells in the blood from RA patients by flow cytometry following a standard flow cytometry protocol.

Blood from a RA patient is isolated and 100 ul of this blood is incubated with either of the MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD4/PE (clone MT310 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD4/PE and the MHC(peptide)/APC multimers 5 described above and thereby the presence of RA specific T cells in the blood. Blood analysed with MHC(peptide)/APC multimer 6 should show no staining of CD3 and CD4 positive cells with this SA-MHC(peptide)/APC multimers.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the RA specific T cells.

We conclude that the APC-multimerisation domain coupled MHC(peptide) constructs may be used to detect the presence of RA specific T cells in the blood of RA patients.

Example 58

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB.

TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from regions in Mycobacterium tuberculosis Antigen 85B (Ag85B) or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain is generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contained 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran was 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs are made:

-   -   37. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide KLVANNTRL         derived from Ag85B.     -   38. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide YLLDGLRAQ         derived from Ag85B.     -   39. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide FLTSELPQW         derived from Ag85B.     -   40. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the non-sense peptide         GLAGDVSAV.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Ag85B specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with 10 μl of one of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC dextran constructs 1, 2 or 3 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with MHC(peptide)/APC dextran construct 4 should show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 59

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled the multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB.

TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from regions in Mycobacterium tuberculosis Antigen 85B (Ag85B) or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes were added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes were purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   41. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide KLVANNTRL derived from Ag85B.     -   42. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide YLLDGLRAQ derived from Ag85B.     -   43. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide FLTSELPQW derived from Ag85B.     -   44. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the non-sense peptide GLAGDVSAV

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Ag85B specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with either of the four SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the SA-MHC(peptide)/APC tetramers 5, 6 or 7 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with SA-MHC(peptide)/APC tetramers 8 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 60

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB. TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis. The MHC multimer used are MHC complexes coupled to

TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from regions in Mycobacterium tuberculosis Antigen 85B (Ag85B) or a negative control peptide are generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   45. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide KLVANNTRL         derived from Ag85B.     -   46. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide YLLDGLRAQ         derived from Ag85B.     -   47. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide FLTSELPQW         derived from Ag85B.     -   48. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the non-sense peptide         GLAGDVSAV

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of Ag85B specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with either of the four MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC multimers 9, 10 or 11 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with MHC(peptide)/APC multimer 12 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 61

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB.

TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-B*0801 heavy chain, human beta2microglobulin and peptide derived from regions in Mycobacterium tuberculosis Antigen 85B (Ag85B) or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain is generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contained 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran was 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs are made:

-   -   49. APC-SA conjugated 270 kDa dextran coupled with HLA-B*0801 in         complex with beta2microglobulin and the peptide MGRDIKVQF         derived from Ag85B.     -   50. APC-SA conjugated 270 kDa dextran coupled with HLA-B*0801 in         complex with beta2microglobulin and the peptide DIKVQFQSG         derived from Ag85B.     -   51. APC-SA conjugated 270 kDa dextran coupled with HLA-B*0801 in         complex with beta2microglobulin and the peptide ENFVRSSNL         derived from Ag85B.     -   52. APC-SA conjugated 270 kDa dextran coupled with HLA-B*0801 in         complex with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Ag85B specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with 10 μl of one of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC dextran constructs 13, 14 or 15 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with MHC(peptide)/APC dextran construct 16 should show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 62

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled the multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB.

TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from regions in Mycobacterium tuberculosis Antigen 85B (Ag85B) or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes were added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes were purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   53. APC-SA coupled with HLA-B*0801 in complex with         beta2microglobulin and the peptide MGRDIKVQF derived from Ag85B.     -   54. APC-SA coupled with HLA-B*0801 in complex with         beta2microglobulin and the peptide DIKVQFQSG derived from Ag85B.     -   55. APC-SA coupled with HLA-B*0801 in complex with         beta2microglobulin and the peptide ENFVRSSNL derived from Ag85B.     -   56. APC-SA coupled with HLA-B*0801 in complex with         beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Ag85B specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with either of the four SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the SA-MHC(peptide)/APC tetramers 17, 18 or 19 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with SA-MHC(peptide)/APC tetramers 20 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 63

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB. TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-B*0801 heavy chain, human beta2microglobulin and peptide derived from regions in Mycobacterium tuberculosis Antigen 85B (Ag85B) or a negative control peptide are generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   57. APC-multimerisation domain coupled with HLA-B*0801 in         complex with beta2microglobulin and the peptide MGRDIKVQF         derived from Ag85B.     -   58. APC-multimerisation domain coupled with HLA-B*0801 in         complex with beta2microglobulin and the peptide DIKVQFQSG         derived from Ag85B.     -   59. APC-multimerisation domain coupled with HLA-B*0801 in         complex with beta2microglobulin and the peptide ENFVRSSNL         derived from Ag85B.     -   60. APC-multimerisation domain coupled with HLA-B*0801 in         complex with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of Ag85B specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with either of the four MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC multimers 21, 22 or 23 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with MHC(peptide)/APC multimer 24 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 64

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB.

TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-B*44 heavy chain, human beta2microglobulin and peptide derived from regions in antigen Mtb39 or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain is generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contained 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran was 3.8×10e-8 M.

The following MHC(peptide)/APC dextran constructs are made:

-   -   61. APC-SA conjugated 270 kDa dextran coupled with HLA-B*44 in         complex with beta2microglobulin and the peptide MWAQDAAAMF         derived from Mtb39.     -   62. APC-SA conjugated 270 kDa dextran coupled with HLA-B*44 in         complex with beta2microglobulin and the peptide AAERGPGQML         derived from Mtb39.     -   63. APC-SA conjugated 270 kDa dextran coupled with HLA-B*44 in         complex with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Mtb39 specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with 10 μl of one of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC dextran constructs 25 or 26 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with MHC(peptide)/APC dextran construct 27 should show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 65

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled the multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB.

TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-B*44 heavy chain, human beta2microglobulin and peptide derived from regions in antigen Mtb39 or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes are added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes are purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   64. APC-SA coupled with HLA-B*44 in complex with         beta2microglobulin and the peptide MWAQDAAAMF derived from         Ag85B.     -   65. APC-SA coupled with HLA-B*44 in complex with         beta2microglobulin and the peptide AAERGPGQML derived from         Ag85B.     -   66. APC-SA coupled with HLA-B*44 in complex with         beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Mtb39 specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with either of the four SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the SA-MHC(peptide)/APC tetramers 28 or 29 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with SA-MHC(peptide)/APC tetramers 30 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 66

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB. TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-B*44 heavy chain, human beta2microglobulin and peptide derived from regions in antigen Mtb39 or a negative control peptide are generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   67. APC-multimerisation domain coupled with HLA-B*44 in complex         with beta2microglobulin and the peptide MWAQDAAAMF derived from         Mtb39.     -   68. APC-multimerisation domain coupled with HLA-B*44 in complex         with beta2microglobulin and the peptide AAERGPGQML derived from         Mtb39.     -   69. APC-multimerisation domain coupled with HLA-B*44 in complex         with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of Mtb39 specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with either of the four MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC multimers 31 or 32 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with MHC(peptide)/APC multimer 33 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 67

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB.

TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-B*14 heavy chain, human beta2microglobulin and peptide derived from regions in culture filtrate protein 10 (CFP10) antigen (Table Y) or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain is generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contained 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran was 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs are made:

-   -   70. APC-SA conjugated 270 kDa dextran coupled with HLA-B*14 in         complex with beta2microglobulin and the peptide RADEEQQQAL         derived from CFP10.     -   71. APC-SA conjugated 270 kDa dextran coupled with HLA-B*14 in         complex with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of CFP10 specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with 10 μl of one of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC dextran constructs 34 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with MHC(peptide)/APC dextran construct 25 should show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 68

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled the multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB.

TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-B*14 heavy chain, human beta2microglobulin and peptide derived from regions in culture filtrate protein 10 (CFP10) antigen (Table Y) or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes are added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes are purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   72. APC-SA coupled with HLA-B*14 in complex with         beta2microglobulin and the peptide RADEEQQQAL derived from         CFP10.     -   73. APC-SA coupled with HLA-B*44 in complex with         beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of CFP10 specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with either of the four SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the SA-MHC(peptide)/APC tetramers 36 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with SA-MHC(peptide)/APC tetramers 37 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 69

This is an example of how MHC multimers may be used for diagnosis of Tuberculosis (TB) in blood samples from humans infected with Mycobacterium tuberculosis.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is TB, thus, immune monitoring of TB. TB is caused by infection by Mycobacterium tuberculosis. During acute infection TB specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated TB specific T cells may thereby act as a surrogate marker for infection with Mycobacterium tuberculosis. MHC multimers carrying TB specific peptides is in this example used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Purified MHC-peptide complexes consisting of HLA-B*14 heavy chain, human beta2microglobulin and peptide derived from regions in culture filtrate protein 10 (CFP10) antigen (Table Y) or a negative control peptide are generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   74. APC-multimerisation domain coupled with HLA-B*14 in complex         with beta2microglobulin and the peptide RADEEQQQAL derived from         CFP10.     -   75. APC-multimerisation domain coupled with HLA-B*14 in complex         with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of CFP10 specific T cells in the blood from TB infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with TB is isolated and 100 ul of this blood is incubated with either of the four MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC multimers 38 described above and thereby the presence of TB specific T cells will indicate that the patient are infected with Mycobacterium tuberculosis. Blood analysed with MHC(peptide)/APC multimer 39 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the TB specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of TB specific T cells in the blood of patients infected with Mycobacterium tuberculosis.

Example 70

This is an example of how MHC multimers may be used for diagnosis of Lyme Disease in blood samples from humans infected with Borrelia bacteria.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow Cytometry. The antigen origin is Borrelia, thus, immune monitoring of a Borrelia infection.

Lyme disease is caused by infection by Borrelia bacteria. During acute infection Borrelia specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated Borrelia specific T cells may thereby act as a surrogate marker for infection with Borrelia bacterium. MHC multimers carrying borrelia specific peptides is in this example used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from regions in Outer surface protein A (Table V) or Flagellin B (Table X) conserved among the three species Borrelia Burgdorferi, Borrelia Garinii and Borrelia Afzelii or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain is generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contains 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran is 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs are made:

-   -   76. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide ALIACKQNV         derived from OspA.     -   77. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide FTKEDTIT derived         from OspA.     -   78. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide SIQIEIEQL         derived from Fla B     -   79. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide NLNEVEKVL         derived from Fla B     -   80. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide SLAKIENAI         derived from Fla B     -   81. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201 in         complex with beta2microglobulin and the non-sense peptide         GLAGDVSAV

The binding of the above described MHC(peptide)/APC dextran is used to determine the presence of Osp A or Fla B specific T cells in the blood from Borrelia infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with Lyme disease is isolated and 100 ul of this blood is incubated with 10 μl of each of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako), mouse-anti-human CD4/FITC (clone MT310 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continues for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 300×g and the supernatant removed. The washing step is repeated twice. The washed cells are resuspended in 400-500 μl PBS+1% BSA; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC dextran constructs 1, 2, 3, 4 and 5 described above and thereby the presence of Borrelia specific T cells indicate that the patient are infected with Borrelia bacteria. Blood analysed with MHC(peptide)/APC dextran construct 6 show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The result is shown in FIG. 19.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the Borrelia specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Example 71

This is an example of how MHC multimers may be used for diagnosis of Lyme Disease in blood samples from humans infected with Borrelia bacteria.

In this example the MHC multimer used are MHC complexes coupled to the fluorophor-labelled multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow Cytometry. The antigen origin is Borrelia, thus, immune monitoring of a Borrelia infection. Lyme disease is caused by infection by Borrelia bacteria. During acute infection Borrelia specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated Borrelia specific T cells may thereby act as a surrogate marker for infection with Borrelia bacterium. MHC multimers carrying borrelia specific peptides is in this example used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from regions in Outer surface protein A (Table V) or Flagellin B (Table X) conserved among the three species Borrelia Burgdorferi, Borrelia Garinii and Borrelia Afzelii or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes were added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes were purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   82. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide ALIACKQNV derived from OspA.     -   83. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide FTKEDTIT derived from OspA.     -   84. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide SIQIEIEQL derived from Fla B.     -   85. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide NLNEVEKVL derived from Fla B.     -   86. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide SLAKIENAI derived from Fla B.     -   87. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the non-sense peptide GLAGDVSAV

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Osp A or Fla B specific T cells in the blood from Borrelia infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with Lyme disease is isolated and 100 ul of this blood is incubated with either of the four SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the SA-MHC(peptide)/APC tetramers 7, 8, 9, 10 or 11 described above and thereby the presence of Borrelia specific T cells will indicate that the patient are infected with Borrelia bacteria. Blood analysed with SA-MHC(peptide)/APC tetramers 12 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the Borrelia specific T cells.

We conclude that the APC-SA coupled MHC(peptide) constructs may be used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Example 72

This is an example of how MHC multimers may be used for diagnosis of Lyme Disease in blood samples from humans infected with Borrelia bacteria.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is Borrelia, thus, immune monitoring of a Borrelia infection.

Lyme disease is caused by infection by Borrelia bacteria. During acute infection Borrelia specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated Borrelia specific T cells may thereby act as a surrogate marker for infection with Borrelia bacterium. MHC multimers carrying borrelia specific peptides is in this example used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from regions in Outer surface protein A (Table V) or Flagellin B (Table X) conserved among the three species Borrelia Burgdorferi, Borrelia Garinii and Borrelia Afzelii or a negative control peptide were generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   88. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide ALIACKQNV         derived from OspA.     -   89. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide FTKEDTIT derived         from OspA.     -   90. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide SIQIEIEQL         derived from Fla B.     -   91. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide NLNEVEKVL         derived from Fla B.     -   92. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide SLAKIENAI         derived from Fla B.     -   93. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the non-sense peptide         GLAGDVSAV

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of Osp A or Fla B specific T cells in the blood from Borrelia infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with Lyme disease is isolated and 100 ul of this blood is incubated with either of the four MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC multimers 13, 14, 15, 16 or 17 described above and thereby the presence of Borrelia specific T cells will indicate that the patient are infected with Borrelia bacteria.

Blood analysed with MHC(peptide)/APC multimer 18 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the Borrelia specific T cells.

We conclude that the APC-multimerisation domain coupled MHC(peptide) constructs may be used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Example 73

This is an example of how MHC multimers may be used for diagnosis of Lyme Disease in blood samples from humans infected with Borrelia bacteria.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow Cytometry. The antigen origin is Borrelia, thus, immune monitoring of a Borrelia infection.

Lyme disease is caused by infection by Borrelia bacteria. During acute infection Borrelia specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated Borrelia specific T cells may thereby act as a surrogate marker for infection with Borrelia bacterium. MHC multimers carrying borrelia specific peptides is in this example used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Purified MHC-peptide complexes consisting of HLA-A*0301 heavy chain, human beta2microglobulin and peptide derived from regions in Outer surface protein C (Table U) conserved among the three species Borrelia Burgdorferi, Borrelia Garinii and Borrelia Afzelii or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes were then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain was generated as described elsewhere herein. MHC-peptide complexes were added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contained 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran was 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs were made:

-   -   94. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0301 in         complex with beta2microglobulin and the peptide TLITEKLSK         derived from OspC.     -   95. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0301 in         complex with beta2microglobulin and the peptide ELANKAIGK         derived from OspC.     -   96. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0301 in         complex with beta2microglobulin and the HIV peptide QVPLRPMTYK.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Osp C specific T cells in the blood from Borrelia infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with Lyme disease is isolated and 100 ul of this blood is incubated with 10 μl of one of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC dextran constructs 19 or 20 described above and thereby the presence of Borrelia specific T cells will indicate that the patient are infected with Borrelia bacteria. Blood analysed with MHC(peptide)/APC dextran construct 21 should show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the Borrelia specific T cells.

We conclude that the APC-SA conjugated 270 kDa dextran coupled MHC(peptide) constructs may be used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Example 74

This is an example of how MHC multimers may be used for diagnosis of Lyme Disease in blood samples from humans infected with Borrelia bacteria.

In this example the MHC multimer used are MHC complexes coupled to the fluorophor-labelled multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow Cytometry. The antigen origin is Borrelia, thus, immune monitoring of a Borrelia infection. Lyme disease is caused by infection by Borrelia bacteria. During acute infection Borrelia specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated Borrelia specific T cells may thereby act as a surrogate marker for infection with Borrelia bacterium. MHC multimers carrying borrelia specific peptides is in this example used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Purified MHC-peptide complexes consisting of HLA-A*0301 heavy chain, human beta2microglobulin and peptide derived from regions in Outer surface protein C (Table U) conserved among the three species Borrelia Burgdorferi, Borrelia Garinii and Borrelia Afzelii or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes were added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes were purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   97. APC-SA coupled with HLA-A*0301 in complex with         beta2microglobulin and the peptide TLITEKLSK derived from OspC.     -   98. APC-SA coupled with HLA-A*0301 in complex with         beta2microglobulin and the peptide ELANKAIGK derived from OspC.     -   99. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the HIV peptide QVPLRPMTYK.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of Osp C specific T cells in the blood from Borrelia infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with Lyme disease is isolated and 100 ul of this blood is incubated with either of the four SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the SA-MHC(peptide)/APC tetramers 22 or 23 described above and thereby the presence of Borrelia specific T cells will indicate that the patient are infected with Borrelia bacteria. Blood analysed with SA-MHC(peptide)/APC tetramers 24 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the Borrelia specific T cells.

We conclude that the APC-SA coupled MHC(peptide) constructs may be used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Example 75

This is an example of how MHC multimers may be used for diagnosis of Lyme Disease in blood samples from humans infected with Borrelia bacteria.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is Borrelia, thus, immune monitoring of a Borrelia infection.

Lyme disease is caused by infection by Borrelia bacteria. During acute infection Borrelia specific activated T cells will be present in increased amounts in an activated state compared to healthy individuals. The presences of an increased amount of activated Borrelia specific T cells may thereby act as a surrogate marker for infection with Borrelia bacterium. MHC multimers carrying borrelia specific peptides is in this example used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from regions in Outer surface protein C (Table U) conserved among the three species Borrelia Burgdorferi, Borrelia Garinii and Borrelia Afzelii or a negative control peptide were generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   100. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide TLITEKLSK         derived from OspC.     -   101. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide ELANKAIG derived         from OspC.     -   102. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the HIV peptide QVPLRPMTYK.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of Osp C specific T cells in the blood from Borrelia infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with Lyme disease is isolated and 100 ul of this blood is incubated with either of the four MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC multimers 25 or 26 described above and thereby the presence of Borrelia specific T cells will indicate that the patient are infected with Borrelia bacteria. Blood analysed with MHC(peptide)/APC multimer 27 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described diagnostic test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the Borrelia specific T cells.

We conclude that the APC-multimerisation domain coupled MHC(peptide) constructs may be used to detect the presence of Borrelia specific T cells in the blood of patients infected with Borrelia.

Example 76

This is an example of how MHC multimers may be used for detection of Cytomegalovirus (CMV) specific T cells in blood samples from humans infected with CMV.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow cytometry. The antigen origin is CMV, thus, immune monitoring of CMV.

MHC multimers carrying CMV specific peptides is in this example used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from a region in CMV internal matrix protein pp65 or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain is generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contains 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran is 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs are made:

-   -   103. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201         in complex with beta2microglobulin and the peptide NLVPMVATV         derived from CMV pp65.     -   104. APC-SA conjugated 270 kDa dextran coupled with HLA-A*0201         in complex with beta2microglobulin and the non-sense peptide         GLAGDVSAV

The binding of the above described MHC(peptide)/APC dextran is used to determine the presence of CMV pp65 specific T cells in the blood from CMV infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with CMV infection is isolated and 100 ul of this blood is incubated with 10 μl of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako), and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continues for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 300×g and the supernatant removed. The washing step is repeated twice. The washed cells are resuspended in 400-500 μl PBS+1% BSA; pH=7.2 and analyzed on flowcytometer. The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC dextran construct 1 described above and thereby the presence of CMV specific T cells indicate that the patient are infected with Cytomegalovirus. Blood analysed with MHC(peptide)/APC dextran construct 2 show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct. The result is shown I FIG. 20

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the CMV specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Example 77

This is an example of how MHC multimers may be used for detection of Cytomegalovirus (CMV) specific T cells in blood samples from humans infected with CMV.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow cytometry. The antigen origin is CMV, thus, immune monitoring of CMV.

MHC multimers carrying CMV specific peptides is in this example used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived from a region in CMV internal matrix protein pp65 or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes were added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes were purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   105. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the peptide NLVPMVATV derived from CMV         pp65.     -   106. APC-SA coupled with HLA-A*0201 in complex with         beta2microglobulin and the non-sense peptide GLAGDVSAV

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of CMV pp65 specific T cells in the blood from Cytomegalovirus infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with CMV is isolated and 100 ul of this blood is incubated with either of the SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the SA-MHC(peptide)/APC tetramers 3 described above and thereby the presence of CMV specific T cells will indicate that the patient are infected with Cytomegalovirus. Blood analysed with SA-MHC(peptide)/APC tetramers 4 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the CMV specific T cells.

We conclude that the APC-SA coupled MHC(peptide) constructs may be used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Example 78

This is an example of how MHC multimers may be used for detection of Cytomegalovirus (CMV) specific T cells in blood samples from humans infected with CMV.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is CMV, thus, immune monitoring of CMV.

MHC multimers carrying CMV specific peptides is in this example used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Purified MHC-peptide complexes consisting of HLA-A*0201 heavy chain, human beta2microglobulin and peptide derived a region in CMV internal matrix protein pp65 or a negative control peptide were generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   107. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the peptide NLVPMVATV         derived from CMV pp65.     -   108. APC-multimerisation domain coupled with HLA-A*0201 in         complex with beta2microglobulin and the non-sense peptide         GLAGDVSAV.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of CMV pp65 specific T cells in the blood from CMV infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with CMV infection is isolated and 100 ul of this blood is incubated with either of the MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC multimers 5 described above and thereby the presence of CMV specific T cells will indicate that the patient are infected with Cytomegalovirus. Blood analysed with MHC(peptide)/APC multimer 6 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the CMV specific T cells.

We conclude that the APC-multimerisation domain coupled MHC(peptide) constructs may be used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Example 79

This is an example of how MHC multimers may be used for detection of Cytomegalovirus (CMV) specific T cells in blood samples from humans infected with CMV.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled dextran (Dextramers). The dextramers are used for direct detection of TCR in flow cytometry. The antigen origin is CMV, thus, immune monitoring of CMV.

MHC multimers carrying CMV specific peptides is in this example used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Purified MHC-peptide complexes consisting of HLA-A*2402 heavy chain, human beta2microglobulin and peptide derived from a region in CMV internal matrix protein pp65 or a negative control peptide are generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled to a 270 kDa dextran multimerization domain labelled with APC by interaction with streptavidin (SA) on the dextran multimerization domain. The dextran-APC-SA multimerization domain is generated as described elsewhere herein. MHC-peptide complexes are added in an amount corresponding to a ratio of three MHC-peptide molecules per SA molecule and each molecule dextran contains 3.7 SA molecule and 8.95 molecules APC. The final concentration of dextran is 3.8×10e-8 M. The following MHC(peptide)/APC dextran constructs are made:

-   -   109. APC-SA conjugated 270 kDa dextran coupled with HLA-A*2402         in complex with beta2microglobulin and the peptide QYDPVAALF         derived from CMV pp65.     -   110. APC-SA conjugated 270 kDa dextran coupled with HLA-A*2402         in complex with beta2microglobulin and the peptide VYALPLKML         derived from CMV pp65.     -   111. APC-SA conjugated 270 kDa dextran coupled with HLA-A*2402         in complex with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran is used to determine the presence of CMV pp65 specific T cells in the blood from CMV infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with CMV infection is isolated and 100 ul of this blood is incubated with 10 μl of the MHC(peptide)/APC dextran constructs described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako), and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continues for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 300×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS+1% BSA; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and the MHC(peptide)/APC dextran constructs 7 or 8 described above and thereby the presence of CMV specific T cells indicate that the patient are infected with Cytomegalovirus. Blood analysed with MHC(peptide)/APC dextran construct 9 show no staining of CD3 and CD8 positive cells with this MHC(peptide)/APC dextran construct.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the CMV specific T cells.

We conclude that the MHC(peptide)/APC dextran constructs can be used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Example 80

This is an example of how MHC multimers may be used for detection of Cytomegalovirus (CMV) specific T cells in blood samples from humans infected with CMV.

In this example the MHC multimer used are MHC complexes coupled to fluorophor-labelled multimerisation domain Streptavidin (SA), used for direct detection of TCR in flow cytometry.

The antigen origin is CMV, thus, immune monitoring of CMV.

MHC multimers carrying CMV specific peptides is in this example used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Purified MHC-peptide complexes consisting of HLA-A*2402 heavy chain, human beta2microglobulin and peptide derived from a region in CMV internal matrix protein pp65 or a negative control peptide were generated by in vitro refolding, purified and biotinylated as described elsewhere herein. Biotinylated MHC-peptide complexes are then coupled SA labelled with APC. MHC-peptide complexes were added in an amount corresponding to a ratio of 5 MHC-peptide molecules per SA molecule. Then SA/APC carrying four MHC complexes were purified from free SA, free monomeric MHC complex, SA carrying three, two and one MHC complexes.

The following SA-MHC(peptide)/APC tetramers are made:

-   -   112. APC-SA coupled with HLA-A*2402 in complex with         beta2microglobulin and the peptide QYDPVAALF derived from CMV         pp65.     -   113. APC-SA coupled with HLA-A*2402 in complex with         beta2microglobulin and the peptide VYALPLKML derived from CMV         pp65.     -   114. APC-SA coupled with HLA-A*2402 in complex with         beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC dextran can be used to determine the presence of CMV pp65 specific T cells in the blood from Cytomegalovirus infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with CMV is isolated and 100 ul of this blood is incubated with either of the SA-MHC(peptide)/APC tetramers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the SA-MHC(peptide)/APC tetramers 10 or 11 described above and thereby the presence of CMV specific T cells will indicate that the patient are infected with Cytomegalovirus. Blood analysed with SA-MHC(peptide)/APC tetramers 12 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC tetramer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the CMV specific T cells.

We conclude that the APC-SA coupled MHC(peptide) constructs may be used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Example 81

This is an example of how MHC multimers may be used for detection of Cytomegalovirus (CMV) specific T cells in blood samples from humans infected with CMV.

In this example the MHC multimer used are MHC complexes coupled to any fluorophor-labelled multimerisation as described elsewhere herein. The MHC multimers are used for direct detection of TCR in flow cytometry. The antigen origin is CMV, thus, immune monitoring of CMV.

MHC multimers carrying CMV specific peptides is in this example used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Purified MHC-peptide complexes consisting of HLA-A*2402 heavy chain, human beta2microglobulin and peptide derived a region in CMV internal matrix protein pp65 or a negative control peptide were generated by in vitro refolding and purified or purified from antigen presenting cells. MHC-peptide complexes are then coupled to a multimerisation domain together with APC.

The following MHC(peptide)/APC multimers are made:

-   -   115. APC-multimerisation domain coupled with HLA-A*2402 in         complex with beta2microglobulin and the peptide QYDPVAALF         derived from CMV pp65.     -   116. APC-multimerisation domain coupled with HLA-A*2402 in         complex with beta2microglobulin and the peptide VYALPLKML         derived from CMV pp65.     -   117. APC-multimerisation domain coupled with HLA-A*2402 in         complex with beta2microglobulin and the non-sense peptide.

The binding of the above described MHC(peptide)/APC multimers can be used to determine the presence of CMV pp65 specific T cells in the blood from CMV infected individuals by flow cytometry following a standard flow cytometry protocol.

Blood from a patient with CMV infection is isolated and 100 ul of this blood is incubated with either of the MHC(peptide)/APC multimers described above for 10 minutes in the dark at room temperature. 5 μl of each of each of the antibodies mouse-anti-human CD3/PB (clone UCHT1 from Dako) and mouse-anti-human CD8/PE (clone DK25 from Dako) are added and the incubation continued for another 20 minutes at 4° C. in the dark. The samples are then washed by adding 2 ml PBS; pH=7.2 followed by centrifugation for 5 minutes at 200×g and the supernatant removed. The washing step is repeated. The washed cells are resuspended in 400-500 μl PBS; pH=7.2 and analyzed on flowcytometer.

The presence of cells labeled with anti-CD3/PB, anti-CD8/PE and either of the MHC(peptide)/APC multimers 13 or 14 described above and thereby the presence of CMV specific T cells will indicate that the patient are infected with Cytomegalovirus. Blood analysed with MHC(peptide)/APC multimer 15 should show no staining of CD3 and CD8 positive cells with this SA-MHC(peptide)/APC multimer.

The sensitivity of the above described test may be enhanced by addition of labeled antibodies specific for activation markers expressed in or on the surface of the CMV specific T cells.

We conclude that the APC-multimerisation domain coupled MHC(peptide) constructs may be used to detect the presence of CMV specific T cells in the blood of patients infected with Cytomegalovirus.

Example 82

This is an example of measurement of antigen reactive T-Cells by IFN-γ capture in blood samples by ELISPOT.

This is an example of indirect detection of TCR, where individual cells are immobilized and measured by a chromogen assay.

The example provides a sensitive assay for the detection of T-cells reactive to an antigen by detecting a soluble factor whose secretion is induced by stimulation of the T-cell by the antigen.

A summary flow chart of the method is shown in FIG. 20. In brief, peripheral blood is diluted threefold in Dulbecco's phosphate buffered saline (DPBS), underlain with 15 ml of Ficoll (Pharmacia Ficoll-Paque #17-0840-02, Piscataway, N.J.) per 40 ml diluted blood in a 50 ml polypropylene centrifuge tube, and spun at 2000 RPM for 20 minutes in a Beckman CS-6R centrifuge (Beckman Inc., Palo Alto, Calif.). The buffy layer at the DPBS/Ficoll interface is removed, washed twice with DPBS and once with human tissue culture medium (hTCM: αMEM+5% heat inactivated human AB serum (Ultraserum, BioWhittaker, Walkersville, Md.), penicillin/streptomycin, 1-glutamine) at low RCF to remove platelets. Sixty percent of the PBMCs are resuspended in freezing medium (10% dimethyl sulfoxide (Sigma Chemical Co., St. Louis, Mo.), 90% fetal bovine serum to a concentration of 5×10⁶ cells/ml, frozen in a programmable Cryo-Med (New Baltimore, Mich.) cell freezer, and stored under liquid nitrogen until needed.

The purified PBMCs are plated at 2×10⁵ cells/well at a volume of 0.1 ml in 96 well Costar cell culture plates. An equal volume of antigen at 10 μg/ml is added to triplicate or sextuplet sets of wells and the plate is incubated in a 37° C., 5% CO₂ incubator. On day five, 10 μl/well of 100 U/ml stock recombinant IL-2 (Advanced Biotechnologies Inc., Columbia, Md.) is added to each well. On day 8, frozen PBMCs are thawed, washed in DPBS+0.5% bovine serum albumin (BSA) to remove DMSO, resuspended to a concentration of 4×10⁶ cells/ml in hTCM, and γ-irradiated (3,000 RADS). Fifty microliters/well are dispensed along with 50 μl of the appropriate antigen at a stock concentration of 40 μl/ml to give a final antigen concentration of 10 μg/ml.

To prepare a capture plate, IFN-γ capture antibody (monoclonal mouse anti-human IFN-g, Endogen #M700A, Cambridge, Mass.) is diluted to 10 μg/ml in sterile 0.1 M Na(CO₃)₂ pH 8.2 buffer, aliquotted at 50 μl/well in flat bottomed 96 well sterile microtiter plates (Corning Costar Corp.), and incubated at 4° C. for a minimum of 24 hours. Prior to use, excess antibody is removed and wells are washed twice with dPBS+1% Tween 20 (PBST). To block further nonspecific protein binding, plates are incubated with 250 μl/well of PBS+5% BSA at room temperature for 1 hour. After discarding the blocking solution, wells are washed once with PBST (0.1% Tween), followed by hTCM in preparation for the antigen stimulated cells.

On day 9 of the assay, twenty four hours after the second antigen stimulation, the stimulation plate is spun for 5 minutes at 1500 RPM in a Beckman CS-6R centrifuge and 90 μl of supernatant is carefully removed from each well with a micropipette. The pelleted cells are resuspended in 100 μl of hTCM, pooled in sterile tubes (Corning Costar corp sterile ClusterTAb #4411, Cambridge, Mass.), mixed and transferred into an equal number of wells of an anti IFN-γ capture plate. Capture plates are incubated undisturbed at 37° C. for 16-20 hours. At the end of the IFN-γ secretion phase, the cells are discarded and the plates are washed three times with 0.1% PBST. A final aliquot of PBST is added to the wells for ten minutes, removed, and 100 μl of a 1:500 dilution of rabbit anti-human IFN-γ polyclonal antibody (Endogen #P700, Cambridge, Mass.) in PBST+1% BSA is added to each well for 3.5 hours at room temperature with gentle rocking. Unbound anti-IFN-γ polyclonal antibody is removed by three washes with PBST, followed by a wash with 250 μl of 1×Tris-buffered saline+0.05% Tween 20 (TBST). Next, a 100 μl aliquot of 1:5000 alkaline phosphatase-conjugated mouse anti-rabbit polyclonal antibody (Jackson Immunological #211-055-109, West Grove, Pa.) diluted in TBST is added to each well and incubated at room temperature for 1.5-2 hours with gentle rocking. Excess enzyme-conjugated antibody is removed by three washes with PBST and two washes with alkaline phosphatase buffer (APB=0.1 M NaCl, 0.05 M MgCl.sub.2, 0.1 M Tris HCl, pH 9.5) followed by addition of the substrate mix of p-Toluidine salt and nitroblue tetrazolium chloride (BCIP/NBT, GIBCO BRL #18280-016, Gaithersburg, Md.). To stop the calorimetric reaction, plates were washed three times in dH₂O, inverted to minimize deposition of dust in the wells, and dried overnight at 28° C. in a dust free drying oven.

Images of the spots corresponding to the lymphokine secreted by individual antigen-stimulated T cells are captured with a CCD video camera and the image is analyzed by NIH image software. Captured images are enhanced using the Look Up Table which contrasts the images. Thresholding is then applied to every image and a wand tool is used to highlight the border to effectively subtract the edge of the well so that background counts won't be high and artificial. Density slicing over a narrow range is then used to highlight the spots produced from secreting cells. Pixel limits are set to subtract out small debris and large particles, and the number of spots falling within the prescribed pixel range are counted by the software program. Totals from each well are then manually recorded for future analysis. Alternatively, spots can be counted by other commercially available or customized software applications, or may be quantitated manually by a technician using standard light microscopy. Spots can also be counted manually under a light microscope.

We conclude that the protocol detailed above can be used for the enumeration of single IFN-γ secreting T cells.

Example 83

This is an example of measurement of antigen reactive T-Cells by IFN-γ capture in blood samples from Multiple Sclerosis (MS) patients by ELISPOT.

This is an example of indirect detection of TCR, where individual cells are immobilized and measured by a chromogen assay. The antigenic peptide origin is MS, thus, immune monitoring of MS.

The example provides a sensitive assay for the detection of T-cells reactive to the antigen Myelin Basic Protein (MBP), by detecting a soluble factor whose secretion is induced by stimulation of the T-cell by the antigen.

This example is similar to the experiment above. PBMCs from Multiple Sclerosis patients are isolated, prepared and stored as described in the example above.

The purified PBMCs are plated at 2×10⁵ cells/well at a volume of 0.1 ml in 96 well Costar cell culture plates. An equal volume of antigen, MBP 83-102 (YDENPVVHFF KNIVTPRTPP) or 144-163 (VDAQGTLSKIFKLGGRDSRS), at 10 μg/ml is added to triplicate or sextuplet sets of wells and the plate is incubated in a 37° C., 5% CO₂ incubator. On day five, 10 μl/well of 100 U/ml stock recombinant IL-2 is added to each well. On day 8, frozen PBMCs are thawed, washed in DPBS+0.5% BSA to remove DMSO, resuspended to a concentration of 4×10⁶ cells/ml in hTCM, and γ-irradiated (3,000 RADS). 50 μl/well are dispensed along with 50 μl of the appropriate antigen at a stock concentration of 40 μl/ml to give a final antigen concentration of 10 μg/ml.

A capture plate with IFN-γ antibody is prepared, washed and blocked as described in the example above.

On day 9 of the assay, twenty four hours after the second antigen stimulation, the stimulation plate is spun for 5 minutes at 1500 RPM and 90 μl of supernatant is carefully removed from each well with a micropipette. The pelleted cells are resuspended in 100 μl of hTCM, pooled in sterile tubes, mixed and transferred into an equal number of wells of an anti IFN-γ capture plate. Capture plates are incubated undisturbed at 37° C. for 16-20 hours. At the end of the IFN-γ secretion phase, the cells are discarded and the plates are washed three times with 0.1% PBST. A final aliquot of PBST is added to the wells for ten minutes, removed, and 100 μl of a 1:500 dilution of rabbit anti-human IFN-γ polyclonal antibody in PBST+1% BSA is added to each well for 3.5 hours at room temperature with gentle rocking. Unbound anti-IFN-γ polyclonal antibody is removed by three washes with PBST, followed by a wash with 250 μl of 1×Tris-buffered saline+0.05% Tween 20 (TBST). Next, a 100 μl aliquot of 1:5000 alkaline phosphatase-conjugated mouse anti-rabbit polyclonal antibody diluted in TBST is added to each well and incubated at room temperature for 1.5-2 hours with gentle rocking. Excess enzyme-conjugated antibody is removed by three washes with PBST and two washes with alkaline phosphatase followed by addition of the substrate mix of p-Toluidine salt and nitroblue tetrazolium chloride. To stop the calorimetric reaction, plates were washed three times in dH₂O, inverted to minimize deposition of dust in the wells, and dried overnight at 28° C. in a dust free drying oven.

Images of the spots corresponding to the lymphokine secreted by individual antigen-stimulated T cells are captured with a CCD video camera and the image is analyzed as described in the example above

We conclude that the experiment detailed above can be used for the enumeration of single IFN-γ secreting T cells in blood from Multiple Sclerosis patients.

Example 84

This is an example of measurement of antigen reactive T-Cells by IFN-γ capture in blood samples from Multiple Sclerosis (MS) patients by ELISPOT.

This is an example of indirect detection of TCR, where individual cells are immobilized and measured by a chromogen assay. Antigenic peptide origin is MS, thus, immune monitoring of MS.

The example provides a sensitive assay for the detection of T-cells reactive to the antigen Myelin Oligodendrocyte Glycoprotein (MOG), by detecting a soluble factor whose secretion is induced by stimulation of the T-cell by the antigen.

This example is similar to the experiment above PBMCs from Multiple Sclerosis patients are isolated, prepared and stored as described in the example above.

The purified PBMCs are plated at 2×10⁵ cells/well at a volume of 0.1 ml in 96 well Costar cell culture plates. An equal volume of antigen, MOG 1-20 (GQFRVIGPRHPIRALVGDEV) or 41-60 (RPPFSRVVHLYRNGKDQDGD), at 10 μg/ml is added to triplicate or sextuplet sets of wells and the plate is incubated in a 37° C., 5% CO₂ incubator. On day five, 10 μl/well of 100 U/ml stock recombinant IL-2 is added to each well. On day 8, frozen PBMCs are thawed, washed in DPBS+0.5% BSA to remove DMSO, resuspended to a concentration of 4×10⁶ cells/ml in hTCM, and γ-irradiated (3,000 RADS). 50 μl/well are dispensed along with 50 μl of the appropriate antigen at a stock concentration of 40 μl/ml to give a final antigen concentration of 10 μg/ml.

A capture plate with IFN-γ antibody is prepared, washed and blocked as described in the example above.

On day 9 of the assay, twenty four hours after the second antigen stimulation, the stimulation plate is spun for 5 minutes at 1500 RPM and 90 μl of supernatant is carefully removed from each well with a micropipette. The pelleted cells are resuspended in 100 μl of hTCM, pooled in sterile tubes, mixed and transferred into an equal number of wells of an anti IFN-γ capture plate. Capture plates are incubated undisturbed at 37° C. for 16-20 hours. At the end of the IFN-γ secretion phase, the cells are discarded and the plates are washed three times with 0.1% PBST. A final aliquot of PBST is added to the wells for ten minutes, removed, and 100 μl of a 1:500 dilution of rabbit anti-human IFN-γ polyclonal antibody in PBST+1% BSA is added to each well for 3.5 hours at room temperature with gentle rocking. Unbound anti-IFN-γ polyclonal antibody is removed by three washes with PBST, followed by a wash with 250 μl of 1×Tris-buffered saline+0.05% Tween 20 (TBST). Next, a 100 μl aliquot of 1:5000 alkaline phosphatase-conjugated mouse anti-rabbit polyclonal antibody diluted in TBST is added to each well and incubated at room temperature for 1.5-2 hours with gentle rocking. Excess enzyme-conjugated antibody is removed by three washes with PBST and two washes with alkaline phosphatase followed by addition of the substrate mix of p-Toluidine salt and nitroblue tetrazolium chloride. To stop the calorimetric reaction, plates were washed three times in dH₂O, inverted to minimize deposition of dust in the wells, and dried overnight at 28° C. in a dust free drying oven.

Images of the spots corresponding to the lymphokine secreted by individual antigen-stimulated T cells are captured with a CCD video camera and the image is analyzed as described in the example above

We conclude that the experiment detailed above can be used for the enumeration of single IFN-δ secreting T cells in blood from Multiple Sclerosis patients.

Example 85

This is an example of measurement of antigen reactive T-Cells by IFN-γ capture in blood samples from Rheumatoid Arthritis (RA) patients by ELISPOT.

This is an example of indirect detection of TCR, where individual cells are immobilized and measured by a chromogen assay. Antigenic peptide origin is RA, thus, immune monitoring of RA.

The example provides a sensitive assay for the detection of T-cells reactive to the antigen type II collagen (CII) 261-273, by detecting a soluble factor whose secretion is induced by stimulation of the T-cell by the antigen.

This example is similar to the experiment above. PBMCs from Rheumatoid Arthritis patients are isolated, prepared and stored as described in the example above.

The purified PBMCs are plated at 2×10⁵ cells/well at a volume of 0.1 ml in 96 well Costar cell culture plates. An equal volume of antigen, CII 261-273 (AGFKGEQGPKGEP), at 10 μg/ml is added to triplicate or sextuplet sets of wells and the plate is incubated in a 37° C., 5% CO₂ incubator. On day five, 10 μl/well of 100 U/ml stock recombinant IL-2 is added to each well. On day 8, frozen PBMCs are thawed, washed in DPBS+0.5% BSA to remove DMSO, resuspended to a concentration of 4×10⁶ cells/ml in hTCM, and γ-irradiated (3,000 RADS). 50 μl/well are dispensed along with 50 μl of the appropriate antigen at a stock concentration of 40 μl/ml to give a final antigen concentration of 10 μg/ml.

A capture plate with IFN-γ antibody is prepared, washed and blocked as described in the example above.

On day 9 of the assay, twenty four hours after the second antigen stimulation, the stimulation plate is spun for 5 minutes at 1500 RPM and 90 μl of supernatant is carefully removed from each well with a micropipette. The pelleted cells are resuspended in 100 μl of hTCM, pooled in sterile tubes, mixed and transferred into an equal number of wells of an anti IFN-γ capture plate. Capture plates are incubated undisturbed at 37° C. for 16-20 hours. At the end of the IFN-γ secretion phase, the cells are discarded and the plates are washed three times with 0.1% PBST. A final aliquot of PBST is added to the wells for ten minutes, removed, and 100 μl of a 1:500 dilution of rabbit anti-human IFN-γ polyclonal antibody in PBST+1% BSA is added to each well for 3.5 hours at room temperature with gentle rocking. Unbound anti-IFN-γ polyclonal antibody is removed by three washes with PBST, followed by a wash with 250 μl of 1×Tris-buffered saline+0.05% Tween 20 (TBST). Next, a 100 μl aliquot of 1:5000 alkaline phosphatase-conjugated mouse anti-rabbit polyclonal antibody diluted in TBST is added to each well and incubated at room temperature for 1.5-2 hours with gentle rocking. Excess enzyme-conjugated antibody is removed by three washes with PBST and two washes with alkaline phosphatase followed by addition of the substrate mix of p-Toluidine salt and nitroblue tetrazolium chloride. To stop the calorimetric reaction, plates were washed three times in dH₂O, inverted to minimize deposition of dust in the wells, and dried overnight at 28° C. in a dust free drying oven.

Images of the spots corresponding to the lymphokine secreted by individual antigen-stimulated T cells are captured with a CCD video camera and the image is analyzed as described in the example above

We conclude that the experiment detailed above can be used for the enumeration of single IFN-γ secreting T cells in blood from Rheumatoid Arthritis patients.'

Example 86

This is an example of measurement of antigen reactive T-Cells by IFN-γ capture in blood samples from Melanoma patients by ELISPOT.

This is an example of indirect detection of TCR, where individual cells are immobilized and measured by a chromogen assay. The antigenic peptide origin is Melanoma, thus, immune monitoring of cancer.

The example provides a sensitive assay for the detection of T-cells reactive to the antigen MELAN-A/MART-1 27-35, by detecting a soluble factor whose secretion is induced by stimulation of the T-cell by the antigen.

This example is similar to the experiment above. PBMCs from Melanoma patients are isolated, prepared and stored as described in the example above.

The purified PBMCs are plated at 2×10⁵ cells/well at a volume of 0.1 ml in 96 well Costar cell culture plates. An equal volume of antigen, MELAN-A/MART-1 27-35 (AAGIGILTV), at 10 μg/ml is added to triplicate or sextuplet sets of wells and the plate is incubated in a 37° C., 5% CO₂ incubator. On day five, 10 μl/well of 100 U/ml stock recombinant IL-2 is added to each well. On day 8, frozen PBMCs are thawed, washed in DPBS+0.5% BSA to remove DMSO, resuspended to a concentration of 4×10⁶ cells/ml in hTCM, and γ-irradiated (3,000 RADS). 50 μl/well are dispensed along with 50 μl of the appropriate antigen at a stock concentration of 40 μl/ml to give a final antigen concentration of 10 μg/ml.

A capture plate with IFN-γ antibody is prepared, washed and blocked as described in the example above.

On day 9 of the assay, twenty four hours after the second antigen stimulation, the stimulation plate is spun for 5 minutes at 1500 RPM and 90 μl of supernatant is carefully removed from each well with a micropipette. The pelleted cells are resuspended in 100 μl of hTCM, pooled in sterile tubes, mixed and transferred into an equal number of wells of an anti IFN-γ capture plate. Capture plates are incubated undisturbed at 37° C. for 16-20 hours. At the end of the IFN-γ secretion phase, the cells are discarded and the plates are washed three times with 0.1% PBST. A final aliquot of PBST is added to the wells for ten minutes, removed, and 100 μl of a 1:500 dilution of rabbit anti-human IFN-γ polyclonal antibody in PBST+1% BSA is added to each well for 3.5 hours at room temperature with gentle rocking. Unbound anti-IFN-γ polyclonal antibody is removed by three washes with PBST, followed by a wash with 250 μl of 1×Tris-buffered saline+0.05% Tween 20 (TBST). Next, a 100 μl aliquot of 1:5000 alkaline phosphatase-conjugated mouse anti-rabbit polyclonal antibody diluted in TBST is added to each well and incubated at room temperature for 1.5-2 hours with gentle rocking. Excess enzyme-conjugated antibody is removed by three washes with PBST and two washes with alkaline phosphatase followed by addition of the substrate mix of p-Toluidine salt and nitroblue tetrazolium chloride. To stop the calorimetric reaction, plates were washed three times in dH₂O, inverted to minimize deposition of dust in the wells, and dried overnight at 28° C. in a dust free drying oven.

Images of the spots corresponding to the lymphokine secreted by individual antigen-stimulated T cells are captured with a CCD video camera and the image is analyzed as described in the example above

We conclude that the experiment detailed above can be used for the enumeration of single IFN-γ secreting T cells in blood from Melanoma patients.

Example 87

This is an example of measurement of antigen reactive T-Cells by IFN-γ capture in blood samples by ELISPOT.

This is an example of indirect detection of TCR, where individual cells are immobilized and measured by a chromogen assay. The antigenic peptide origin is a library of antigens.

The example provides a sensitive assay for the detection of T-cells reactive to the antigen of a library generated as described in example 42, by detecting a soluble factor whose secretion is induced by stimulation of the T-cell by the antigen.

This example is similar to the experiment above. PMBC are isolated, prepared and stored as described in the example above.

The purified PBMCs are plated at 2×10⁵ cells/well at a volume of 0.1 ml in 96 well Costar cell culture plates. An equal volume of antigens from the library, at 10 μg/ml is added to triplicate or sextuplet sets of wells and the plate is incubated in a 37° C., 5% CO₂ incubator. On day five, 10 μl/well of 100 U/ml stock recombinant IL-2 is added to each well. On day 8, frozen PBMCs are thawed, washed in DPBS+0.5% BSA to remove DMSO, resuspended to a concentration of 4×10⁶ cells/ml in hTCM, and γ-irradiated (3,000 RADS). 50 μl/well are dispensed along with 50 μl of the appropriate antigen at a stock concentration of 40 μl/ml to give a final antigen concentration of 10 μg/ml.

A capture plate with IFN-γ antibody is prepared, washed and blocked as described in the example above.

On day 9 of the assay, twenty four hours after the second antigen stimulation, the stimulation plate is spun for 5 minutes at 1500 RPM and 90 μl of supernatant is carefully removed from each well with a micropipette. The pelleted cells are resuspended in 100 μl of hTCM, pooled in sterile tubes, mixed and transferred into an equal number of wells of an anti IFN-γ capture plate. Capture plates are incubated undisturbed at 37° C. for 16-20 hours. At the end of the IFN-γ secretion phase, the cells are discarded and the plates are washed three times with 0.1% PBST. A final aliquot of PBST is added to the wells for ten minutes, removed, and 100 μl of a 1:500 dilution of rabbit anti-human IFN-γ polyclonal antibody in PBST+1% BSA is added to each well for 3.5 hours at room temperature with gentle rocking. Unbound anti-IFN-γ polyclonal antibody is removed by three washes with PBST, followed by a wash with 250 μl of 1×Tris-buffered saline+0.05% Tween 20 (TBST). Next, a 100 μl aliquot of 1:5000 alkaline phosphatase-conjugated mouse anti-rabbit polyclonal antibody diluted in TBST is added to each well and incubated at room temperature for 1.5-2 hours with gentle rocking. Excess enzyme-conjugated antibody is removed by three washes with PBST and two washes with alkaline phosphatase followed by addition of the substrate mix of p-Toluidine salt and nitroblue tetrazolium chloride. To stop the calorimetric reaction, plates were washed three times in dH₂O, inverted to minimize deposition of dust in the wells, and dried overnight at 28° C. in a dust free drying oven.

Images of the spots corresponding to the lymphokine secreted by individual antigen-stimulated T cells are captured with a CCD video camera and the image is analyzed as described in the example above

We conclude that the experiment detailed above can be used for the enumeration of single IFN-γ secreting T cells in blood.

Example 88

This is an example of how antigen specific T-cells can be detected using a direct detection method detecting T cell immobilized in solid tissue. In this example MHC dextramers are used to detect antigen specific T cells on frozen tissue sections using enzymatic chromogenic precipitation detection.

Equilibrate the cryosection tissue (e.g. section of spleen from transgenic mice) to −20° C. in the cryostate. Cut 5 μm sections and then dry sections on slides at room temperature. Store slides frozen until use at −20° C.

Equilibrate frozen sections to room temperature. Fix with acetone for 5 min.

Immediately after fixation transfer slides to TBS buffer (50 mM Tris-HCL pH 7.6, 150 mM NaCl) for 10 min.

Incubate slides with FITC-conjugated MHC-dextramers at appropriate dilution (1:40-1:80) and incubate for 30 min at room temperature. Other dilution ranges, as well as incubation time and temperature, may be desirable.

Decant solution and gently tap slides against filter paper, submerge in TBS buffer.

Decant and wash for 10 min in TBS buffer.

Incubate with rabbit polyclonal anti-FITC antibody (Dako P5100) at 1:100 dilution in TBS at room temperature for 30 min.

Repeat step 5 and 6.

Incubate with Envision anti-Rabbit HRP (Dako K4003) at room temperature for 30 min. Other visualization systems may be used.

Repeat step 5 and 6.

Develop with DAB+ (Dako K3468) in fume hood for 10 min. Other substrates may be used

Rinse slides in tap-water for 5 min.

Counterstain with hematoxylin (Dako 53309) for 2 min.

Repeat step 12, mount slides.

The slides stained with MHC-Dextramers can now be evaluated by microscopy.

Example 89

This is an example of how antigen specific T-cells can be detected using a direct detection method detecting T cell immobilized in solid tissue. In this example MHC dextramers are used to detect antigen specific T cells on paraffin embedded tissue sections using enzymatic chromogenic precipitation detection.

Formaldehyde fixed paraffin-embedded tissue are cut in section and mounted on the glass slice, for subsequent IHC staining with MHC-dextramers. Tissue fixed and prepared according to other protocols may be used as well. E.g. fresh tissue, lightly fixed tissue section (e.g. tissue fixed in 2% formaldehyde) or formalin-fixed, paraffin-embedded tissue section.

Optimal staining may require target retrieval treatment with enzymes as well as heating in a suitable buffer before incubation with antibodies and MHC-dextramer.

The sample is stained for DNA using DAPI stain, followed by incubated with an antigen specific MHCdex/FITC reagent, followed by addition of anti-FITC antibody labeled with HRP. Then the substrate for HRP, “DAP” is added and the reaction allows to progress.

The sample is analyzed by light microscopy for the present of a colored precipitate on the cells (DAPI stained nucleus) positive for the specific MHC/dex reagent.

A digital image of the stained sample is obtained, and this can be analyzed manually in the same way as by microscopy. However, a digital image may be used for automatic determination of where and how many cells that are positive, related to the total amount of cells, determined by the DAPI staining, or other criteria or stainings.

Items

The present invention is further disclosed herein below by citation of the following, non-limiting items of the invention.

1. A MHC complex comprising one or more functional MHC molecule(s) capable of binding a peptide P,

wherein, when more than one MHC molecule is present, the MHC complex further comprises a multimerization domain preferably comprising at least one binding entity and/or a carrier,

wherein, when the multimerization domain is present, the more than one functional MHC molecules are attached either to the at least one binding entity and/or to the carrier,

wherein, when the more than one functional MHC molecules are attached to the carrier, the MHC molecules are either attached directly to the carrier or attached to the carrier via one or more binding entities.

2. The MHC complex according to item 1, wherein the MHC molecule is a vertebrate MHC molecule such as a human, a murine, a rat, a porcine, a bovine or an avian molecule.

3. The MHC complex according to item 1 or 2, wherein the MHC molecule is a human MHC molecule.

4. The MHC complex according to any one of items 1-3, wherein the MHC molecule is a MHC Class I molecule selected from the group consisting of a heavy chain, a heavy chain combined with a β₂m, a heavy chain combined with a peptide, and a heavy chain/□₂m dimer with a peptide;

or a MHC Class II molecule selected from the group consisting of an α/β dimer, an α/β dimer with a peptide, α/β dimer combined through an affinity tag and a α/β dimer combined through an affinity tag with a peptide;

or a MHC Class I like molecule or MHC Class II like molecule.

5. The MHC complex according to any one of items 1-4, wherein the MHC molecule is a peptide free MHC molecule.

6. The MHC complex according to any one of items 1-5, wherein more than one MHC molecule is present, and wherein at least two of said MHC molecules are different.

7. The MHC complex according to any one of items 1-5, wherein more than one MHC molecule is present, and wherein the MHC molecules are the same.

8. The MHC complex according to any one of items 1-7, wherein at least two of the peptides harboured by the MHC complexes are different.

9. The MHC complex according to any one of items 1-7, wherein the peptides harboured by the MHC complexes are the same.

10. The MHC complex according to any one of items 1-9, wherein the MHC molecule(s) are attached to the carrier directly.

11. The MHC complex according to any one of items 1-9, wherein the MHC molecule(s) are attached to the carrier via one or more binding entities.

12. The MHC complex according to item 11, wherein each binding entity has attached thereto from 1 to 10 MHC molecules.

13. The MHC complex according to item 11, wherein each binding entity has attached thereto from 1 to 8 MHC molecules.

14. The MHC complex according to item 11, wherein each binding entity has attached thereto from 1 to 6 MHC molecules.

15. The MHC complex according to item 11, wherein each binding entity has attached thereto from 1 to 4 MHC molecules.

16. The MHC complex according to item 11, wherein each binding entity has attached thereto from 1 to 3 MHC molecules.

17. The MHC complex according to item 11, wherein each binding entity has attached thereto 1 or 2 MHC molecules.

18. The MHC complex according to any one of items 1-17, wherein the total number of MHC molecules of the construct is from 1 to 100.

19. The MHC complex according to any one of items 1-17, wherein the total number of MHC molecules of the construct is from 1 to 50.

20. The MHC complex according to any one of items 1-17, wherein the total number of MHC molecules of the construct is from 1 to 25.

21. The MHC complex according to item 1, wherein the binding entity is selected from streptavidin (SA) and avidin and derivatives thereof, biotin, immunoglobulins, antibodies (monoclonal, polyclonal, and recombinant), antibody fragments and derivatives thereof, leucine zipper domain of AP-1 (jun and fos), hexa-his (metal chelate moiety), hexa-hat GST (glutathione S-tranferase) glutathione affinity, Calmodulin-binding peptide (CBP), Strep-tag, Cellulose Binding Domain, Maltose Binding Protein, S-Peptide Tag, Chitin Binding Tag, Immuno-reactive Epitopes, Epitope Tags, E2Tag, HA Epitope Tag, Myc Epitope, FLAG Epitope, AU1 and AU5 Epitopes, Glu-Glu Epitope, KT3 Epitope, IRS Epitope, Btag Epitope, Protein Kinase-C Epitope, VSV Epitope, lectins that mediate binding to a diversity of compounds, including carbohydrates, lipids and proteins, e.g. Con A (Canavalia ensiformis) or WGA (wheat germ agglutinin) and tetranectin or Protein A or G (antibody affinity).

22. The MHC complex according to any one of items 1-21, further comprising one or more biologically active molecules.

23. The MHC complex according to claim 22, wherein the biologically active molecules is selected from proteins, co-stimulatory molecules, cell modulating molecules, receptors, accessory molecules, adhesion molecules, natural ligands, and toxic molecules, and antibodies and recombinant binding molecules thereto, and combinations thereof.

24. The MHC complex according to items 22 or 23, wherein the biologically active molecule is attached to the carrier either directly or via one or more of the binding entities.

25. The MHC complex according to any one of items 22-24, wherein the biologically active molecule is selected from proteins such as MHC Class I-like proteins like MIC A, MIC B, CD1d, HLA E, HLA F, HLA G, HLA H, ULBP-1, ULBP-2, and ULBP-3,

co-stimulatory molecules such as CD2, CD3, CD4, CD5, CD8, CD9, CD27, CD28, CD30, CD69, CD134 (OX40), CD137 (4-1BB), CD147, CDw150 (SLAM), CD152 (CTLA-4), CD153 (CD30L), CD40L (CD154), NKG2D, ICOS, HVEM, HLA Class II, PD-1, Fas (CD95), FasL expressed on T and/or NK cells, CD40, CD48, CD58, CD70, CD72, B7.1 (CD80), B7.2 (CD86), B7RP-1, B7-H3, PD-L1, PD-L2, CD134L, CD137L, ICOSL, LIGHT expressed on APC and/or tumour cells, cell modulating molecules such as CD16, NKp30, NKp44, NKp46, NKp80, 2B4, KIR, LIR, CD94/NKG2A, CD94/NKG2C expressed on NK cells, IFN-alpha, IFN-beta, IFN-gamma, IL-1, IL-2, IL-3, IL-4, IL-6, IL-7, IL-8, IL-10, IL-11, IL-12, IL-15, CSFs (colony-stimulating factors), vitamin D3, IL-2 toxins, cyclosporin, FK-506, rapamycin, TGF-beta, clotrimazole, nitrendipine, and charybdotoxin, accessory molecules such as LFA-1, CD11a/18, CD54 (ICAM-1), CD106 (VCAM), and CD49a,b,c,d,e,f/CD29 (VLA-4), adhesion molecules such as ICAM-1, ICAM-2, GlyCAM-1, CD34, anti-LFA-1, anti-CD44, anti-beta7, chemokines, CXCR4, CCR5, anti-selectin L, anti-selectin E, and anti-selectin P, toxic molecules such as cyclophosphamide, methrotrexate, Azathioprine, mizoribine, 15-deoxuspergualin, neomycin, staurosporine, genestein, herbimycin A, Pseudomonas exotoxin A, saporin, Rituxan, Ricin, gemtuzumab ozogamicin, Shiga toxin, heavy metals like inorganic and organic mercurials, and FN18-CRM9, radioisotopes such as incorporated isotopes of iodide, cobalt, selenium, tritium, and phosphor, and haptens such as DNP, and digoxiginin, and antibodies thereto, or antibody derivatives or fragments thereof, and combinations thereof.

26. The MHC complex according to any of items 1-25 further comprising one or more labelling compounds.

27. The MHC complex according to item 26, wherein one or more labelling compounds are attached to the carrier.

28. The MHC complex according to item 26, wherein one or more labelling compounds are attached to one or more of the binding entities.

29. The MHC complex according to item 26, wherein one or more labelling compounds are attached to the MHC molecule(s).

30. The MHC complex according to item 26, wherein one or more labelling compounds are attached to the carrier and/or one or more of the binding entities and/or one or more of the MHC molecules.

31. The MHC complex according to any one of items 26-30, wherein the labelling compound is directly or indirectly detectable.

32. The MHC complex according to any of items 26-31, wherein the labelling compound is a fluorescent label, an enzyme label, a radioisotope, a chemiluminescent label, a bioluminescent label, a polymer, a metal particle, a hapten, an antibody, or a dye.

33. The MHC complex according to any one of items 26-32, wherein the labelling compound

is selected from fluorescent labels such as 5-(and 6)-carboxyfluorescein, 5- or 6-carboxyfluorescein, 6-(fluorescein)-5-(and 6)-carboxamido hexanoic acid, fluorescein isothiocyanate (F)TC), rhodamine, tetramethylrhodamine, and dyes such as Cy2, Cy3, and Cy5, optionally substituted coumarin including AMCA, PerCP, phycobiliproteins including R-phycoerythrin (RPE) and allophycoerythrin (APC), Texas Red, Princeston Red, Green fluorescent protein (GFP) and analogues thereof, and conjugates of R-phycoerythrin or allophycoerythrin and e.g. Cy5 or Texas Red, and inorganic fluorescent labels based on semiconductor nanocrystals (like quantum dot and Qdot™ nanocrystals), and time-resolved fluorescent labels based on lanthanides like Eu3+ and Sm3+, from haptens such as DNP, biotin, and digoxiginin, or is selected from enzymatic labels such as horse radish peroxidase (HRP), alkaline phosphatase (AP), beta-galactosidase (GAL), glucose-6-phosphate dehydrogenase, beta-N-acetyl-glucosaminidase, β-glucuronidase, invertase, Xanthine Oxidase, firefly luciferase and glucose oxidase (GO), or is selected from luminiscence labels such as luminol, isoluminol, acridinium esters, 1,2-dioxetanes and pyridopyridazines, or is selected from radioactivity labels such as incorporated isotopes of iodide, cobalt, selenium, tritium, and phosphor.

34. The MHC complex according to any one of items 1-33, wherein the carrier is selected from

polysaccharides including dextrans, carboxy methyl dextran, dextran polyaldehyde, carboxymethyl dextran lactone, and cyclodextrins,

pullulans, schizophyllan, scleroglucan, xanthan, gellan, O-ethylamino guaran, chitins and chitosans including 6-O-carboxymethyl chitin and N-carboxymethyl chitosan,

derivatised cellolosics including carboxymethyl cellulose, carboxymethyl hydroxyethyl cellulose, hydroxyethyl cellulose, 6-amino-6-deoxy cellulose and O-ethylamine cellulose,

hydroxylated starch, hydroxypropyl starch, hydroxyethyl starch, carrageenans, alginates, and agarose,

synthetic polysaccharides including ficoll and carboxymethylated ficoll,

vinyl polymers including poly(acrylic acid), poly(acryl amides), poly(acrylic esters), poly(2-hydroxy ethyl methacrylate), poly(methyl methacrylate), poly(maleic acid), poly(maleic anhydride), poly(acrylamide), poly(ethyl-co-vinyl acetate), poly(methacrylic acid), poly(vinyl-alcohol), poly(vinyl alcohol-co-vinyl chloroacetate), aminated poly(vinyl alcohol), and co block polymers thereof, poly ethylene glycol (PEG) or polypropylene glycol or poly(ethylene oxide-co-propylene oxides) containing polymer backbones including linear, comb-shaped or StarBurst™ dendrimers, poly amino acids including polylysines, polyglutamic acid, polyurethanes, poly(ethylene imines), pluriol. proteins including albumins, immunoglobulins, and virus-like proteins (VLP), and polynucleotides, DNA, PNA, LNA, oligonucleotides and oligonucleotide dendrimer constructs.

35. The MHC complex according to any one of items 1-34, wherein the carrier is a soluble carrier.

36. The MHC complex according to any one of items 1-35 in soluble form.

37. The MHC complex according to any one of items 1-36 immobilised onto a solid or semi-solid support.

38. The MHC complex according to item 37, immobilised directly to the solid or semi-solid support.

39. The MHC complex according to item 37, immobilised to the solid or semi-solid support via a linker, a spacer, or an antibody, an antibody derivative or a fragment thereof.

40. The MHC complex according to any one of items 37-39, wherein the support is selected from particles, beads, biodegradable particles, sheets, gels, filters, membranes (e.g. nylon membranes), fibres, capillaries, needles, microtitre strips, tubes, plates or wells, combs, pipette tips, micro arrays, and chips.

41. The MHC complex according to item 40, wherein the support is selected from beads and particles.

42. The MHC complex according to item 41, wherein the beads and particles are polymeric beads, polymeric particles, magnetic beads, magnetic particles, supermagnetic beads, or supermagnetic particles.

43. The MHC complex according to any one of items 1-42 for use in a flow cytometric method.

44. The MHC complex according to any one of items 1-42 for use in a histological method.

45. The MHC complex according to any one of items 1-42 for use in a cytological method.

46. A method for detecting the presence of MHC recognising cells in a sample comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC complex according to items 1-42, and

(c) determining any binding of the MHC complex, which binding indicates the presence of MHC recognising cells.

47. A method for monitoring MHC recognising cells comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC complex according to items 1-42, and

(c) determining any binding of the MHC complex, thereby monitoring MHC recognising cells.

48. A method for establishing a prognosis of a disease involving MHC recognising cells comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC complex according to items 1-42, and

(c) determining any binding of the MHC complex, thereby establishing a prognosis of a disease involving MHC recognising cells.

49. A method for determining the status of a disease involving MHC recognising cells comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC complex according to items 1-42, and

(c) determining any binding of the MHC complex, thereby determining the status of a disease involving MHC recognising cells.

50. A method for diagnosing a disease involving MHC recognising cells comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells,

(b) contacting the sample with a MHC complex according to items 1-42, and

(c) determining any binding of the MHC complex, thereby diagnosing a disease involving MHC recognising cells.

51. A method for determining the effectiveness of a medicament against a disease involving MHC recognising cells comprising the steps of

(a) providing a sample from a subject receiving treatment with a medicament,

(b) contacting the sample with a MHC complex according to items 1-42, and

(c) determining any binding of the MHC complex, thereby determining the effectiveness of the medicament.

52. The method according to any one of items 46-51, wherein the MHC recognising cells are involved in a disease of inflammatory, auto-immune, allergic, viral, cancerous, infectious, allo- or xenogene (graft versus host and host versus graft) origin.

53. The method according to item 52, wherein the disease is a chronic inflammatory bowel disease such as Crohn's disease or ulcerative colitis, sclerosis, type I diabetes, rheumatoid arthritis, psoriasis, atopic dermatitis, asthma, malignant melanoma, renal carcinoma, breast cancer, lung cancer, cancer of the uterus, cervical cancer, prostatic cancer, brain cancer, head and neck cancer, leukaemia, cutaneous lymphoma, hepatic carcinoma, colorectal cancer, bladder cancer, rejection-related disease, Graft-versus-host-related disease, or a viral disease associated with hepatitis, AIDS, measles, pox, chicken pox, rubella or herpes.

54. The method according to any one of items 46-53, wherein the MHC recognising cells selected from subpopulations of CD3+ T-cells, gamma,delta T-cells, alpha,beta T-cells, CD4+ T-cells, T helper cells, CD8+ T-cells, Suppressor T-cells, CD8+ cytotoxic T-cells, CTLs, NK cells, NKT cells, LAK cells, and MAK.

55. The method according to any one of items 46-51, wherein the sample is selected from histological material, cytological material, primary tumours, secondary organ metastasis, fine needle aspirates, spleen tissue, bone marrow specimens, cell smears, exfoliative cytological specimens, touch preparations, oral swabs, laryngeal swabs, vaginal swabs, bronchial lavage, gastric lavage, from the umbilical cord, and from body fluids such as blood (e.g. from a peripheral blood mononuclear cell (PBMC) population isolated from blood or from other blood-derived preparations such as leukopheresis products), from sputum samples, expectorates, and bronchial aspirates.

56. The method according to any one of items 46-55, wherein the determination of the binding is carried out by inspection in a microscope, by light, by fluorescence, by electron transmission, or by flow cytometry.

57. The method according to any one of items 46-56, wherein the sample is mounted on a support.

58. The method according to item 57, wherein the support is a solid or semi-solid support.

59. The method according to item 57 or 58, wherein the support is selected from glass slides, microtiter plates having one or more wells, beads, particles, membranes, filters, filter membranes, polymer slides, polymer membranes, chamber slides, dishes, and petridishes.

60. A composition comprising a MHC complex according to any one of items 1-42 in a solubilising medium.

61. The composition according to item 60, wherein the MHC complex comprises peptide filled MHC molecules.

62. The composition according to item 60, wherein the MHC complex comprises peptide free MHC molecules.

63. The composition according to item 62, wherein peptides to fill the peptide free MHC molecules, and the MHC complex comprising peptide free molecules are provided separately.

64. A composition comprising a MHC complex according to any one of items 1-42, wherein the MHC complex is immobilised onto a solid or semi-solid support.

65. The composition according to item 64, wherein the support is selected from glass slides, microtiter plates having one or more wells, beads, particles, membranes, filters, filter membranes, polymer slides, polymer membranes, chamber slides, dishes, and petridishes.

66. The composition according to item 64 or 65, wherein the beads and particles are polymeric beads, polymeric particles, magnetic beads, magnetic particles, supermagnetic beads, or supermagnetic particles.

67. The composition according to item 64, wherein the MHC complex comprises peptide filled MHC molecules.

68. The composition according to item 64, wherein the MHC complex comprises peptide free MHC molecules.

69. The composition according to item 68, wherein peptides to fill the peptide free MHC molecules, and the MHC complex comprising peptide free molecules are provided separately.

70. Use of a MHC complex according to any one of items 1-42 as a detection system.

71. Use of a MHC complex according to any one of items 1-42 for diagnosing a disease involving MHC recognising cells.

72. Use of a MHC complex according to any one of items 1-42 for monitoring a disease involving MHC recognising cells.

73. Use of a MHC complex according to any one of items 1-42 for establishing a prognosis for a disease involving MHC recognising cells.

74. Use of a MHC complex according to any one of items 1-42 for determining the status of a disease involving MHC recognising cells.

75. Use of a MHC complex according to any one of items 1-42 for determining the effectiveness of a medicament against a disease involving MHC recognising cells.

76. Use according to any one of items 71, wherein the MHC recognising cells are involved in a disease of inflammatory, auto-immune, allergic, viral, cancerous, infectious, allo- or xenogene (graft-versus-host and host-versus-graft) origin.

77. Use according to item 76, wherein the disease is a chronic inflammatory bowel disease such as Crohn's disease or ulcerative colitis, sclerosis, type I diabetes, rheumatoid arthritis, psoriasis, atopic dermatitis, asthma, malignant melanoma, renal carcinoma, breast cancer, lung cancer, cancer of the uterus, cervical cancer, prostatic cancer, brain cancer, head and neck cancer, leukaemia, cutaneous lymphoma, hepatic carcinoma, colorectal cancer, bladder cancer, rejection-related disease, Graft-versus-host-related disease, or a viral disease associated with hepatitis, AIDS, measles, pox, chicken pox, rubella or herpes.

78. Use according to any one of items 70-77, wherein the MHC recognising cells are selected from subpopulations of CD3+ T-cells, gamma,delta T-cells, alpha,beta T-cells, CD4+ T-cells, T helper cells, CD8+ T-cells, Suppressor T-cells, CD8+ cytotoxic T-cells, CTLs, NK cells, NKT cells, LAK cells, and MAK.

79. The MHC complex according to any one of items 1-42 for use as a therapeutic composition.

80. The MHC complex according to any one of items 1-42 for use in in vivo therapy.

81. The MHC complex according to any one of items 1-42 for use in ex vivo therapy.

82. A therapeutic composition comprising as active ingredient a MHC complex as defined in any one of items 1-42.

83. The therapeutic composition according to item 82, wherein the MHC complex is immobilised to a biodegradable solid or semi-solid support.

84. The therapeutic composition according to item 82 or 83, wherein the MHC complex comprises

a carrier having attached thereto one or more MHC molecules, said MHC molecules being attached to the carrier either directly or via one or more binding entities.

85. The therapeutic composition according to item 82 or 83, wherein the MHC molecule is a vertebrate MHC molecule such as a human, a murine, a rat, a porcine, a bovine or an avian molecule.

86. The therapeutic composition according to any one of items 82-85, wherein the MHC molecule is a human MHC molecule.

87. The therapeutic composition according to any one of items 82-86, wherein the MHC molecule is

a MHC Class I molecule selected from the group consisting of a heavy chain, a heavy chain combined with a β₂m, a heavy chain combined with a peptide, and a heavy chain/□₂m dimer with a peptide;

or a MHC Class II molecule selected from the group consisting of an α/β dimer, an α/β dimer with a peptide, α/β dimer combined through an affinity tag and a α/β dimer combined through an affinity tag with a peptide

or a MHC Class I like molecule or a MHC Class II like molecule.

88. The therapeutic composition according to any one of items 82-87, wherein the MHC molecule is a peptide free MHC molecule.

89. The therapeutic composition according to any one of items 82-88, wherein at least two of the MHC molecules are different.

90. The therapeutic composition according to any one of items 82-88, wherein the MHC molecules are the same.

91. The therapeutic composition according to any one of items 82-88, wherein at least two of the peptides harboured by the MHC molecules are different.

92. The therapeutic composition according to any one of items 82-88, wherein the peptides harboured by the MHC molecules are the same.

93. The therapeutic composition according to any one of items 82-92, wherein the MHC molecules are attached to the carrier directly.

94. The therapeutic composition according to any one of items 82-92, wherein the MHC molecules are attached to the carrier via one or more binding entities.

95. The therapeutic composition according to item 94, wherein each binding entity has attached thereto from 1 to 10 MHC molecules.

96. The therapeutic composition according to item 94, wherein each binding entity has attached thereto from 1 to 8 MHC molecules.

97. The therapeutic composition according to item 94, wherein each binding entity has attached thereto from 1 to 6 MHC molecules.

98. The therapeutic composition according to item 94, wherein each binding entity has attached thereto from 1 to 4 MHC molecules.

99. The therapeutic composition according to item 94, wherein each binding entity has attached thereto from 1 to 3 MHC molecules.

100. The therapeutic composition according to item 94, wherein each binding entity has attached thereto 1 or 2 MHC molecules.

101. The therapeutic composition according to any one of items 82-100, wherein the total number of MHC molecules of the construct is from 1 to 100.

102. The therapeutic composition according to any one of items 82-100, wherein the total number of MHC molecules of the construct is from 1 to 50.

103. The therapeutic composition according to any one of items 82-100, wherein the total number of MHC molecules of the construct is from 1 to 25.

104. The therapeutic composition according to item 94, wherein the binding entity is selected from streptavidin (SA) and avidin and derivatives thereof, biotin, immunoglobulins, antibodies (monoclonal, polyclonal, and recombinant), antibody fragments and derivatives thereof, leucine zipper domain of AP-1 (jun and fos), hexa-his (metal chelate moiety), hexa-hat GST (glutathione S-tranferase) glutathione affinity, Calmodulin-binding peptide (CBP), Strep-tag, Cellulose Binding Domain, Maltose Binding Protein, S-Peptide Tag, Chitin Binding Tag, Immuno-reactive Epitopes, Epitope Tags, E2Tag, HA Epitope Tag, Myc Epitope, FLAG Epitope, AU1 and AU5 Epitopes, Glu-Glu Epitope, KT3 Epitope, IRS Epitope, Btag Epitope, Protein Kinase-C Epitope, VSV Epitope, lectins that mediate binding to a diversity of compounds, including carbohydrates, lipids and proteins, e.g. Con A (Canavalia ensiformis) or WGA (wheat germ agglutinin) and tetranectin or Protein A or G (antibody affinity).

105. The therapeutic composition according to any one of items 82-104 further comprising one or more biologically active molecules.

106. The therapeutic composition according to item 105, wherein the biologically active molecules is selected from proteins, co-stimulatory molecules, cell modulating molecules, receptors, accessory molecules, adhesion molecules, natural ligands, and toxic molecules, and antibodies and recombinant binding molecules thereto, and combinations thereof.

107. The therapeutic composition according to item 105 or 106, wherein the biologically active molecule is attached to the carrier either directly or via one or more of the binding entities.

108. The therapeutic composition according to any one of items 105-107, wherein the biologically active molecule is selected from

proteins such as MHC Class I-like proteins like MIC A, MIC B, CD1d, HLA E, HLA F, HLA G, HLA H, ULBP-1, ULBP-2, and ULBP-3,

co-stimulatory molecules such as CD2, CD3, CD4, CD5, CD8, CD9, CD27, CD28, CD30, CD69, CD134 (OX40), CD137 (4-1BB), CD147, CDw150 (SLAM), CD152 (CTLA-4), CD153 (CD30L), CD40L (CD154), NKG2D, ICOS, HVEM, HLA Class II, PD-1, Fas (CD95), FasL expressed on T and/or NK cells, CD40, CD48, CD58, CD70, CD72, B7.1 (CD80), B7.2 (CD86), B7RP-1, B7-H3, PD-L1, PD-L2, CD134L, CD137L, ICOSL, LIGHT expressed on APC and/or tumour cells, cell modulating molecules such as CD16, NKp30, NKp44, NKp46, NKp80, 2B4, KIR, LIR, CD94/NKG2A, CD94/NKG2C expressed on NK cells, IFN-alpha, IFN-beta, IFN-gamma, IL-1, IL-2, IL-3, IL-4, IL-6, IL-7, IL-8, IL-10, IL-11, IL-12, IL-15, CSFs (colony-stimulating factors), vitamin D3, IL-2 toxins, cyclosporin, FK-506, rapamycin, TGF-beta, clotrimazole, nitrendipine, and charybdotoxin, accessory molecules such as LFA-1, CD11a/18, CD54 (ICAM-1), CD106 (VCAM), and CD49a,b,c,d,e,f/CD29 (VLA-4), adhesion molecules such as ICAM-1, ICAM-2, GlyCAM-1, CD34, anti-LFA-1, anti-CD44, anti-beta7, chemokines, CXCR4, CCR5, anti-selectin L, anti-selectin E, and anti-selectin P, toxic molecules such as cyclophosphamide, methrotrexate, Azathioprine, mizoribine, 15-deoxuspergualin, neomycin, staurosporine, genestein, herbimycin A, Pseudomonas exotoxin A, saporin, Rituxan, Ricin, gemtuzumab ozogamicin, Shiga toxin, heavy metals like inorganic and organic mercurials, and FN18-CRM9, radioisotopes such as incorporated isotopes of iodide, cobalt, selenium, tritium, and phosphor, and haptens such as DNP, and digoxiginin, and antibodies thereto, or antibody derivatives or fragments thereof, and combinations thereof.

109. The therapeutic composition according to any one of items 82-108, wherein the carrier is selected from

polysaccharides including dextrans, carboxy methyl dextran, dextran polyaldehyde, carboxymethyl dextran lactone, and cyclodextrins,

pullulans, schizophyllan, scleroglucan, xanthan, gellan, O-ethylamino guaran, chitins and chitosans including 6-O-carboxymethyl chitin and N-carboxymethyl chitosan,

derivatised cellolosics including carboxymethyl cellulose, carboxymethyl hydroxyethyl cellulose, hydroxyethyl cellulose, 6-amino-6-deoxy cellulose and O-ethylamine cellulose,

hydroxylated starch, hydroxypropyl starch, hydroxyethyl starch, carrageenans, alginates, and agarose,

synthetic polysaccharides including ficoll and carboxymethylated ficoll, vinyl polymers including poly(acrylic acid), poly(acryl amides), poly(acrylic esters), poly(2-hydroxy ethyl methacrylate), poly(methyl methacrylate), poly(maleic acid), poly(maleic anhydride), poly(acrylamide), poly(ethyl-co-vinyl acetate), poly(methacrylic acid), poly(vinyl-alcohol), poly(vinyl alcohol-co-vinyl chloroacetate), aminated poly(vinyl alcohol), and co block polymers thereof, poly ethylene glycol (PEG) or polypropylene glycol or poly(ethylene oxide-co-propylene oxides) containing polymer backbones including linear, comb-shaped or StarBurst™ dendrimers, poly amino acids including polylysines, polyglutamic acid, polyurethanes, poly(ethylene imines), pluriol. proteins including albumins, immunoglobulins, and virus-like proteins (VLP), and polynucleotides, DNA, PNA, LNA, oligonucleotides and oligonucleotide dendrimer constructs.

110. The therapeutic composition according to any one of items 82-109, wherein the carrier is a soluble carrier.

111. The therapeutic composition according to any one of items 82-110 further comprising one or more adjuvants and/or excipients.

112. The therapeutic composition according to item 111, wherein the adjuvant is selected from saponins such as Quil A and Qs-21, oil in water emulsions such as MF59, MPL, PLG, PLGA, aluminium salts, calcium phosphate, water in oil emulsions such as IFA (Freund's incomplete adjuvant) and CFA (Freund's complete adjuvant), interleukins such as IL-1β, IL-2, IL-7, IL-12, and INFγ, Adju-Phos®, glucan, antigen formulation, biodegradable microparticles, Cholera Holotoxin, liposomes, DDE, DHEA, DMPC, DMPG, DOC/Alum Complex, ISCOMs®, muramyl dipeptide, monophosphoryl lipid A, muramyl tripeptide, and phospatidylethanolamine In a preferred embodiment, the adjuvant is selected from saponins such as Quil A and Qs-21, MF59, MPL, PLG, PLGA, calcium phosphate, and aluminium salts.

113. The therapeutic composition according to item 113, wherein the excipient is selected from diluents, buffers, suspending agents, wetting agents, solubilising agents, pH-adjusting agents, dispersing agents, preserving agents, and/or colorants.

114. The therapeutic composition according to any one of items 82-113 for the treatment, prevention, stabilisation, or alleviation of disease involving MHC recognising cells.

115. The therapeutic composition according to item 114, wherein the MHC recognising cells are involved in a disease of inflammatory, auto-immune, allergic, viral, cancerous, infectious, allo- or xenogene (graft versus host and host versus graft) origin.

116. The therapeutic composition according to item 115, wherein the disease is a chronic inflammatory bowel disease such as Crohn's disease or ulcerative colitis, sclerosis, type I diabetes, rheumatoid arthritis, psoriasis, atopic dermatitis, asthma, malignant melanoma, renal carcinoma, breast cancer, lung cancer, cancer of the uterus, prostatic cancer, brain cancer, head and neck cancer, leukaemia, cutaneous lymphoma, hepatic carcinoma, colorectal cancer, bladder cancer, rejection-related disease, Graft-versus-host-related disease, or a viral disease associated with hepatitis, AIDS, measles, pox, chicken pox, rubella or herpes.

117. The therapeutic composition according to any one of items 82-116 formulated for parenteral administration, including intravenous, intramuscular, intraarticular, subcutaneous, intradermal, epicutantous/transdermal, and intraperitoneal administration, for infusion, for oral administration, for nasal administration, for rectal administration, or for topic administration.

118. A therapeutic composition comprising as active ingredient an effective amount of MHC recognising cells, the MHC recognising cells being obtained by

bringing a sample from a subject comprising MHC recognising cells into contact with the MHC complex according to any one of items 1-42, whereby the MHC recognising cells become bound to the MHC complex,

isolating the bound MHC complex and the MHC recognising cells, and

expanding such MHC recognising cells to a clinically relevant number.

119. The therapeutic composition according to item 118, wherein the isolated MHC recognising cells are liberated from the MHC complex prior to expansion.

120. The therapeutic composition according to items 118 or 119, wherein the MHC complex is immobilised onto a solid or semi-solid support.

121. The therapeutic composition according to item 120, wherein the MHC complex is immobilised onto the solid or semi-solid support prior to contact with the sample.

122. The therapeutic composition according to item 120, wherein the MHC complex is immobilised onto the solid or semi-solid support following contact with the sample.

123. The therapeutic composition according to any one of items 118-122, wherein the expansion is carried out in the presence of one or more MHC complexes, optionally one or more biologically active molecules and optionally feeder cells such as dendritic cells or feeder cells.

124. The therapeutic composition according to any one of items 120-123, wherein the MHC complex is immobilised onto the solid or semi-solid support directly.

125. The therapeutic composition according to any one of items 120-124, wherein the MHC complex is immobilised to the solid or semi-solid support via a linker, a spacer, or an antibody, an antibody derivative or a fragment thereof.

126. The therapeutic composition according to any one of items 120-125, wherein the solid or semi-solid support is selected from particles, beads, biodegradable particles, sheets, gels, filters, membranes, fibres, capillaries, needles, microtitre strips, tubes, plates or wells, combs, pipette tips, micro arrays, chips, and microtiter plates having one or more wells.

127. The therapeutic composition according to any one of items 120-126, wherein the solid support is selected from particles and beads.

128. The therapeutic composition according to item 127, wherein the particles and beads are polymeric, magnetic or superparamagnetic.

129. The therapeutic composition according to any one of items 118-128, wherein the isolation is performed by applying a magnetic field or by flow cytometry.

130. The therapeutic composition according to any one of items 118-128, wherein the MHC complex comprises

a carrier having attached thereto one or more MHC molecules, said MHC molecules being attached to the carrier either directly or via one or more binding entities.

131. The therapeutic composition according to any one of items 118-130, wherein the MHC molecule is a vertebrate MHC molecule such as a human, a murine, a rat, a porcine, a bovine or an avian molecule.

132. The therapeutic composition according to any one of items 118-131, wherein the MHC molecule is a human MHC molecule.

133. The therapeutic composition according to any one of items 118-132, wherein the MHC molecule is

a MHC Class I molecule selected from the group consisting of a heavy chain, a heavy chain combined with a □₂m, a heavy chain combined with a peptide, and a heavy chain/□₂m dimer with a peptide;

or a MHC Class II molecule selected from the group consisting of an {tilde over (α)}□ dimer, an {tilde over (α)}□ dimer with a peptide, {tilde over (□)}□dimer combined through an affinity tag and a {tilde over (□)}□dimer combined through an affinity tag with a peptide;

or a MHC Class I like molecule or a MHC Class II molecule.

134. The therapeutic composition according to any one of items 118-133, wherein the MHC molecule is a peptide free MHC molecule.

135. The therapeutic composition according to any one of items 118-134, wherein at least two of the MHC molecules are different.

136. The therapeutic composition according to any one of items 118-135, wherein the MHC molecules are the same.

137. The therapeutic composition according to any one of items 118-136, wherein at least two of the peptides harboured by the MHC molecules are different.

138. The therapeutic composition according to any one of items 118-137, wherein the peptides harboured by the MHC molecules are the same.

139. The therapeutic composition according to any one of items 118-138, wherein the MHC molecules are attached to the carrier directly.

140. The therapeutic composition according to any one of items 118-138, wherein the MHC molecules are attached to the carrier via one or more binding entities.

141. The therapeutic composition according to item 140, wherein each binding entity has attached thereto from 1 to 10 MHC molecules.

142. The therapeutic composition according to item 140, wherein each binding entity has attached thereto from 1 to 8 MHC molecules.

143. The therapeutic composition according to item 140, wherein each binding entity has attached thereto from 1 to 6 MHC molecules.

144. The therapeutic composition according to item 140, wherein each binding entity has attached thereto from 1 to 4 MHC molecules.

145. The therapeutic composition according to item 140, wherein each binding entity has attached thereto from 1 to 3 MHC molecules.

146. The therapeutic composition according to item 140, wherein each binding entity has attached thereto 1 or 2 MHC molecules.

147. The therapeutic composition according to any one of items 118-146, wherein the total number of MHC molecules of the construct is from 1 to 100.

148. The therapeutic composition according to any one of items 118-146, wherein the total number of MHC molecules of the construct is from 1 to 50.

149. The therapeutic composition according to any one of items 118-146, wherein the total number of MHC molecules of the construct is from 1 to 25.

150. The therapeutic composition according to item 140, wherein the binding entity is selected from streptavidin streptavidin (SA) and avidin and derivatives thereof, biotin, immunoglobulins, antibodies (monoclonal, polyclonal, and recombinant), antibody fragments and derivatives thereof, leucine zipper domain of AP-1 (jun and fos), hexa-his (metal chelate moiety), hexa-hat GST (glutathione S-tranferase) glutathione affinity, Calmodulin-binding peptide (CBP), Strep-tag, Cellulose Binding Domain, Maltose Binding Protein, S-Peptide Tag, Chitin Binding Tag, Immuno-reactive Epitopes, Epitope Tags, E2Tag, HA Epitope Tag, Myc Epitope, FLAG Epitope, AU1 and AU5 Epitopes, Glu-Glu Epitope, KT3 Epitope, IRS Epitope, Btag Epitope, Protein Kinase-C Epitope, VSV Epitope, lectins that mediate binding to a diversity of compounds, including carbohydrates, lipids and proteins, e.g. Con A (Canavalia ensiformis) or WGA (wheat germ agglutinin) and tetranectin or Protein A or G (antibody affinity).

151. The therapeutic composition according to any one of items 118-150 further comprising one or more biologically active molecules.

152. The therapeutic composition according to item 151, wherein the biologically active molecules is selected from proteins, co-stimulatory molecules, cell modulating molecules, receptors, accessory molecules, adhesion molecules, natural ligands, and toxic molecules, and antibodies and recombinant binding molecules thereto, and combinations thereof.

153. The therapeutic composition according to item 150 or 151, wherein the biologically active molecule is attached to the carrier either directly or via one or more of the binding entities.

154. The therapeutic composition according to any one of items 151-153, wherein the biologically active molecule is selected from

proteins such as MHC Class I-like proteins like MIC A, MIC B, CD1d, HLA E, HLA F, HLA G, HLA H, ULBP-1, ULBP-2, and ULBP-3,

co-stimulatory molecules such as CD2, CD3, CD4, CD5, CD8, CD9, CD27, CD28, CD30, CD69, CD134 (OX40), CD137 (4-1BB), CD147, CDw150 (SLAM), CD152 (CTLA-4), CD153 (CD30L), CD40L (CD154), NKG2D, ICOS, HVEM, HLA Class II, PD-1, Fas (CD95), FasL expressed on T and/or NK cells, CD40, CD48, CD58, CD70, CD72, B7.1 (CD80), B7.2 (CD86), B7RP-1, B7-H3, PD-L1, PD-L2, CD134L, CD137L, ICOSL, LIGHT expressed on APC and/or tumour cells, cell modulating molecules such as CD16, NKp30, NKp44, NKp46, NKp80, 2B4, KIR, LIR, CD94/NKG2A, CD94/NKG2C expressed on NK cells, IFN-alpha, IFN-beta, IFN-gamma, IL-1, IL-2, IL-3, IL-4, IL-6, IL-7, IL-8, IL-10, IL-11, IL-12, IL-15, CSFs (colony-stimulating factors), vitamin D3, IL-2 toxins, cyclosporin, FK-506, rapamycin, TGF-beta, clotrimazole, nitrendipine, and charybdotoxin, accessory molecules such as LFA-1, CD11a/18, CD54 (ICAM-1), CD106 (VCAM), and CD49a,b,c,d,e,f/CD29 (VLA-4), adhesion molecules such as ICAM-1, ICAM-2, GlyCAM-1, CD34, anti-LFA-1, anti-CD44, anti-beta7, chemokines, CXCR4, CCR5, anti-selectin L, anti-selectin E, and anti-selectin P, toxic molecules such as cyclophosphamide, methrotrexate, Azathioprine, mizoribine, 15-deoxuspergualin, neomycin, staurosporine, genestein, herbimycin A, Pseudomonas exotoxin A, saporin, Rituxan, Ricin, gemtuzumab ozogamicin, Shiga toxin, heavy metals like inorganic and organic mercurials, and FN18-CRM9, radioisotopes such as incorporated isotopes of iodide, cobalt, selenium, tritium, and phosphor, and haptens such as DNP, and digoxiginin, and antibodies thereto, or antibody derivatives or fragments thereof, and combinations thereof.

155. The therapeutic composition according to any one of items 118-154, wherein the carrier is selected from

polysaccharides including dextrans, carboxy methyl dextran, dextran polyaldehyde, carboxymethyl dextran lactone, and cyclodextrins,

pullulans, schizophyllan, scleroglucan, xanthan, gellan, O-ethylamino guaran, chitins and chitosans including 6-O-carboxymethyl chitin and N-carboxymethyl chitosan,

derivatised cellolosics including carboxymethyl cellulose, carboxymethyl hydroxyethyl cellulose, hydroxyethyl cellulose, 6-amino-6-deoxy cellulose and O-ethylamine cellulose,

hydroxylated starch, hydroxypropyl starch, hydroxyethyl starch, carrageenans, alginates, and agarose,

synthetic polysaccharides including ficoll and carboxymethylated ficoll,

vinyl polymers including poly(acrylic acid), poly(acryl amides), poly(acrylic esters), poly(2-hydroxy ethyl methacrylate), poly(methyl methacrylate), poly(maleic acid), poly(maleic anhydride), poly(acrylamide), poly(ethyl-co-vinyl acetate), poly(methacrylic acid), poly(vinyl-alcohol), poly(vinyl alcohol-co-vinyl chloroacetate), aminated poly(vinyl alcohol), and co block polymers thereof, poly ethylene glycol (PEG) or polypropylene glycol or poly(ethylene oxide-co-propylene oxides) containing polymer backbones including linear, comb-shaped or StarBurst™ dendrimers, poly amino acids including polylysines, polyglutamic acid, polyurethanes, poly(ethylene imines), pluriol. proteins including albumins, immunoglobulins, and virus-like proteins (VLP), and polynucleotides, DNA, PNA, LNA, oligonucleotides and oligonucleotide dendrimer constructs.

156. The therapeutic composition according to any one of items 118-155 further comprising one or more labelling compounds.

157. The therapeutic composition according to item 156, wherein one or more labelling compounds are attached to the carrier.

158. The therapeutic composition according to item 156, wherein one or more labelling compounds are attached to one or more of the binding entities.

159. The therapeutic composition according to item 156, wherein one or more labelling compounds are attached to the one or more MHC molecules.

160. The therapeutic composition according to item 156, wherein one or more labelling compounds are attached to the carrier and/or one or more of the binding entities and/or one or more of the MHC molecules.

161. The therapeutic composition according to any one of items 156-160, wherein the labelling compound is directly or indirectly detectable.

162. The therapeutic composition according to any one of items 156-161, wherein the labelling compound is a fluorescent label, an enzyme label, a radioisotope, a chemiluminescent label, a bioluminescent label, a polymer, a metal particle, a hapten, an antibody, or a dye.

163. The therapeutic composition according to any one of items 156-162, wherein the labelling compound

is selected from fluorescent labels such as 5-(and 6)-carboxyfluorescein, 5- or 6-carboxyfluorescein, 6-(fluorescein)-5-(and 6)-carboxamido hexanoic acid, fluorescein isothiocyanate (FITC), rhodamine, tetramethylrhodamine, and dyes such as Cy2, Cy3, and Cy5, optionally substituted coumarin including AMCA, PerCP, phycobiliproteins including R-phycoerythrin (RPE) and allophycoerythrin (APC), Texas Red, Princeston Red, Green fluorescent protein (GFP) and analogues thereof, and conjugates of R-phycoerythrin or allophycoerythrin and e.g. Cy5 or Texas Red, and inorganic fluorescent labels based on semiconductor nanocrystals (like quantum dot and Qdot™ nanocrystals), and time-resolved fluorescent labels based on lanthanides like Eu3+ and Sm3+, from haptens such as DNP, biotin, and digoxiginin, or is selected from haptens such as DNP, fluorescein isothiocyanate (FITC), biotin, and digoxiginin, or is selected from enzymatic labels such as horse radish peroxidase (HRP), alkaline phosphatase (AP), beta-galactosidase (GAL), glucose-6-phosphate dehydrogenase, beta-N-acetyl-glucosaminidase, β-glucuronidase, invertase, Xanthine Oxidase, firefly luciferase and glucose oxidase (GO), or is selected from luminiscence labels such as luminol, isoluminol, acridinium esters, 1,2-dioxetanes and pyridopyridazines, or is selected from radioactivity labels such as incorporated isotopes of iodide, cobalt, selenium, tritium, and phosphor.

164. The therapeutic composition according to any one of items 118-163, wherein the carrier is a soluble carrier.

165. The therapeutic composition according to any one of items 118-164 further comprising one or more excipients.

166. The therapeutic composition according to items 165, wherein the excipient is selected from diluents, buffers, suspending agents, wetting agents, solubilising agents, pH-adjusting agents, dispersing agents, preserving agents, and/or colorants.

167. The therapeutic composition according to any one of items 118-166 for the treatment, prevention, stabilisation, or alleviation of a disease involving MHC recognising cells.

168. The therapeutic composition according to item 167, wherein MHC recognising cells are involved in a disease of inflammatory, auto-immune, allergic, viral, cancerous, infectious, allo- or xenogene (graft versus host and host versus graft) origin.

169. The therapeutic composition according to item 167 or 168, wherein the disease is a chronic inflammatory bowel disease such as Crohn's disease or ulcerative colitis, sclerosis, type I diabetes, rheumatoid arthritis, psoriasis, atopic dermatitis, asthma, malignant melanoma, renal carcinoma, breast cancer, lung cancer, cancer of the uterus, prostatic cancer, brain cancer, head and neck cancer, leukaemia, cutaneous lymphoma, hepatic carcinoma, colorectal cancer, bladder cancer, rejection-related disease, Graft-versus-host-related disease, or a viral disease associated with hepatitis, AIDS, measles, pox, chicken pox, rubella or herpes.

170. The therapeutic composition according to any one of items 118-169 formulated for parenteral administration, including intravenous, intramuscular, intraarticular, subcutaneous, intradermal, epicutantous/transdermal, and intraperitoneal administration, for infusion, for oral administration, for nasal administration, for rectal administration, or for topic administration.

171. The therapeutic composition according to any one of items 82-170 for use in in vivo therapy.

172. A method of treating an animal, including a human being, comprising administering a therapeutic composition according to any one of items 82-170 in an effective amount.

173. A method of up-regulating, down-regulating, modulate an immune response in an animal, including a human being, comprising administering a therapeutic composition according to any one of items 82-170 in an effective amount.

174. A method of inducing anergy of a cell in an animal, including a human being, comprising administering a therapeutic composition according to any one of items 82-170 in an effective amount.

175. An adoptive cellular immunotherapeutic method comprising administrating to an animal, including a human being, a therapeutic composition according to any one of items 82-170.

176. A method of obtaining MHC recognising cells comprising

bringing into contact a MHC complex according to any one of items 1-42 and a sample suspected of comprising MHC recognising cells under conditions whereby the MHC recognising cells bind to the MHC complex, and

isolating the bound MHC complex and MHC recognising cells.

177. The method according to item 176, wherein the isolation is carried out by applying a magnetic field or by flow cytometry.

178. A method for producing a therapeutic composition according to any one of items 82-170, comprising

providing a MHC complex as defined in items 1-42,

solubilising or dispersing the MHC complex in a medium suitable for therapeutic substances,

and optionally adding other adjuvants and/or excipients.

179. A method for producing a therapeutic composition according to any one of items 118-170, comprising

obtaining MHC recognising cells using a MHC complex according to any one of items 1-42,

expanding such MHC recognising cells to a clinically relevant number,

formulating the obtained cells in a medium suitable for administration, and

optionally adding adjuvants and/or excipients.

180. Use of a MHC complex according to any one of items 1-42 for ex vivo expansion of MHC recognising cells.

181. Use according to item 180, wherein the MHC complex is in soluble form.

182. Use according to item 180, wherein the MHC complex is immobilised onto a solid or semi-solid support.

183. Use according to item 182, wherein the solid or semi-solid support is selected from particles, beads, biodegradable particles, sheets, gels, filters, membranes (e.g. nylon membranes), fibres, capillaries, needles, microtitre strips, tubes, plates or wells, combs, pipette tips, micro arrays, chips, and slides.

184. Use according to item 182 or 183, wherein the solid or semi-solid support is selected from beads and particles.

185. Use according to item 184, wherein the solid or semi-solid support is selected from polymeric, magnetic or superparamagnetic particles and beads.

186. Use according to any one of items 180-185, wherein the MHC complex further comprises one or more biologically active molecules.

187. Use according to any one of items 180-186, wherein the biologically active molecule is selected from

proteins such as MHC Class I-like proteins like MIC A, MIC B, CD1d, HLA E, HLA F, HLA G, HLA H, ULBP-1, ULBP-2, and ULBP-3,

co-stimulatory molecules such as CD2, CD3, CD4, CD5, CD8, CD9, CD27, CD28, CD30, CD69, CD134 (OX40), CD137 (4-1BB), CD147, CDw150 (SLAM), CD152 (CTLA-4), CD153 (CD30L), CD40L (CD154), NKG2D, ICOS, HVEM, HLA Class II, PD-1, Fas (CD95), FasL expressed on T and/or NK cells, CD40, CD48, CD58, CD70, CD72, B7.1 (CD80), B7.2 (CD86), B7RP-1, B7-H3, PD-L1, PD-L2, CD134L, CD137L, ICOSL, LIGHT expressed on APC and/or tumour cells, cell modulating molecules such as CD16, NKp30, NKp44, NKp46, NKp80, 2B4, KIR, LIR, CD94/NKG2A, CD94/NKG2C expressed on NK cells, IFN-alpha, IFN-beta, IFN-gamma, IL-1, IL-2, IL-3, IL-4, IL-6, IL-7, IL-8, IL-10, IL-11, IL-12, IL-15, CSFs (colony-stimulating factors), vitamin D3, IL-2 toxins, cyclosporin, FK-506, rapamycin, TGF-beta, clotrimazole, nitrendipine, and charybdotoxin, accessory molecules such as LFA-1, CD11a/18, CD54 (ICAM-1), CD106 (VCAM), and CD49a,b,c,d,e,f/CD29 (VLA-4), adhesion molecules such as ICAM-1, ICAM-2, GlyCAM-1, CD34, anti-LFA-1, anti-CD44, anti-beta7, chemokines, CXCR4, CCR5, anti-selectin L, anti-selectin E, and anti-selectin P, toxic molecules such as cyclophosphamide, methrotrexate, Azathioprine, mizoribine, 15-deoxuspergualin, neomycin, staurosporine, genestein, herbimycin A, Pseudomonas exotoxin A, saporin, Rituxan, Ricin, gemtuzumab ozogamicin, Shiga toxin, heavy metals like inorganic and organic mercurials, and FN18-CRM9, radioisotopes such as incorporated isotopes of iodide, cobalt, selenium, tritium, and phosphor, and haptens such as DNP, and digoxiginin, and antibodies thereto, or antibody derivatives or fragments thereof, and combinations thereof.

187. Use of a MHC molecule in a histological method.

188. Use of a MHC molecule in a cytological method.

189. Use of a MHC molecule according to item 187 or 188 in a method for determining the presence of MHC recognising cells in a sample, in which method the MHC recognising cells of the sample are mounted on a support.

190. Use of a MHC molecule according to item 187 or 188, in a method for monitoring the presence of MHC recognising cells in a sample, in which method the MHC recognising cells of the sample are mounted on a support.

191. Use of a MHC molecule according to item 187 or 188 in a method for determining the status of a disease involving MHC recognising cells, in which method the MHC recognising cells of the sample are mounted on a support.

192. Use of a MHC molecule according to item 187 or 188 in a method for establishing a prognosis of a disease involving MHC recognising cells, in which method the MHC recognising cells of the sample are mounted on a support.

193. Use of a MHC molecule according to any one of items 187-192, wherein the support is a solid or semi-solid support.

194. Use of a MHC molecule according to any one of items 187-193, wherein the support is selected from glass slides, membranes, filters, polymer slides, chamber slides, dishes, and petridishes.

195. Use according to any one of items 187-194, wherein the sample is selected from histological material, cytological material, primary tumours, secondary organ metastasis, fine needle aspirates, spleen tissue, bone marrow specimens, cell smears, exfoliative cytological specimens, touch preparations, oral swabs, laryngeal swabs, vaginal swabs, bronchial lavage, gastric lavage, from the umbilical cord, and from body fluids such as blood (e.g. from a peripheral blood mononuclear cell (PBMC) population isolated from blood or from other blood-derived preparations such as leukopheresis products), from sputum samples, expectorates, and bronchial aspirates.

196. The use according to any one of items 187-195, wherein the MHC molecule is

a MHC Class I molecule selected from the group consisting of a heavy chain, a heavy chain combined with a □₂m, a heavy chain combined with a peptide, and a heavy chain/□₂m dimer with a peptide;

or a MHC Class II molecule selected from the group consisting of an α/□dimer, an α/□ dimer with a peptide, □/□ dimer combined through an affinity tag and a □/□ dimer combined through an affinity tag with a peptide;

or a MHC Class I like molecule or a MHC Class II like molecule.

197. The use according to any one of items 187-196, wherein the MHC molecule is a vertebrate MHC molecule such as a human, a murine, a rat, a porcine, a bovine or an avian molecule.

198. The use according to any one of items 187-197, wherein the MHC molecule is a human MHC molecule.

199. The use according to any one of items 187-198, wherein the MHC molecule is a peptide free MHC molecule.

200. The use according to any one of items 187-199, wherein the MHC molecule is attached to a binding entity.

201. Use according to item 200, wherein the binding entity has attached thereto from 1 to 10 MHC molecules, such as from 1 to 9, from 1 to 8, from 1 to 7, from 1 to 6, from 1 to 5, from 1 to 4, from 1 to 3, or 1 or 2 MHC molecules.

202. Use according to item 200, wherein the binding entity is selected from streptavidin streptavidin (SA) and avidin and derivatives thereof, biotin, immunoglobulins, antibodies (monoclonal, polyclonal, and recombinant), antibody fragments and derivatives thereof, leucine zipper domain of AP-1 (jun and fos), hexa-his (metal chelate moiety), hexa-hat GST (glutathione S-tranferase) glutathione affinity, Calmodulin-binding peptide (CBP), Strep-tag, Cellulose Binding Domain, Maltose Binding Protein, S-Peptide Tag, Chitin Binding Tag, Immuno-reactive Epitopes, Epitope Tags, E2Tag, HA Epitope Tag, Myc Epitope, FLAG Epitope, AU1 and AU5 Epitopes, Glu-Glu Epitope, KT3 Epitope, IRS Epitope, Btag Epitope, Protein Kinase-C Epitope, VSV Epitope, lectins that mediate binding to a diversity of compounds, including carbohydrates, lipids and proteins, e.g. Con A (Canavalia ensiformis) or WGA (wheat germ agglutinin) and tetranectin or Protein A or G (antibody affinity).

203. Use according to any one of items 187-202, wherein the MHC molecule further comprises a labelling compound.

204. Use according to item 203, wherein the labelling compound can be detected directly or indirectly.

205. Use according to item 203 or 204, wherein the labelling compound is a fluorescent label, an enzyme label, a radioisotope, a chemiluminescent label, a bioluminescent label, a polymer, a metal particle, a hapten, an antibody, or a dye.

206. Use according to any one of items 203-205, wherein the labelling compound is selected from

5-(and 6)-carboxyfluorescein, 5- or 6-carboxyfluorescein, 6-(fluorescein)-5-(and 6)-carboxamido hexanoic acid, fluorescein isothiocyanate (FITC), rhodamine, tetramethylrhodamine, and dyes such as Cy2, Cy3, and Cy5, optionally substituted coumarin including AMCA, PerCP, phycobiliproteins including R-phycoerythrin (RPE) and allophycoerythrin (APC), Texas Red, Princeston Red, Green fluorescent protein (GFP) and analogues thereof, and conjugates of R-phycoerythrin or allophycoerythrin and e.g. Cy5 or Texas Red, and inorganic fluorescent labels based on semiconductor nanocrystals (like quantum dot and Qdot™ nanocrystals), and time-resolved fluorescent labels based on lanthanides like Eu3+ and Sm3+, from haptens such as DNP, biotin, and digoxiginin, or is selected from enzymatic labels such as horse radish peroxidase (HRP), alkaline phosphatase (AP), beta-galactosidase (GAL), glucose-6-phosphate dehydrogenase, beta-N-acetyl-glucosaminidase, β-glucuronidase, invertase, Xanthine Oxidase, firefly luciferase and glucose oxidase (GO), or is selected from luminiscence labels such as luminol, isoluminol, acridinium esters, 1,2-dioxetanes and pyridopyridazines, or is selected from radioactivity labels such as incorporated isotopes of iodide, cobalt, selenium, tritium, and phosphor.

207. The use according to any one of items 203-206, wherein the labelling compound is attached to the MHC molecule and/or the binding entity.

208. A method for detecting the presence of MHC recognising cells in a sample comprising the steps of

(a) providing a sample suspected of comprising MHC recognising cells mounted on a support,

(b) contacting the sample with a MHC molecule as defined in items 187-207, and

(c) determining any binding of the MHC molecule, which binding indicates the presence of MHC recognising cells.

209. A method for monitoring MHC recognising cells comprising the steps of

(a) providing a sample suspected comprising MHC recognising cells mounted on a support,

(b) contacting the sample with a MHC molecule as defined in items 187-207, and

(c) determining any binding of the MHC molecule, thereby monitoring MHC recognising cells.

210. A method for the prognosis of a disease involving MHC recognising cells comprising the steps of

(a) providing a sample suspected comprising MHC recognising cells mounted on a support,

(b) contacting the sample with a MHC molecule as defined in items 187-207, and

(c) determining any binding of the MHC molecule, thereby establishing a prognosis of a disease involving MHC recognising cells.

211. A method for determining the status of a disease involving MHC recognising cells comprising the steps of

(a) providing a sample suspected comprising MHC recognising cells mounted on a support,

(b) contacting the sample with a MHC molecule as defined in items 187-207, and

(c) determining any binding of the MHC molecule, thereby determining the status of a disease involving MHC recognising cells.

212. A method for the diagnosis of a disease involving MHC recognising cells comprising the steps of

(a) providing a sample suspected comprising MHC recognising cells mounted on a support,

(b) contacting the sample with a MHC molecule as defined in items 187-207, and

(c) determining any binding of the MHC molecule, thereby diagnosing a disease involving MHC recognising cells.

213. A method for the effectiveness of a medicament against a disease involving MHC recognising cells comprising the steps of

(a) providing a sample from a subject receiving treatment with a medicament mounted on a support,

(b) contacting the sample with a MHC molecule as defined in items 187-207, and

(c) determining any binding of the MHC molecule, thereby determining the effectiveness of the medicament.

214. The method according to any one of items 208-213, wherein the MHC recognising cells are involved in a disease of inflammatory, auto-immune, allergic, viral, cancerous, infectious, allo- or xenogene (graft-versus-host and host-versus-graft) origin.

215. The method according to item 214, wherein the disease is a chronic inflammatory bowel disease such as Crohn's disease or ulcerative colitis, sclerosis, type I diabetes, rheumatoid arthritis, psoriasis, atopic dermatitis, asthma, malignant melanoma, renal carcinoma, breast cancer, lung cancer, cancer of the uterus, cervical cancer, prostatic cancer, brain cancer, head and neck cancer, leukaemia, cutaneous lymphoma, hepatic carcinoma, colorectal cancer, bladder cancer, rejection-related disease, Graft-versus-host-related disease, or a viral disease associated with hepatitis, AIDS, measles, pox, chicken pox, rubella or herpes.

216. The method according to any one of items 208-214, wherein the MHC recognising cells are selected from subpopulations of CD3+ T-cells, gamma,delta T-cells, alpha,beta T-cells, CD4+ T-cells, T helper cells, CD8+ T-cells, Suppressor T-cells, CD8+ cytotoxic T-cells, CTLs, NK cells, NKT cells, LAK cells, and MAK.

217. The method or use according to any one of items 201-216, wherein the sample is selected from histological material, cytological material, primary tumours, secondary organ metastasis, fine needle aspirates, spleen tissue, bone marrow specimens, cell smears, exfoliative cytological specimens, touch preparations, oral swabs, laryngeal swabs, vaginal swabs, bronchial lavage, gastric lavage, from the umbilical cord, and from body fluids such as blood (e.g. from a peripheral blood mononuclear cell (PBMC) population isolated from blood or from other blood-derived preparations such as R 

The invention claimed is:
 1. An isolated MHC multimer comprising (a-b-P)_(n), wherein n>1, wherein a and b together form a functional MHC protein which is bound to the peptide P, wherein (a-b-P) is the MHC peptide complex formed when the peptide P is bound to the functional MHC protein, wherein each MHC peptide complex of the MHC multimer is associated with one or more multimerization domains selected from the group consisting of scaffolds, carriers, optionally substituted organic molecules, membranes, liposomes or micelles, polymers, polysaccharides, dextran moieties, IgG domains, coiled-coil polypeptide structures, DNA duplexes, nucleic acid duplexes, PNA-PNA, PNA-DNA, DNA-RNA, avidins, streptavidins, antibodies, small organic molecules, proteins, a solid support, and biological polymers, with the proviso that the one or more multimerization domains is not a cell, wherein each MHC protein is an MHC class I molecule encoded by an HLA-A*02 allele, and wherein in at least one MHC peptide complex, the sequence of P originates from a Borrelia OspC antigen, is capable of binding said MHC class I molecule encoded by an HLA-A*02 allele, and is selected from the group consisting of SEQ ID NOS:49735, 49739, 49779, 49795, 49921, and
 49937. 2. The isolated MHC multimer according to claim 1, wherein n is in the range from 8 to
 25. 3. The isolated MHC multimer according to claim 1, wherein n>10.
 4. The isolated MHC multimer according to claim 1, wherein the MHC multimer comprises one or more covalently or non-covalently attached labels, and wherein said one or more labels can be selected from the group consisting of fluorescent labels, fluorophores, enzymes, radioisotopes, chemiluminescent labels, dyes, bioluminescent labels, metal particles, haptens, polymers, and antibodies.
 5. A composition comprising a plurality of MHC multimers according to claim 1 and a carrier, wherein the MHC multimers are identical.
 6. A composition comprising a plurality of MHC multimers according to claim 1 and a carrier, wherein the MHC multimers are different.
 7. A kit comprising a MHC multimer according to claim 1, a positive control, and/or instructions for use.
 8. The isolated MHC multimer according to claim 1, wherein the HLA*02 allele is selected from the group consisting of HLA-A*0201, HLA-A*0202, HLA-A*0203, HLA-A*0206, HLA-A*0211, HLA-A*0212, HLA-A*0216, HLA-A*0217, HLA-A*0219, and HLA-A*0250. 